|
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 ... |
874-1954 |
0e+00 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 1500.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 874 TRQDEVMQAKAVELQKVQEKHTKTQMDLKELENKYQQLSEEKTILAEQLQAETELFAEAEEMRARLAARKQELEDILHEL 953
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKEKQQKAESELKELEKKHQQLCEEKNILAEQLQAETELFAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 954 ESRVEEEEERCQQLQGDKKKMQQHVQDLEEQLEEEEAARQKLQLEKVSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEER 1033
Cdd:pfam01576 81 EARLEEEEERSQQLQNEKKKMQQHIQDLEEQLEEEEAARQKLQLEKVTTEAKIKKMEEDILLLEDQNNKLQKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1034 LSEFTSHMAEEEEKVKSLSKLRNKYEAVMADMEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALAR 1113
Cdd:pfam01576 161 ISEFTSNLAEEEEKSKSLNKLKNKHEAMISDLEDRLKKEEKGRQELEKAKRKLEGESSDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1114 KEAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQEDMESEKLARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQE 1193
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNAALKKLRELEAQLSELQEDLESERAARAKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1194 LRSKREQEVTELKKTIEEEVKVHEAQVLDMRQRHTSALEELSEQLEQSRRFKINLEKTKQALEGENAEMQKEVKLLQAAK 1273
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKASLEKAKQALESENAELQAELRSLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1274 LESEQRRKKLEGQVQELQLRAGEGERAKAELVERLVKLQNELDGVSGTLGSTESKTIKLAKDLATVESHLQDTQELLQEE 1353
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQSRLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1354 TRQKLNLSSRVRQLEEEKAAMLEQLEEEEAAKANFSRQMQSLQQQVMETKKKLEEDAGVAEAIEEARRRAAKDLESLSVR 1433
Cdd:pfam01576 481 TRQKLNLSSRLRQLEDEKNSLQEQLEEEEEAKRNVERQLQTLQAQLSDLKKKLEEDAGAVEALEEGRKRLQRELEALTQR 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1434 YEERVQACDKLEKGRTRLQQELDDVTVALDQQRQVVSALEKKQKKFDQMLAEEKLISARYAEERDRAEADAREKETKVLS 1513
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETKALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1514 LSRALEEALETREEMERQNKQLRAEMDDLVSSKDDVGKNVHELERFKRALEQQVQEMRAQMEELEDELQATEDGKLRLEV 1593
Cdd:pfam01576 641 LARALEEALDAKEELERQNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1594 NMQALKAQHERELQNRDDANDDKKKLLSKQVRELEAELDAERKQRAQALAGRKKLELDLQEAMAQLDAANKGRDEAGKQL 1673
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIEAANKGRDEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1674 RKLQAQMKELWREVEEARAAREEIFIQSRESEKKLKNLEAELLQLQEDLAASERAKRQAQQERDDLADELANGNSGKSAL 1753
Cdd:pfam01576 801 KKLQAQMKDLQRELDEARASRDEIFAQSKESEKKLKSLEAELLQLQEDLAAAERARRQAQQERDELAEEIASGNSGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1754 LDEKRHLEARIGQLEEELDEEQSNMELLNDRYRKLSMQVETLTTELGAERSFSQKTENARQQLERQNKDLRAKLGEMDSS 1833
Cdd:pfam01576 881 LDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKLTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1834 VKSKYKMAIATLESKVAQLEEQLEQESRERILSGKLVRRAEKKLKEVILQVDEERRNADQYKDQVEKGHLRLKQLKRQLE 1913
Cdd:pfam01576 961 VKSKYKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRNADQYKDQAEKGNSRLKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 1033370542 1914 EAEEEASRANASRRRMQRELEDVTESAESMNREVTSLRNRL 1954
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESAEAMNREVTTLRSKL 1081
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
93-797 |
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: 1421.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 172
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 173 ESGAGKTENTKKVIQYLAHVASSHKARKDHNIppeypteakQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 252
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNI---------PGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 253 FDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLSNGYLPIPGQQDKEIFHET 332
Cdd:cd14920 152 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQET 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 333 MESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGMNVTEFTRAILTPRIKVGRDYVQ 412
Cdd:cd14920 232 MEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 413 KAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 492
Cdd:cd14920 312 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 493 TMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKSFVEKVSQEQGTHPKFQKPRQL 572
Cdd:cd14920 392 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 573 RDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKDeiqniqkvyffdsyavapqgpveMDRIV 652
Cdd:cd14920 472 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKD-----------------------VDRIV 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 653 GLDQVSGMGDLAFGASYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLE 732
Cdd:cd14920 529 GLDQVTGMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLE 608
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033370542 733 GIRICRQGFPNRIIFQEFRQRYEILTPNAIPKGFMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd14920 609 GIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
93-797 |
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: 1320.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 172
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 173 ESGAGKTENTKKVIQYLAHVASSHKARKDHNIppeypteaKQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 252
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGK--------KKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 253 FDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPF-NQYRFLSNGYLPIPGQQDKEIFHE 331
Cdd:cd01377 153 FGSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDpSYYFFLSQGELTIDGVDDAEEFKL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 332 TMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGMNVTEFTRAILTPRIKVGRDYV 411
Cdd:cd01377 233 TDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 412 QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 491
Cdd:cd01377 313 TKGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 492 HTMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKSFVEKVSQEQGTHPK-FQKPR 570
Cdd:cd01377 392 HHMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 571 QLRDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKDEiqniqkvyffdsyavapqgpvemdr 650
Cdd:cd01377 470 PKKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDY------------------------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 651 ivgldqvsgMGDLAFGASYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGV 730
Cdd:cd01377 525 ---------EESGGGGGKKKKKGGSFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGV 595
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033370542 731 LEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKGFMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd01377 596 LEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
93-797 |
0e+00 |
|
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276895 [Multi-domain] Cd Length: 676 Bit Score: 1236.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 172
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 173 ESGAGKTENTKKVIQYLAHVASSHKARKDHNippeyPTEAKQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 252
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQS-----SIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 253 FDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLSNGYLPIPGQQDKEIFHET 332
Cdd:cd14932 156 FDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAET 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 333 MESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGMNVTEFTRAILTPRIKVGRDYVQ 412
Cdd:cd14932 236 MEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 413 KAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 492
Cdd:cd14932 316 KAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 493 TMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKSFVEKVSQEQGTHPKFQKPRQL 572
Cdd:cd14932 396 TMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 573 RDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKDeiqniqkvyffdsyavapqgpveMDRIV 652
Cdd:cd14932 476 KDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKD-----------------------VDRIV 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 653 GLDQVSGMGDLAFGAsYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLE 732
Cdd:cd14932 533 GLDKVAGMGESLHGA-FKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLE 611
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033370542 733 GIRICRQGFPNRIIFQEFRQRYEILTPNAIPKGFMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd14932 612 GIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
93-797 |
0e+00 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 1196.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 172
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 173 ESGAGKTENTKKVIQYLAHVASSHKARKDhnippeypteakQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 252
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKD------------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 253 FDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLSNGYLPIPGQQDKEIFHET 332
Cdd:cd14919 149 FDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQET 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 333 MESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGMNVTEFTRAILTPRIKVGRDYVQ 412
Cdd:cd14919 229 MEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 413 KAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 492
Cdd:cd14919 309 KAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNH 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 493 TMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKSFVEKVSQEQGTHPKFQKPRQL 572
Cdd:cd14919 389 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQL 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 573 RDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKDeiqniqkvyffdsyavapqgpveMDRIV 652
Cdd:cd14919 469 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKD-----------------------VDRII 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 653 GLDQVSGMGDLAFGASYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLE 732
Cdd:cd14919 526 GLDQVAGMSETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLE 605
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033370542 733 GIRICRQGFPNRIIFQEFRQRYEILTPNAIPKGFMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd14919 606 GIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
93-797 |
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: 1166.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 172
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 173 ESGAGKTENTKKVIQYLAHVASSHKARKDHNIPPEYPTEAKQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 252
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 253 FDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLSNGYLPIPGQQDKEIFHET 332
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 333 MESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGMNVTEFTRAILTPRIKVGRDYVQ 412
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 413 KAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 492
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 493 TMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKSFVEKVSQEQGTHPKFQKpRQL 572
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TDF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 573 RDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKDEiqniqkvyffdsyavapqgpvemdRIV 652
Cdd:cd14911 477 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDA------------------------EIV 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 653 GLDQvSGMGDLAFGAsyKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLE 732
Cdd:cd14911 533 GMAQ-QALTDTQFGA--RTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLE 609
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033370542 733 GIRICRQGFPNRIIFQEFRQRYEILTPNAIPKGFMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd14911 610 GIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
93-797 |
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: 1164.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 172
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 173 ESGAGKTENTKKVIQYLAHVASSHKARKDHNIppeypteakQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 252
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSI---------TGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 253 FDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLSNGYLPIPGQQDKEIFHET 332
Cdd:cd14921 152 FDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQET 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 333 MESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGMNVTEFTRAILTPRIKVGRDYVQ 412
Cdd:cd14921 232 LEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 413 KAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 492
Cdd:cd14921 312 KAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 493 TMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKSFVEKVSQEQGTHPKFQKPRQL 572
Cdd:cd14921 392 TMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 573 RDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKDeiqniqkvyffdsyavapqgpveMDRIV 652
Cdd:cd14921 472 KDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKD-----------------------VDRIV 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 653 GLDQVSGMGDLAFGASYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLE 732
Cdd:cd14921 529 GLDQMAKMTESSLPSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLE 608
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033370542 733 GIRICRQGFPNRIIFQEFRQRYEILTPNAIPKGFMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd14921 609 GIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
93-797 |
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: 1163.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 172
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 173 ESGAGKTENTKKVIQYLAHVASSHKARKDHNippeyPTEAKQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 252
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQN-----SLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 253 FDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLSNGYLPIPGQQDKEIFHET 332
Cdd:cd15896 156 FDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTET 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 333 MESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGMNVTEFTRAILTPRIKVGRDYVQ 412
Cdd:cd15896 236 MEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 413 KAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 492
Cdd:cd15896 316 KAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 493 TMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKSFVEKVSQEQGTHPKFQKPRQL 572
Cdd:cd15896 396 TMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 573 RDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKDeiqniqkvyffdsyavapqgpveMDRIV 652
Cdd:cd15896 476 KDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKD-----------------------VDRIV 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 653 GLDQVSGMGDLAfgASYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLE 732
Cdd:cd15896 533 GLDKVSGMSEMP--GAFKTRKGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLE 610
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033370542 733 GIRICRQGFPNRIIFQEFRQRYEILTPNAIPKGFMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd15896 611 GIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
93-797 |
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: 1159.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 172
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 173 ESGAGKTENTKKVIQYLAHVASSHKARKDHNIPpeypteakqGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 252
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP---------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 253 FDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLSNGYLPIPGQQdKEIFHET 332
Cdd:cd14930 152 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQET 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 333 MESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGMNVTEFTRAILTPRIKVGRDYVQ 412
Cdd:cd14930 231 LESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 413 KAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 492
Cdd:cd14930 311 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 493 TMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKSFVEKVSQEQGTHPKFQKPRQL 572
Cdd:cd14930 391 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 573 RDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKDeiqniqkvyffdsyavapqgpveMDRIV 652
Cdd:cd14930 471 RDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKD-----------------------VEGIV 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 653 GLDQVSGMGDLAFGAsyKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLE 732
Cdd:cd14930 528 GLEQVSSLGDGPPGG--RPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLE 605
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033370542 733 GIRICRQGFPNRIIFQEFRQRYEILTPNAIPKGFMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd14930 606 GIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
81-797 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 Cd Length: 674 Bit Score: 1102.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 81 VEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSML 160
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 161 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKArkdhnippeypteAKQGELERQLLQANPILEAFGNAKTVKND 240
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSA-------------GNVGRLEEQILQSNPILEAFGNAKTVRNN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 241 NSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLSN-GYLP 319
Cdd:pfam00063 148 NSSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQsGCYT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 320 IPGQQDKEIFHETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGMNVTEFTRAI 399
Cdd:pfam00063 228 IDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKAL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 400 LTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCI 479
Cdd:pfam00063 308 CKRRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 480 NYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKSFVEKVSQE 559
Cdd:pfam00063 388 NYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYST 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 560 QGTHPKFQKPRQlRDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKDEiqniqkvyffdsya 639
Cdd:pfam00063 465 FSKHPHFQKPRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDY-------------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 640 vapqgpvemdrivGLDQVSGMGDLAFGASYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPH 719
Cdd:pfam00063 530 -------------ETAESAAANESGKSTPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNS 596
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1033370542 720 LVLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKGFMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:pfam00063 597 LVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
74-809 |
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: 1015.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 74 NPPKFTKVEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISE 153
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 154 AAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKarkdhnippeypteaKQGELERQLLQANPILEAFGN 233
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNT---------------EVGSVEDQILESNPILEAFGN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 234 AKTVKNDNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFL 313
Cdd:smart00242 146 AKTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 314 SNG-YLPIPGQQDKEIFHETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASMPDNT-AAQKLCHLLGMN 391
Cdd:smart00242 226 NQGgCLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 392 VTEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDrTKRQGASFIGILDIAGFEIFQL 471
Cdd:smart00242 306 PEELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLS-FKDGSTYFIGVLDIYGFEIFEV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 472 NSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKS 551
Cdd:smart00242 385 NSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQT 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 552 FVEKVSQEQGTHPKFQKPRQlRDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKDEIQNiqk 631
Cdd:smart00242 462 FLEKLNQHHKKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSN--- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 632 vyffdsyavapqgpvemdrivgldqvsgmgdlafgasyKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEK 711
Cdd:smart00242 538 --------------------------------------AGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEK 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 712 RAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKGFMDGKQACERMIKALELDPNLFRIGQ 791
Cdd:smart00242 580 KPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGK 659
|
730
....*....|....*...
gi 1033370542 792 SKIFFRAGVLAHLEEERD 809
Cdd:smart00242 660 TKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
30-1182 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 914.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 30 VWVPSERHGFEAAGLREERGDEVMVELA---ENGRQVLVAKDDIQ--KMNPPKFTKVEDMAELTCLNEASVLHNLKDRYY 104
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEEgkkEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 105 SGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGESGAGKTENTKK 184
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 185 VIQYLAHVASSHKARKdhnippeypteakqGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGANI 264
Cdd:COG5022 172 IMQYLASVTSSSTVEI--------------SSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 265 ETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLSNGYLP-IPGQQDKEIFHETMESMRIMGFSH 343
Cdd:COG5022 238 ETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 344 EEIHCMLRMVSAVLQFGNIVFRKERNtDQASMPDNTAAQKLCHLLGMNVTEFTRAILTPRIKVGRDYVQKAQTKEQADFA 423
Cdd:COG5022 318 EEQDQIFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 424 VEALAKATYERLFRWLVHRINRALDRTKRQGaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQ 503
Cdd:COG5022 397 RDSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 504 REGIEWNFIDFgLDLQPCIDLIERpANPPGVLALLDEECWFPKATDKSFVEKVSQ--EQGTHPKFQKPRQLRDKadFCII 581
Cdd:COG5022 476 KEGIEWSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDNK--FVVK 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 582 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKDEiQNIQkvyffdsyavapqgpvemdrivgldqvsgmg 661
Cdd:COG5022 552 HYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDE-ENIE------------------------------- 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 662 dlafgasyktKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGF 741
Cdd:COG5022 600 ----------SKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGF 669
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 742 PNRIIFQEFRQRYEILTPNA----IPKGFMDGKQACERMIKALELDPNLFRIGQSKIFFRAGVLAHLEEERDLKITDIIV 817
Cdd:COG5022 670 PSRWTFDEFVQRYRILSPSKswtgEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIAT 749
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 818 SFQAAARGYLARKAFMKKQQQMSALKVMQRNCAAYLKLRHWQWWRLFTKVKPLLQVTRQDEVMQAKAVELQKVQekhtkt 897
Cdd:COG5022 750 RIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQ------ 823
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 898 qmdlKELENKYQQLSEEKTILAEQLQAETELFAEAEEMRARLAARKQELedILHELESRVEEEEERCQQLQGDKKKMQQh 977
Cdd:COG5022 824 ----KTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKET--IYLQSAQRVELAERQLQELKIDVKSISS- 896
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 978 vqdleeqleeeeAARQKLQLEKVSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEER-LSEFTSHMAEEEEKVKSLSKLRN 1056
Cdd:COG5022 897 ------------LKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIdLEEGPSIEYVKLPELNKLHEVES 964
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1057 KYEAVMADMEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQ------QQLEELRQALARKEAELQ------AALAR 1124
Cdd:COG5022 965 KLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGalqestKQLKELPVEVAELQSASKiissesTELSI 1044
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|....*...
gi 1033370542 1125 VEDEAAQKNAVLKSLRELQAQLAELQEDMESEKLARAKAEKQRRDLGEELEALKTELE 1182
Cdd:COG5022 1045 LKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLE 1102
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
93-797 |
0e+00 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 Cd Length: 633 Bit Score: 855.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRH-EMPPHIYAISEAAYRSMLQDREDQSILCT 171
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 172 GESGAGKTENTKKVIQYLAHVASSHKARKDHNippeypteakQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 251
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSS----------ASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIEL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 252 NFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFL-----SNGYLPIPGQQDK 326
Cdd:cd00124 151 QFDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDDA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 327 EIFHETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVF--RKERNTDQASMPDNTAAQKLCHLLGMNVTEFTRAILTPRI 404
Cdd:cd00124 231 EEFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFeeDEEDEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 405 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQ-GASFIGILDIAGFEIFQLNSFEQLCINYTN 483
Cdd:cd00124 311 KVGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYAN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 484 EKLQQLFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKSFVEKVSQEQGTH 563
Cdd:cd00124 391 EKLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSH 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 564 PKFQKPRQLRDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADkftaelwkdeiqniqkvyffdsyavapq 643
Cdd:cd00124 468 PRFFSKKRKAKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ---------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 644 gpvemdrivgldqvsgmgdlafgasyktkkgmfrtvgqlYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLD 723
Cdd:cd00124 519 ---------------------------------------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLE 559
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033370542 724 QLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKGFMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd00124 560 QLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
93-797 |
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: 775.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 172
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 173 ESGAGKTENTKKVIQYLAHVASSHKARKDhniPPEYPTEAKQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 252
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGK---KAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 253 FDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLL--EPFNqYRFLSNGYLPIPGQQDKEIFH 330
Cdd:cd14927 158 FGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVsmNPYD-YHFCSQGVTTVDNMDDGEELM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 331 ETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGMNVTEFTRAILTPRIKVGRDY 410
Cdd:cd14927 237 ATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 411 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 490
Cdd:cd14927 317 VTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 491 NHTMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKSFVEKVSQEQ-GTHPKFQKP 569
Cdd:cd14927 396 NHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 570 R---QLRDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELwkdeiqniqkvyfFDSYavapqgpv 646
Cdd:cd14927 473 RpdkKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATL-------------YENY-------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 647 emdriVGLDQVsgmGDLAFGASYKTKKGM-FRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQL 725
Cdd:cd14927 532 -----VGSDST---EDPKSGVKEKRKKAAsFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQL 603
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1033370542 726 RCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPK-GFMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd14927 604 RCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
94-797 |
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: 758.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 94 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 173
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 174 SGAGKTENTKKVIQYLAHVASSHKARKDHNippeyptEAKQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 253
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGDLAKKKD-------SKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 254 DVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLL--EPFNqYRFLSNGYLPIPGQQDKEIFHE 331
Cdd:cd14913 155 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLIttNPYD-YPFISQGEILVASIDDAEELLA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 332 TMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGMNVTEFTRAILTPRIKVGRDY 410
Cdd:cd14913 234 TDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 411 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 490
Cdd:cd14913 313 VTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 491 NHTMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKSFVEKV-SQEQGTHPKFQKP 569
Cdd:cd14913 392 NHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSNNFQKP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 570 RQLRDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELwkdeiqniqkvyfFDSYAVAPqgpve 647
Cdd:cd14913 469 KVVKGRAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHL-------------YATFATAD----- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 648 mdrivgldqvsgmGDLAFGASYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRC 727
Cdd:cd14913 531 -------------ADSGKKKVAKKKGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRC 597
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033370542 728 NGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKG-FMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
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 ... |
93-797 |
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: 743.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 172
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 173 ESGAGKTENTKKVIQYLAHVASSHKARKDhnippeyptEAKQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 252
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEA---------AKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 253 FDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLL-EPFNQYRFLSNGYLPIPGQQDKEIFHE 331
Cdd:cd14909 152 FGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFSL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 332 TMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGMNVTEFTRAILTPRIKVGRDYV 411
Cdd:cd14909 232 TDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 412 QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 491
Cdd:cd14909 312 TQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 492 HTMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKSFVEKVSQEQ-GTHPKFQKPR 570
Cdd:cd14909 391 HHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 571 QLR---DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKDEiqniqkvyffdsyavAPQgpve 647
Cdd:cd14909 468 PPKpgqQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADH---------------AGQ---- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 648 mdrivgldqvSGMGDLAFGASYKtKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRC 727
Cdd:cd14909 529 ----------SGGGEQAKGGRGK-KGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTC 597
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 728 NGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIpKGFMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
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 ... |
93-797 |
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: 722.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 172
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 173 ESGAGKTENTKKVIQYLAHVASSHKARKDhnippeypteaKQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 252
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSD-----------GKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 253 FDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPF-NQYRFLSNGYLPIPGQQDKEIFHE 331
Cdd:cd14934 150 FGTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNpKEYHWVSQGVTVVDNMDDGEELQI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 332 TMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGMNVTEFTRAILTPRIKVGRDYV 411
Cdd:cd14934 230 TDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 412 QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 491
Cdd:cd14934 310 QKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 492 HTMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKSFVEKVSQEQ-GTHPKFQKPR 570
Cdd:cd14934 389 HHMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 571 QLRDK---ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKDEIqniqkvyffdsyavapqgpve 647
Cdd:cd14934 466 GGKGKgpeAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEE--------------------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 648 mdrivgldqvsgmgdlAFGASYKTKKG-MFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLR 726
Cdd:cd14934 525 ----------------APAGSKKQKRGsSFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLA 588
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033370542 727 CNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKGFMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd14934 589 CNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
94-797 |
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: 710.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 94 SVLHNLKDRYYSG-LIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 172
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 173 ESGAGKTENTKKVIQYLAHVASShkARKDHNIppeypteakqgelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 252
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGS--SSGETQV-------------EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEIL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 253 FDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLSNG-YLPIPGQQDKEIFHE 331
Cdd:cd01380 147 FDKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGgSPVIDGVDDAAEFEE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 332 TMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGMNVTEFTRAILTPRIKVGRDYV 411
Cdd:cd01380 227 TRKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 412 QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQGA-SFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 490
Cdd:cd01380 307 VKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 491 NHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKSFVEKVSQEQGTHPK--FQK 568
Cdd:cd01380 387 NQHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 569 PRqlRDKADFCIIHYAGKVDYKADEWLMKNMDPLNdnvatllhqsadkftaelwkDEIQNIQKvyffdsyavapqgpvem 648
Cdd:cd01380 463 PR--FSNTAFIVKHFADDVEYQVEGFLEKNRDTVS--------------------EEHLNVLK----------------- 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 649 drivgldqvsgmgdlafgASYKTKKgmfrTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCN 728
Cdd:cd01380 504 ------------------ASKNRKK----TVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRAC 561
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1033370542 729 GVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKGfMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
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 ... |
93-797 |
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: 703.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 172
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 173 ESGAGKTENTKKVIQYLAHVASSHKARKdhnippeypteaKQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 252
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKK------------KLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 253 FDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLSNGYLPIPGQQDKEIFHET 332
Cdd:cd14929 149 FGARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 333 MESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGMNVTEFTRAILTPRIKVGRDYVQ 412
Cdd:cd14929 229 EQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 413 KAQTKEQADFAVEALAKATYERLFRWLVHRINRALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 492
Cdd:cd14929 309 RSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 493 TMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKSFVEKVSQEQ-GTHPKFQKPRQ 571
Cdd:cd14929 388 HMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 572 LRDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKDEIqniqkvyffdsyavapqgpvemd 649
Cdd:cd14929 465 DKKKfeAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYI----------------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 650 rivgldqvSGMGDLAFGASYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNG 729
Cdd:cd14929 522 --------STDSAIQFGEKKRKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNG 593
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1033370542 730 VLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKG-FMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd14929 594 VLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
94-797 |
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: 702.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 94 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 173
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 174 SGAGKTENTKKVIQYLAHVAS-SHKARKDHNippeypteAKQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 252
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAiGDRSKKDQT--------PGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 253 FDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLL--EPFNqYRFLSNGYLPIPGQQDKEIFH 330
Cdd:cd14917 154 FGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItnNPYD-YAFISQGETTVASIDDAEELM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 331 ETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGMNVTEFTRAILTPRIKVGRD 409
Cdd:cd14917 233 ATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 410 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 489
Cdd:cd14917 312 YVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 490 FNHTMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKSFVEKV-SQEQGTHPKFQK 568
Cdd:cd14917 391 FNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLfDNHLGKSNNFQK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 569 PRQLRDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELwkdeiqniqkvyfFDSYAVApQGPV 646
Cdd:cd14917 468 PRNIKGKpeAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNL-------------FANYAGA-DAPI 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 647 EmdrivgldqvSGMGdlafgasyKTKKG-MFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQL 725
Cdd:cd14917 534 E----------KGKG--------KAKKGsSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQL 595
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1033370542 726 RCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKG-FMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd14917 596 RCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
95-797 |
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: 685.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 95 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGES 174
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 175 GAGKTENTKKVIQYLAHVASSHKARKDHnippeypTEAKQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 254
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEE-------SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 255 VAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLL--EPFNqYRFLSNGYLPIPGQQDKEIFHET 332
Cdd:cd14918 156 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLIttNPYD-YAFVSQGEITVPSIDDQEELMAT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 333 MESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGMNVTEFTRAILTPRIKVGRDYV 411
Cdd:cd14918 235 DSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 412 QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 491
Cdd:cd14918 314 TKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 492 HTMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKSFVEKV-SQEQGTHPKFQKPR 570
Cdd:cd14918 393 HHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSANFQKPK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 571 QLRDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELwkdeiqniqkvyfFDSYAvapqgpvem 648
Cdd:cd14918 470 VVKGKAEahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASL-------------FSTYA--------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 649 drivgldqvSGMGDLAFGASYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCN 728
Cdd:cd14918 528 ---------SAEADSGAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCN 598
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 729 GVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKG-FMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd14918 599 GVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
94-797 |
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: 684.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 94 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 173
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 174 SGAGKTENTKKVIQYLAHVAS-SHKARKDHnippeypTEAKQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 252
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKEN-------PNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 253 FDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLL--EPFNqYRFLSNGYLPIPGQQDKEIFH 330
Cdd:cd14916 155 FGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtnNPYD-YAFVSQGEVSVASIDDSEELL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 331 ETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASmPDNTA-AQKLCHLLGMNVTEFTRAILTPRIKVGRD 409
Cdd:cd14916 234 ATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 410 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 489
Cdd:cd14916 313 YVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 490 FNHTMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKSFVEKVSQEQ-GTHPKFQK 568
Cdd:cd14916 392 FNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 569 PRQLRDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELwkdeiqniqkvyfFDSYAVApqgpv 646
Cdd:cd14916 469 PRNVKGKqeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATL-------------FSTYASA----- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 647 emdrivgldqvsGMGDLAFGASYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLR 726
Cdd:cd14916 531 ------------DTGDSGKGKGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLR 598
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1033370542 727 CNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKG-FMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd14916 599 CNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
94-797 |
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: 679.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 94 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 173
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 174 SGAGKTENTKKVIQYLAHVASSHKARKDhnippEYPTEAKQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 253
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKE-----EITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 254 DVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLL--EPFNqYRFLSNGYLPIPGQQDKEIFHE 331
Cdd:cd14912 157 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLIttNPYD-YPFVSQGEISVASIDDQEELMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 332 TMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGMNVTEFTRAILTPRIKVGRDY 410
Cdd:cd14912 236 TDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 411 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 490
Cdd:cd14912 315 VTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 491 NHTMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKSFVEKV-SQEQGTHPKFQKP 569
Cdd:cd14912 394 NHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyEQHLGKSANFQKP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 570 RQLRDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWkdeiqniqkvyffdSYAVAPQGpve 647
Cdd:cd14912 471 KVVKGKAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLF--------------SGAQTAEG--- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 648 mdrivgldQVSGMGDLAFGasyKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRC 727
Cdd:cd14912 534 --------ASAGGGAKKGG---KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRC 602
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033370542 728 NGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKG-FMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd14912 603 NGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
94-797 |
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: 677.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 94 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 173
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 174 SGAGKTENTKKVIQYLAHVASSHKARKDHNippeyPTEAkQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 253
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQQ-----PGKM-QGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 254 DVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLE--PFNqYRFLSNGYLPIPGQQDKEIFHE 331
Cdd:cd14923 156 GATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIStnPFD-FPFVSQGEVTVASIDDSEELLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 332 TMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGMNVTEFTRAILTPRIKVGRDY 410
Cdd:cd14923 235 TDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 411 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 490
Cdd:cd14923 314 VTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 491 NHTMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKSFVEKV-SQEQGTHPKFQKP 569
Cdd:cd14923 393 NHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSNNFQKP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 570 RQLRDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAelwkdeiqniqkvYFFDSYAVAPQGpve 647
Cdd:cd14923 470 KPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLS-------------FLFSNYAGAEAG--- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 648 mdrivgldqvSGMGDLAFGasyKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRC 727
Cdd:cd14923 534 ----------DSGGSKKGG---KKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRC 600
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033370542 728 NGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKG-FMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd14923 601 NGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
94-797 |
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: 676.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 94 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 173
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 174 SGAGKTENTKKVIQYLAHVASSHKARKDhnippEYPTEAKQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 253
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKE-----EATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 254 DVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLL--EPFNqYRFLSNGYLPIPGQQDKEIFHE 331
Cdd:cd14910 157 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLIttNPYD-YAFVSQGEITVPSIDDQEELMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 332 TMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGMNVTEFTRAILTPRIKVGRDY 410
Cdd:cd14910 236 TDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 411 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 490
Cdd:cd14910 315 VTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 491 NHTMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKSFVEKV-SQEQGTHPKFQKP 569
Cdd:cd14910 394 NHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyEQHLGKSNNFQKP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 570 RQLRDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWkdeiqniqkvyffdsyavapQGPVE 647
Cdd:cd14910 471 KPAKGKveAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLF--------------------SGAAA 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 648 MDRIVGLDQVSGmgdlafgasyKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRC 727
Cdd:cd14910 531 AEAEEGGGKKGG----------KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRC 600
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033370542 728 NGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKG-FMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd14910 601 NGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
94-797 |
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: 668.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 94 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 173
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 174 SGAGKTENTKKVIQYLAHVASSHKARKDhnippEYPTEAKQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 253
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKE-----EAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 254 DVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKgELLLEPFNQYRF--LSNGYLPIPGQQDKEIFHE 331
Cdd:cd14915 157 GATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELI-EMLLITTNPYDFafVSQGEITVPSIDDQEELMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 332 TMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGMNVTEFTRAILTPRIKVGRDY 410
Cdd:cd14915 236 TDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 411 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 490
Cdd:cd14915 315 VTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 491 NHTMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKSFVEKV-SQEQGTHPKFQKP 569
Cdd:cd14915 394 NHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyEQHLGKSNNFQKP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 570 RQLRDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAelwkdeiqniqkvYFFDSYAVApqgpve 647
Cdd:cd14915 471 KPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLA-------------FLFSGGQTA------ 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 648 mdrivgldQVSGMGDLAFGasyKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRC 727
Cdd:cd14915 532 --------EAEGGGGKKGG---KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRC 600
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033370542 728 NGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKG-FMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd14915 601 NGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
94-797 |
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: 645.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 94 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 173
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 174 SGAGKTENTKKVIQYLAHVASSHKarkdhnippeypteakqgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 253
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS------------------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 254 DVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGE--HMKGELLLEPFNQYRFLS-NGYLPIPGQQDKEIFH 330
Cdd:cd14883 144 DASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDFD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 331 ETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRK-ERNTDQASMPDNTAAQKLCHLLGMNVTEFTRAILTPRIKVGRD 409
Cdd:cd14883 224 HLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGN 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 410 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQGaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 489
Cdd:cd14883 304 VTEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKF 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 490 FNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKSFVEKVSQEQGTHPKFQKP 569
Cdd:cd14883 383 FNHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKP 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 570 RQLRDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKdeiqniqkvyffdsyavapqgPVEMD 649
Cdd:cd14883 460 DRRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFT---------------------YPDLL 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 650 RIVGLDQVSGmGDLAFGASYKTKKgmfrTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNG 729
Cdd:cd14883 519 ALTGLSISLG-GDTTSRGTSKGKP----TVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAG 593
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1033370542 730 VLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKGFMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd14883 594 MLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
94-797 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 641.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 94 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 173
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 174 SGAGKTENTKKVIQYLAHVASSHkarkdhnippeyptEAKQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 253
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGS--------------ESEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 254 DVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLE-PFNQYRFLSNGYLPIPGQQDKEIFHET 332
Cdd:cd01378 148 DFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQrPEQYYYYSKSGCFDVDGIDDAADFKEV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 333 MESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFrKERNTDQASMPDNTAAQKLCHLLGMNVTEFTRAILTPRIKVG---RD 409
Cdd:cd01378 228 LNAMKVIGFTEEEQDSIFRILAAILHLGNIQF-AEDEEGNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 410 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 489
Cdd:cd01378 307 VYEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 490 FnhTMFVL--EQEEYQREGIEWNFIDFgLDLQPCIDLIErpANPPGVLALLDEECWFP-KATDKSFVEKVSQEQGTHPKF 566
Cdd:cd01378 387 F--IELTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 567 QKP---RQLRDkADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWkdeiqniqkvyffdsyavaPQ 643
Cdd:cd01378 462 ECPsghFELRR-GEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLF-------------------PE 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 644 GPVEMDrivgldqvsgmgdlafgasyktkKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLD 723
Cdd:cd01378 522 GVDLDS-----------------------KKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLH 578
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033370542 724 QLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKGFMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd01378 579 QVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
94-797 |
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: 636.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 94 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRgkKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 173
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 174 SGAGKTENTKKVIQYLAHVASSHKArkdhnippeypteakqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 253
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG------------------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 254 DVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLS-NGYLPIPGQQDKEIFHET 332
Cdd:cd01383 142 DAAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNqSNCLTIDGVDDAKKFHEL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 333 MESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGMNVTEFTRAILTPRIKVGRDYVQ 412
Cdd:cd01383 222 KEALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 413 KAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 492
Cdd:cd01383 302 KKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 493 TMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKSFVEKVSQEQGTHPKFQKPrql 572
Cdd:cd01383 382 HLFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGE--- 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 573 RDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKDEIQNIQKVyffdsyavapqgpvemdriv 652
Cdd:cd01383 456 RGGA-FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFASKMLDASRKA-------------------- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 653 gldqvsgMGDLAFGASYKTKkgmfRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLE 732
Cdd:cd01383 515 -------LPLTKASGSDSQK----QSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLE 583
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033370542 733 GIRICRQGFPNRIIFQEFRQRYEILTPNAIpKGFMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd01383 584 VVRISRSGYPTRMTHQEFARRYGFLLPEDV-SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
93-797 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 612.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCT 171
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 172 GESGAGKTENTKKVIQYLAHVASshkarkdhnippeyPTEAKQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 251
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGG--------------RAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 252 NFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFL--SNGYlPIPGQQDKEIF 329
Cdd:cd01384 147 QFDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLnqSKCF-ELDGVDDAEEY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 330 HETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKL---CHLLGMNVTEFTRAiLTPRIKV 406
Cdd:cd01384 226 RATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDA-LCKRVIV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 407 GRD-YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQgASFIGILDIAGFEIFQLNSFEQLCINYTNEK 485
Cdd:cd01384 305 TPDgIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 486 LQQLFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKSFVEKVSQEQGTHPK 565
Cdd:cd01384 384 LQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKR 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 566 FQKPRqlRDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWkdeiqniqkvyffdsyavaPQGP 645
Cdd:cd01384 461 FSKPK--LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLF-------------------PPLP 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 646 VEmdrivgldqvsgmgdlafGASYKTKkgmFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQL 725
Cdd:cd01384 520 RE------------------GTSSSSK---FSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQL 578
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1033370542 726 RCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAiPKGFMDGKQACERMIKALELDPnlFRIGQSKIFFR 797
Cdd:cd01384 579 RCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
93-797 |
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: 603.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 172
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 173 ESGAGKTENTKKVIQYLAHVASSHKArkdhnippeypteakqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 252
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHSW------------------IEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 253 FDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLSNG-YLPIPGQQDKEIFHE 331
Cdd:cd01381 143 FNKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGnCLTCEGRDDAAEFAD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 332 TMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRK--ERNTDQASMPDNTAAQKLCHLLGMNVTEFTRAILTPRIKVGRD 409
Cdd:cd01381 223 IRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 410 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQGAS--FIGILDIAGFEIFQLNSFEQLCINYTNEKLQ 487
Cdd:cd01381 303 TVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 488 QLFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLI-ERPANppgVLALLDEECWFPKATDKSFVEKVSQEQGTHPKF 566
Cdd:cd01381 383 QFFVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNY 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 567 QKPRQLRDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELwkdeiqniqkvyfFDSyavapqgpv 646
Cdd:cd01381 459 LKPKSDLNTS-FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQL-------------FNE--------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 647 emdrivgldqvsgmgDLAFGASYKTKKgmfRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLR 726
Cdd:cd01381 516 ---------------DISMGSETRKKS---PTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLR 577
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033370542 727 CNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKGFMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd01381 578 YSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
93-797 |
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: 571.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCT 171
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 172 GESGAGKTENTKKVIQYLAHVASSHkarkdhnippeypteakQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 251
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSG-----------------AGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 252 NFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFnqyrflsngylpipgQQDKEIFHE 331
Cdd:cd01382 144 HFNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDPL---------------LDDVGDFIR 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 332 TMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNT-------DQASMPDNTAAQKlchLLGMNVTEF-----TRAI 399
Cdd:cd01382 209 MDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYAAE---LLGLDQDELrvsltTRVM 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 400 LTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKrqGASFIGILDIAGFEIFQLNSFEQLCI 479
Cdd:cd01382 286 QTTRGGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVNSFEQFCI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 480 NYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKSFVEKVSQE 559
Cdd:cd01382 364 NYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQK 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 560 QGTHPKFQKPRQ--------LRDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKDEIQNiqk 631
Cdd:cd01382 441 HKNHFRLSIPRKsklkihrnLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNN--- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 632 vyffdsyavapqgpvemdrivgldqvsgmgdlafGASYKTKKG--MFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNH 709
Cdd:cd01382 518 ----------------------------------NKDSKQKAGklSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNL 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 710 EKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKgfMDGKQACERMIKALELDPNLFRI 789
Cdd:cd01382 564 KMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKF 641
|
....*...
gi 1033370542 790 GQSKIFFR 797
Cdd:cd01382 642 GLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
93-797 |
0e+00 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 563.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 172
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 173 ESGAGKTENTKKVIQYLAHVASShkarkdhnippeypteakQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 252
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGS------------------TNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 253 FDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPfnQYRFLS-NGYLPIPGQQDKEIFHE 331
Cdd:cd14872 143 FDNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSA--AYGYLSlSGCIEVEGVDDVADFEE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 332 TMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCH---LLGMNVTEFTRAILTPRIKV-G 407
Cdd:cd14872 221 VVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLEEALTSRLMEIkG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 408 RDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQ 487
Cdd:cd14872 301 CDPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 488 QLFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKSFVEKVSQEQGTHPKFQ 567
Cdd:cd14872 381 QHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 568 KPRQLRDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKdeiqniqkvyffdsyavapqgPVE 647
Cdd:cd14872 458 YAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFP---------------------PSE 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 648 MDRivgldqvsgmgdlafgasyKTKKGmfrTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRC 727
Cdd:cd14872 517 GDQ-------------------KTSKV---TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRY 574
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033370542 728 NGVLEGIRICRQGFPNRIIFQEFRQRYEILtPNAIPKGFM-DGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd14872 575 AGVFEAVKIRKTGYPFRYSHERFLKRYRFL-VKTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
93-797 |
7.46e-178 |
|
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: 556.31 E-value: 7.46e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQ----DREDQS 167
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 168 ILCTGESGAGKTENTKKVIQYLAHVASSHKARKDHNIP-PEYPTEAKQGELERQLLQANPILEAFGNAKTVKNDNSSRFG 246
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEaASEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 247 KFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLSNGYLPIPGQQDK 326
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 327 EIFHETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASmpDNTAAQKLCH---LLGMNVTEFTRAILTPR 403
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQSLKLaaeLLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 404 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQgASFIGILDIAGFEIFQLNSFEQLCINYTN 483
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 484 EKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIE-RPANPPGVLALLDeECWFPKAT--DKSFVEKVSQEQ 560
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLHASF 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 561 GT-------------HPKFQKPRQLRDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSAdkftaelwkdeiQ 627
Cdd:cd14890 476 GRksgsggtrrgssqHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR------------R 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 628 NIQKVyffdsyavapqgpvemdrivgldqvsgmgdlafgasyktkkgmfrTVGQLYKESLSKLMSTLRNTNPNFVRCIIP 707
Cdd:cd14890 543 SIREV---------------------------------------------SVGAQFRTQLQELMAKISLTNPRYVRCIKP 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 708 NHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAipkgfMDGKQACERMIKALELDPNLF 787
Cdd:cd14890 578 NETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADW 652
|
730
....*....|
gi 1033370542 788 RIGQSKIFFR 797
Cdd:cd14890 653 QIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
93-797 |
8.06e-168 |
|
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: 528.94 E-value: 8.06e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 172
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 173 ESGAGKTENTKKVIQYLAHVASShkarkdhniPPEYPTEakqgelerQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 252
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQR---------RNNLVTE--------QILEATPLLEAFGNAKTVRNDNSSRFGKYLEVF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 253 FDvAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLSNG-YLPIPGQQDKEIFHE 331
Cdd:cd01387 144 FE-GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFRR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 332 TMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQ---ASMPDNTAAQKLCHLLGMNVTEFTRAILTPRIKVGR 408
Cdd:cd01387 223 LLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 409 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINrALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 488
Cdd:cd01387 303 ERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 489 LFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKSFVEKVSQEQGTHPKFQK 568
Cdd:cd01387 382 YFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 569 PRQlrDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKDEIQNIQKvyffdsyaVAPQGPvem 648
Cdd:cd01387 459 PRM--PLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDK--------APPRLG--- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 649 drivgldqvsgmgdlafGASYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCN 728
Cdd:cd01387 526 -----------------KGRFVTMKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYS 588
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 729 GVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKGfMDGKQACERMIKALELDP-NLFRIGQSKIFFR 797
Cdd:cd01387 589 GMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
93-797 |
1.25e-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: 522.80 E-value: 1.25e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCT 171
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 172 GESGAGKTENTKKVIQYLAHVASshkARKDHNIppeypteakqgeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 251
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG---GLNDSTI--------------KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 252 NFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLvgAGEHMKGELLLEPFNQYRFL-SNGYLPIPGQQDKEIFH 330
Cdd:cd14903 144 QFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLL--ASPDVEERLFLDSANECAYTgANKTIKIEGMSDRKHFA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 331 ETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASM--PDNTAAQKLCHLLGMNVTEFTRAILTPRIKVGR 408
Cdd:cd14903 222 RTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 409 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQgASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 488
Cdd:cd14903 302 DVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 489 LFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKSFVEKVSqeqGTHPKFQK 568
Cdd:cd14903 381 KFTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQD 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 569 ----PRQlrDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKdeiqniQKVYFFDSYAVAPQG 644
Cdd:cd14903 454 viefPRT--SRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFK------EKVESPAAASTSLAR 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 645 PvemdrivgldqvsgmgdlafGASYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQ 724
Cdd:cd14903 526 G--------------------ARRRRGGALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQ 585
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033370542 725 LRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAiPKGFMDGKQACERMIKALELD-PNLFRIGQSKIFFR 797
Cdd:cd14903 586 LRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
94-797 |
2.82e-165 |
|
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: 520.68 E-value: 2.82e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 94 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 173
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 174 SGAGKTENTKKVIQYLAHVAsshkarkdhnippeyptEAKQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 253
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLG-----------------KANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 254 DVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMK-GELLLEPFNQYRFLSNGYLPIPGQQDKEI---- 328
Cdd:cd01379 145 TSTGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKlAKYKLPENKPPRYLQNDGLTVQDIVNNSGnrek 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 329 FHETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFR---KERNTDQASM-PDNTAAQKLCHLLGMNVTEFTRAiLTPRI 404
Cdd:cd01379 225 FEEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRiSNPEALNNVAKLLGIEADELQEA-LTSHS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 405 KVGR-DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRAL--DRTKRQGASFIGILDIAGFEIFQLNSFEQLCINY 481
Cdd:cd01379 304 VVTRgETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 482 TNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCID-LIERPAnppGVLALLDEECWFPKATDKSFVEKVsqEQ 560
Cdd:cd01379 384 ANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKF--HN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 561 GTHPKFQKpRQLRDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAelwkdeiqniQKVyffdsyav 640
Cdd:cd01379 458 NIKSKYYW-RPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR----------QTV-------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 641 apqgpvemdrivgldqvsgmgdlafgASYktkkgmFRTvgqlykeSLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHL 720
Cdd:cd01379 519 --------------------------ATY------FRY-------SLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREK 559
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033370542 721 VLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKGFMDgKQACERMIKALELDPnlFRIGQSKIFFR 797
Cdd:cd01379 560 VLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
93-797 |
1.06e-164 |
|
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: 519.25 E-value: 1.06e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKK-RHEMPPHIYAISEAAYRSMLQDREDQSILCT 171
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 172 GESGAGKTENTKKVIQYLAHVASShkarkdhnippeypteaKQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 251
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPS-----------------DDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIEL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 252 NFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLSNGYLPIPGQQDKE---- 327
Cdd:cd14897 144 HFTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDSEeley 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 328 ---IFHETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGMNVTEFTRAILTPRI 404
Cdd:cd14897 224 yrqMFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVN 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 405 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRAL----DRTKRQGASFIGILDIAGFEIFQLNSFEQLCIN 480
Cdd:cd14897 304 TIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCIN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 481 YTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKSFVEKVSQEQ 560
Cdd:cd14897 384 LSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKYC 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 561 GTHPKFQKPrqLRDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELwkdeiqniqkvyfFDSYav 640
Cdd:cd14897 461 GESPRYVAS--PGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDL-------------FTSY-- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 641 apqgpvemdrivgldqvsgmgdlafgasyktkkgmfrtvgqlYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHL 720
Cdd:cd14897 524 ------------------------------------------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDEL 561
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033370542 721 VLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAiPKGFMDGKQACERMIKALELDPnlFRIGQSKIFFR 797
Cdd:cd14897 562 VRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
93-797 |
3.23e-164 |
|
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: 520.01 E-value: 3.23e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 172
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 173 ESGAGKTENTKKVIQYLahVASSHKArkdHNippeypteakqGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 252
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKG---YG-----------SGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 253 FDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLS-NGYLPIPGQQDKEIFHE 331
Cdd:cd01385 145 YRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNqSDCYTLEGEDEKYEFER 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 332 TMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKER-NTDQASMPDNTAAQKL-CHLLGMNVTEFTRAILTPRIKVGRD 409
Cdd:cd01385 225 LKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDIiSELLRVKEETLLEALTTKKTVTVGE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 410 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRAL----DRTKRQGASfIGILDIAGFEIFQLNSFEQLCINYTNEK 485
Cdd:cd01385 305 TLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEH 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 486 LQQLFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKSFVEKVSQEQGTHPK 565
Cdd:cd01385 384 LQYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKY 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 566 FQKPrQLRDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAEL----------WkdeiqNIQKVYFF 635
Cdd:cd01385 461 YEKP-QVMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELigidpvavfrW-----AVLRAFFR 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 636 DSYAVAPQGpveMDRIVGLDQVSGM----GDLAFGASYKTKKGMfrTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEK 711
Cdd:cd01385 534 AMAAFREAG---RRRAQRTAGHSLTlhdrTTKSLLHLHKKKKPP--SVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEK 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 712 RAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNaipkgfmdGKQACERMIKALE----LDPNLF 787
Cdd:cd01385 609 KPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPK--------GLISSKEDIKDFLeklnLDRDNY 680
|
730
....*....|
gi 1033370542 788 RIGQSKIFFR 797
Cdd:cd01385 681 QIGKTKVFLK 690
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
93-759 |
4.23e-163 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 516.17 E-value: 4.23e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRgKKRHEMPPHIYAISEAAYRSMLQDREDQSILCT 171
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 172 GESGAGKTENTKKVIQYLAHVASSHKARKDhnippeypteakqgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 251
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS--------------LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 252 NFD---------VAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLSNGYLP--- 319
Cdd:cd14888 146 QFSklkskrmsgDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADAKPisi 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 320 ---------------------IPGQQDKEIFHETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASMPDN 378
Cdd:cd14888 226 dmssfephlkfryltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 379 TAAQKL---CHLLGMNVTEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQGA 455
Cdd:cd14888 306 SCTDDLekvASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 456 SFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVL 535
Cdd:cd14888 386 LFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIF 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 536 ALLDEECWFPKATDKSFVEKVSQEQGTHPKFQKPRQlrDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSAD 615
Cdd:cd14888 463 CMLDEECFVPGGKDQGLCNKLCQKHKGHKRFDVVKT--DPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKN 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 616 KFTAELwkdeiqniqkvyfFDSYavapqgpvemdrivgldqvsgmgdLAFGASYKTKKGMFRTVGQLYKESLSKLMSTLR 695
Cdd:cd14888 541 PFISNL-------------FSAY------------------------LRRGTDGNTKKKKFVTVSSEFRNQLDVLMETID 583
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033370542 696 NTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTP 759
Cdd:cd14888 584 KTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
93-795 |
2.20e-161 |
|
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: 511.26 E-value: 2.20e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMY------RGKKRHEMPPHIYAISEAAYRSMLQDRE-- 164
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 165 --DQSILCTGESGAGKTENTKKVIQYLAHVaSSHKARKDHNippeypteAKQGELERQLLQANPILEAFGNAKTVKNDNS 242
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASV-SSATTHGQNA--------TERENVRDRVLESNPILEAFGNARTNRNNNS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 243 SRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFL--SNGYLPI 320
Cdd:cd14901 152 SRFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQCYDRR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 321 PGQQDKEIFHETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVF-RKERNTDQASMPDNTAAQKLCHLLGMNVTEFTRAI 399
Cdd:cd14901 232 DGVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 400 LTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQGAS-FIGILDIAGFEIFQLNSFEQLC 478
Cdd:cd14901 312 CTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLC 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 479 INYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFgldlqP----CIDLIErpANPPGVLALLDEECWFPKATDKSFVE 554
Cdd:cd14901 392 INFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLAN 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 555 KVSQEQGTHPKFQKPRQLRDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAElwkdeiqniqkvyf 634
Cdd:cd14901 465 KYYDLLAKHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS-------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 635 fdsyavapqgpvemdrivgldqvsgmgdlafgasyktkkgmfrTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAG 714
Cdd:cd14901 531 -------------------------------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPS 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 715 KLEPHLVLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKGFMDGKQACERM-----IKALELDPNLFRI 789
Cdd:cd14901 568 EFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMsqlqhSELNIEHLPPFQV 647
|
....*.
gi 1033370542 790 GQSKIF 795
Cdd:cd14901 648 GKTKVF 653
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
93-797 |
1.67e-158 |
|
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: 503.17 E-value: 1.67e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCT 171
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 172 GESGAGKTENTKKVIQYLAHVaSSHKArkdhnippEYPTEAKQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 251
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVI-SQQSL--------ELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 252 NFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLS-NGYLPIPGQQDKEIFH 330
Cdd:cd14873 152 NICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 331 ETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFrkeRNTDQASMPDNTAAQKLCHLLGMNVTEFTRAiLTPRIKVGR-D 409
Cdd:cd14873 232 EVITAMEVMQFSKEEVREVSRLLAGILHLGNIEF---ITAGGAQVSFKTALGRSAELLGLDPTQLTDA-LTQRSMFLRgE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 410 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRaldRTKRQGA-SFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 488
Cdd:cd14873 308 EILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINS---RIKGKEDfKSIGILDIFGFENFEVNHFEQFNINYANEKLQE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 489 LFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKSFVEKVSQEQGTHPKFQK 568
Cdd:cd14873 385 YFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVK 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 569 PRQLRDkaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKDeiqniqkvyffDSYAvapqgpvem 648
Cdd:cd14873 461 PRVAVN--NFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEH-----------VSSR--------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 649 drivgldqvsGMGDLAFGASYKTKKgmfrTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCN 728
Cdd:cd14873 519 ----------NNQDTLKCGSKHRRP----TVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYS 584
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1033370542 729 GVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKGFMDGKqaCERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd14873 585 GMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
93-797 |
3.67e-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: 502.37 E-value: 3.67e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEM---PPHIYAISEAAYRSMLQDR----ED 165
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 166 QSILCTGESGAGKTENTKKVIQYLAhVASshKARKDhniPPEYPTEAKQGE-LERQLLQANPILEAFGNAKTVKNDNSSR 244
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLA-TAS--KLAKG---ASTSKGAANAHEsIEECVLLSNLILEAFGNAKTIRNDNSSR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 245 FGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLSNG-YLPIPGQ 323
Cdd:cd14892 155 FGKYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGnCVEVDGV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 324 QDKEIFHETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFrkERNTDQ----ASMPDNTAAQKLCHLLGMNVTEFTRAI 399
Cdd:cd14892 235 DDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 400 LTPRIKVGRDYV-QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQ---------GASFIGILDIAGFEIF 469
Cdd:cd14892 313 VTQTTSTARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 470 QLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFP-KAT 548
Cdd:cd14892 393 PTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTT 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 549 DKSFVEKVSQEQ-GTHPKFQKPRQLRDkaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADkftaelwkdeiq 627
Cdd:cd14892 470 DKQLLTIYHQTHlDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 628 niqkvyffdsyavapqgpvemdrivgldqvsgmgdlafgasyktkkgmFRTvgqlykeSLSKLMSTLRNTNPNFVRCIIP 707
Cdd:cd14892 536 ------------------------------------------------FRT-------QLAELMEVLWSTTPSYIKCIKP 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 708 NHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPN-AIPKGFMDGKQACERMIKALE----- 781
Cdd:cd14892 561 NNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARKKCEEivara 640
|
730
....*....|....*.
gi 1033370542 782 LDPNLFRIGQSKIFFR 797
Cdd:cd14892 641 LERENFQLGRTKVFLR 656
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
93-760 |
1.07e-145 |
|
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: 468.36 E-value: 1.07e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRH--------EMPPHIYAISEAAYRSMLQDR 163
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 164 EDQSILCTGESGAGKTENTKKVIQYLAHVASSHKARKDHNIPPEY--PTEAKQGELERQLLQANPILEAFGNAKTVKNDN 241
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSSirATSKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 242 SSRFGKFIRINFD-VAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEP---FNQYRFLS-NG 316
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNqlsGDRYDYLKkSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 317 YLPIPGQQDKEIFHETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVF--RKERNTDQASMPDNTAAQKLCHLLGMNVTE 394
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFddSTLDDNSPCCVKNKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 395 FTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRAL-------DRTKRQGASFIGILDIAGFE 467
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 468 IFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIE--WNFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFP 545
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 546 KATDKSFVEKVSQEQGTHPKFQKPRQLRdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKDE 625
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKIN-KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 626 IQNIQkvyffdsyavapqgpvemdrivglDQVSgmgdlafgaSYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCI 705
Cdd:cd14907 557 DGSQQ------------------------QNQS---------KQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCI 603
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1033370542 706 IPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPN 760
Cdd:cd14907 604 KPNEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
95-797 |
1.51e-145 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 467.46 E-value: 1.51e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 95 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSML----QDREDQSILC 170
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 171 TGESGAGKTENTKKVIQYLAHVASSHKarkdhnippeypteakqgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 250
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELCRGNS------------------QLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 251 INFDvAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVG-AGEHMKGELLLEPfNQYRFLSNGYlpipGQQD---- 325
Cdd:cd14889 145 LRFR-NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGiSAEDRENYGLLDP-GKYRYLNNGA----GCKRevqy 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 326 -KEIFHETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFrkERNTDQASMPDNTAAQKL---CHLLGMNVTEFTRAiLT 401
Cdd:cd14889 219 wKKKYDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEALKVENDSNGWLkaaAGQFGVSEEDLLKT-LT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 402 PRIKVGR-DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQG--ASFIGILDIAGFEIFQLNSFEQLC 478
Cdd:cd14889 296 CTVTFTRgEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQAC 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 479 INYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIErpANPPGVLALLDEECWFPKATDKSFVEKVSQ 558
Cdd:cd14889 376 INLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLFL--NKPIGILSLLDEQSHFPQATDESFVDKLNI 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 559 EQGTHPKFQKPRqlRDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKdeiqniqkvyffdsy 638
Cdd:cd14889 453 HFKGNSYYGKSR--SKSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFT--------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 639 AVAPQGPVEMDRIVGLDQvsgmGDLAFGASYKtkkgmfRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEP 718
Cdd:cd14889 516 ATRSRTGTLMPRAKLPQA----GSDNFNSTRK------QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDS 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 719 HLVLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEIL--TPNaIPKgfmdGKQACERMIKALELDPnlFRIGQSKIFF 796
Cdd:cd14889 586 KYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFF 658
|
.
gi 1033370542 797 R 797
Cdd:cd14889 659 K 659
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
94-757 |
3.59e-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: 457.08 E-value: 3.59e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 94 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMY-----------RGKKRHEMPPHIYAISEAAYRSM-- 159
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 160 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHVAsshkarkDHNIPPEYPTEAKQGELERQLLQANPILEAFGNAKTV 237
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAG-------DNNLAASVSMGKSTSGIAAKVLQTNILLESFGNARTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 238 KNDNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEhmkgelllepfnqyrflsngy 317
Cdd:cd14900 155 RNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE--------------------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 318 lpipGQQDKEIFHETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTD-QASMPDNTAAQKL------CHLLGM 390
Cdd:cd14900 214 ----AARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLSV 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 391 NVTEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRAL---DRTKRQGAS-FIGILDIAGF 466
Cdd:cd14900 290 DATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFGF 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 467 EIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPK 546
Cdd:cd14900 370 EVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMPK 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 547 ATDKSFVEKVSQEQGTHPKFQKPRQLRDKADFCIIHYAGKVDYKADEWLMKNMDplndnvatLLHQSAdkftaelwkdei 626
Cdd:cd14900 447 GSDTTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQEA------------ 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 627 qniqkvyffdsyavapqgpvemdrivgLDqvsgmgdlafgasyktkkgMFRTVGQlYKESLSKLMSTLRNTNPNFVRCII 706
Cdd:cd14900 507 ---------------------------VD-------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLK 539
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1033370542 707 PNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEIL 757
Cdd:cd14900 540 PNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
93-797 |
1.58e-135 |
|
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276869 Cd Length: 653 Bit Score: 439.38 E-value: 1.58e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCT 171
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 172 GESGAGKTENTKKVIQYLAHVASshkARKDHNIPpeypteakqgelerQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 251
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA--------------KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 252 NFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFL--SNGYLPIPGQQDKEIF 329
Cdd:cd14904 144 QFDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKLF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 330 HETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFrKERNTDQASMPDNTAAQKLCHLLGMNVTEFTRAILTPRIKVGRD 409
Cdd:cd14904 224 ASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 410 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 489
Cdd:cd14904 303 SVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQK 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 490 FNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKSFVEKV---SQEQGTHPKF 566
Cdd:cd14904 383 FTTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 567 QKPRQLRDKadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAElwkdeiqniqkvyFFDSyavapqgpV 646
Cdd:cd14904 459 DFPKVKRTQ--FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTE-------------LFGS--------S 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 647 EMDRivgldqvsgmgDLAFGASYKTKKGMfRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLR 726
Cdd:cd14904 516 EAPS-----------ETKEGKSGKGTKAP-KSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLR 583
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1033370542 727 CNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKGfmDGKQACERMIKAL-ELDPNLFRIGQSKIFFR 797
Cdd:cd14904 584 SAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
93-797 |
1.97e-133 |
|
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: 432.93 E-value: 1.97e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRyySGLI----YTYSGLFCVVINPYKNLPiytEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDRE---D 165
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 166 QSILCTGESGAGKTENTKKVIQYLAHVASSHKARKDHNIPPEYPTEAKQG-ELERQLLQANPILEAFGNAKTVKNDNSSR 244
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKKRKLSVtSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 245 FGKFIRINFDVAGY-IVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLS-NGYLPIPG 322
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 323 QQDKEIFHETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRK----ERNTDQASMPDNTAAQKLCHLLGMNVTEFTRA 398
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEedtsEGEAEIASESDKEALATAAELLGVDEEALEKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 399 ILTPRIkVGRDYVQKAQ-TKEQADFAVEALAKATYERLFRWLVHRINRALDRtKRQGASFIGILDIAGFEIFQL-NSFEQ 476
Cdd:cd14891 316 ITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFETkNDFEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 477 LCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKSFVEKV 556
Cdd:cd14891 394 LLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIA--SKPNGILPLLDNEARNPNPSDAKLNETL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 557 SQEQGTHPKFQKPRQlRDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSAdKFtaelwkdeiqniqkvyff 635
Cdd:cd14891 471 HKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASSA-KF------------------ 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 636 dsyavapqgpvemdrivgLDQVSGmgdlafgasyktkkgmfrtvgqlykeslskLMSTLRNTNPNFVRCIIPNHEKRAGK 715
Cdd:cd14891 531 ------------------SDQMQE------------------------------LVDTLEATRCNFIRCIKPNAAMKVGV 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 716 LEPHLVLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKGFMDGKQA-CERMIKALELDPNLFRIGQSKI 794
Cdd:cd14891 563 FDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRV 642
|
...
gi 1033370542 795 FFR 797
Cdd:cd14891 643 FFR 645
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
93-783 |
7.06e-132 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 430.10 E-value: 7.06e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYR--GKKRHE-------MPPHIYAISEAAYRSMLQD- 162
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 163 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHkarkdhNIPPEYPTEAKQGELERQLLQANPILEAFGNAKTVKNDNS 242
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGE------EGAPNEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 243 SRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGE--HMKGELL------LEPFNQYRFLS 314
Cdd:cd14908 155 SRFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEeeHEKYEFHdgitggLQLPNEFHYTG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 315 NGYLPIPGQ-QDKEIFHETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNtDQASMPDNTAAQK----LCHLLG 389
Cdd:cd14908 235 QGGAPDLREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEE-DGAAEIAEEGNEKclarVAKLLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 390 MNVTEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRAL--DRTKRQGASfIGILDIAGFE 467
Cdd:cd14908 314 VDVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSS-VGVLDIFGFE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 468 IFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFP-K 546
Cdd:cd14908 393 CFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDECRLGiR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 547 ATDKSFVEKV--------SQEQGTHPKFQKPRQLRDKADFCIIHYAGKVDYKADEWLM-KNmdplndnvatllhqsadkf 617
Cdd:cd14908 470 GSDANYASRLyetylpekNQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKN------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 618 taelwKDEIQNIQKVYFfdsyavapqgpvemdrivgldqvsgmgdlafgasyktkkgmfrTVGQLYKESLSKLMSTLRNT 697
Cdd:cd14908 531 -----KDEIPLTADSLF-------------------------------------------ESGQQFKAQLHSLIEMIEDT 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 698 NPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPnAIPK----GFMDGKQAC 773
Cdd:cd14908 563 DPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlsWSMERLDPQ 641
|
730
....*....|
gi 1033370542 774 ERMIKALELD 783
Cdd:cd14908 642 KLCVKKMCKD 651
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
91-850 |
1.34e-131 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 434.07 E-value: 1.34e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 91 NEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHE-MPPHIYAISEAAYRSMLQDREDQSIL 169
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 170 CTGESGAGKTENTKKVIQYLAhvaSSHKARKDHNIppeypteakqgelERQLLQANPILEAFGNAKTVKNDNSSRFGKFI 249
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA---SSKSGNMDLKI-------------QNAIMAANPVLEAFGNAKTIRNNNSSRFGRFM 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 250 RINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLSNGYLPIPGQQDKEIF 329
Cdd:PTZ00014 252 QLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDF 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 330 HETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVF--RKERNTDQASM--PDNTAA-QKLCHLLGMNVTEFTRAILTPRI 404
Cdd:PTZ00014 332 EEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESLEVfNEACELLFLDYESLKKELTVKVT 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 405 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQGAsFIGILDIAGFEIFQLNSFEQLCINYTNE 484
Cdd:PTZ00014 412 YAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFINITNE 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 485 KLQQLFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKSFVEKVSQEQGTHP 564
Cdd:PTZ00014 491 MLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNP 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 565 KFqKPRQLRDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKDeiqniqkvyffdsyavapqg 644
Cdd:PTZ00014 568 KY-KPAKVDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEG-------------------- 626
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 645 pVEMDRivgldqvsgmGDLAfgasyktkKGMFrtVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQ 724
Cdd:PTZ00014 627 -VEVEK----------GKLA--------KGQL--IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQ 685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 725 LRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKGFMDGKQACERMIKALELDPNLFRIGQSKIFFR---AGVL 801
Cdd:PTZ00014 686 LHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKEL 765
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1033370542 802 AHLEEERDLKITDIIVSFQAAARGYLARKAFMKKqqqmsaLKVMQRNCA 850
Cdd:PTZ00014 766 TQIQREKLAAWEPLVSVLEALILKIKKKRKVRKN------IKSLVRIQA 808
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
93-797 |
2.58e-126 |
|
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: 413.02 E-value: 2.58e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 172
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 173 ESGAGKTENTKKVIQYLahvASSHKARKDHNIppeypteakqgeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 252
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL---SSLYQDQTEDRL--------------RQPEDVLPILESFGHAKTILNANASRFGQVLRLH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 253 FDvAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLSNG-YLPIPGQQDKEIFHE 331
Cdd:cd14896 144 LQ-HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGgACRLQGKEDAQDFEG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 332 TMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQ--ASMPDNTAAQKLCHLLGMNvTEFTRAILTPRIKV-GR 408
Cdd:cd14896 223 LLKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVP-PERLEGAVTHRVTEtPY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 409 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQGA-SFIGILDIAGFEIFQLNSFEQLCINYTNEKLQ 487
Cdd:cd14896 302 GRVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERLQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 488 QLFNHTMFVLEQEEYQREGIEWNFIDfGLDLQPCIDLIErpANPPGVLALLDEECWFPKATDKSFVEKVSQEQGTHPKFQ 567
Cdd:cd14896 382 LFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYA 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 568 KPRQlrDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKdEIQniqkvyffDSYAVAPQGPve 647
Cdd:cd14896 459 KPQL--PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQ-EAE--------PQYGLGQGKP-- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 648 mdrivgldqvsgmgdlafgasyktkkgmfrTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRC 727
Cdd:cd14896 526 ------------------------------TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQ 575
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 728 NGVLEGIRICRQGFPNRIIFQEFRQRYEILTpNAIPKGFMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd14896 576 AGILEAIGTRSEGFPVRVPFQAFLARFGALG-SERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
93-795 |
9.26e-125 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 408.61 E-value: 9.26e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRH-EMPPHIYAISEAAYRSMLQDREDQSILCT 171
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 172 GESGAGKTENTKKVIQYLAhvaSSHKARKDHNIppeypteakqgelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 251
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMDLRI-------------QTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 252 nfDVA--GYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLSNGYLPIPGQQDKEIF 329
Cdd:cd14876 145 --DVAseGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 330 HETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKErntDQASMPDntAA----------QKLCHLLGMNVTEFTRAI 399
Cdd:cd14876 223 EEVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGK---TEQGVDD--AAaisneslevfKEACSLLFLDPEALKREL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 400 LTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDrtKRQG-ASFIGILDIAGFEIFQLNSFEQLC 478
Cdd:cd14876 298 TVKVTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLF 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 479 INYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKSFVEKVSQ 558
Cdd:cd14876 376 INITNEMLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVS 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 559 EQGTHPKFqKPRQLRDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKDeiqniqkvyffdsy 638
Cdd:cd14876 453 KLKSNGKF-KPAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEG-------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 639 avapqgpVEMDRivgldqvsgmGDLAfgasyktkKGMFrtVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEP 718
Cdd:cd14876 518 -------VVVEK----------GKIA--------KGSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNS 570
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033370542 719 HLVLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKGFMDGKQACERMIKALELDPNLFRIGQSKIF 795
Cdd:cd14876 571 SKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
94-758 |
3.65e-124 |
|
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: 408.96 E-value: 3.65e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 94 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPiyteqivEMYRGKKRHE-------MPPHIYAISEAAYRSMLQ----- 161
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 162 --DREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKARKDhnippeypTEAKQGELERQLLQANPILEAFGNAKTVKN 239
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSS--------SKRRRAISGSELLSANPILESFGNARTLRN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 240 DNSSRFGKFIRINF-----DVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFN--QYRF 312
Cdd:cd14895 147 DNSSRFGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 313 LSNG--YLPIPGQQDKEIFHETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTD---------------QASM 375
Cdd:cd14895 227 ISGGqcYQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 376 PDNTAAQKL---CHLLGMNVTEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTK- 451
Cdd:cd14895 307 SSLTVQQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQf 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 452 ---------RQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGLDlQPCI 522
Cdd:cd14895 387 alnpnkaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCL 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 523 DLIErpANPPGVLALLDEECWFPKATDKSFVEKVSQEQGTHPKFQKPRqlRDKAD--FCIIHYAGKVDYKADEWLMKNMD 600
Cdd:cd14895 466 EMLE--QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEGFCEKNKD 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 601 PLNDNVATLLHQSADKFTAELWKdeiqniqkvyFFDSYAVAPQGPVEMDRIVGLDQVSGMGdlafgasyktkkgmfrtVG 680
Cdd:cd14895 542 QPNAELFSVLGKTSDAHLRELFE----------FFKASESAELSLGQPKLRRRSSVLSSVG-----------------IG 594
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1033370542 681 QLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILT 758
Cdd:cd14895 595 SQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
93-759 |
1.52e-123 |
|
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: 407.36 E-value: 1.52e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYR--------GKKRHEMPPHIYAISEAAYRSMLQ-D 162
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 163 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKARKDHNippeypteAKQGELERQLLQANPILEAFGNAKTVKNDNS 242
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEG--------SDAVEIGKRILQTNPILESFGNAQTIRNDNS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 243 SRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLL------EPFNQYrFLSNG 316
Cdd:cd14902 153 SRFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLqkggkyELLNSY-GPSFA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 317 YLPIPGQQDKEIFHETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKE-RNTDQASMPDNTAAQ--KLCHLLGMNVT 393
Cdd:cd14902 232 RKRAVADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAEnGQEDATAVTAASRFHlaKCAELMGVDVD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 394 EFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALD--------RTKRQGASFIGILDIAG 465
Cdd:cd14902 312 KLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 466 FEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLALLDEECWFP 545
Cdd:cd14902 392 FESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLDQECLMP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 546 KATDKSFVEKVSQEQGThpkfqkprqlrdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKDE 625
Cdd:cd14902 469 KGSNQALSTKFYRYHGG------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADE 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 626 IQNiqkvyffdsyavAPQGPVemdrivgldqvsgmgdlafGASYKTKKGMFRT--VGQLYKESLSKLMSTLRNTNPNFVR 703
Cdd:cd14902 537 NRD------------SPGADN-------------------GAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVR 585
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1033370542 704 CIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTP 759
Cdd:cd14902 586 CLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
93-797 |
3.80e-117 |
|
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: 388.21 E-value: 3.80e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 172
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 173 ESGAGKTENTKKVIQYLAHVASSHKARkdhnippeypteakqgeLERQLLQA-NPILEAFGNAKTVKNDNSSRFGKFIRI 251
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV-----------------LSVEKLNAaLTVLEAFGNVRTALNGNATRFSQLFSL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 252 NFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQyrflSNGYLPIPGQQDKEI--- 328
Cdd:cd01386 144 DFDQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAE----SNSFGIVPLQKPEDKqka 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 329 ---FHETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGMNVTEFTRAI------ 399
Cdd:cd01386 220 aaaFSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhls 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 400 ------LTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQGASfIGILDIAGfeiFQLN- 472
Cdd:cd01386 300 ggpqqsTTSSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSS-ITIVDTPG---FQNPa 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 473 --------SFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERP---ANPP--------- 532
Cdd:cd01386 376 hsgsqrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdlrdedrr 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 533 GVLALLDEECWFPKATDKSFVEKVSQEQGTHPKFQKPRQLRDKA---DFCIIHYAGK--VDYKADEWLMK-NMDPLNDNV 606
Cdd:cd01386 456 GLLWLLDEEALYPGSSDDTFLERLFSHYGDKEGGKGHSLLRRSEgplQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNA 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 607 ATLLHQSADKFTAelwkdeiqniqkvyffdsyavapqgpvemdrivgldqvsgmgdlafgasyKTKKGMFRTVgqlyKES 686
Cdd:cd01386 536 TQLLQESQKETAA--------------------------------------------------VKRKSPCLQI----KFQ 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 687 LSKLMSTLRNTNPNFVRCIIPNHEkrAGKLEPH--------------LVLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQ 752
Cdd:cd01386 562 VDALIDTLRRTGLHFVHCLLPQHN--AGKDERStsspaagdelldvpLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRR 639
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1033370542 753 RYEILTPNAIPKGF-----MDGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd01386 640 RFQVLAPPLTKKLGlnsevADERKAVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
93-760 |
3.85e-117 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 388.95 E-value: 3.85e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKR-HEMPPHIYAISEAAYRSMLQDREDQSILC 170
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 171 TGESGAGKTENTKKVIQYLAHVASSHKARKDHNippeyptEAKQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 250
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQNNNN-------NNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 251 INFDVAGYIV-GANIETYLLEKSR-AIRQAKDERTFHIFYQLLVGAGEHMKGELLLEP-FNQYRFL-------------- 313
Cdd:cd14906 154 IEFRSSDGKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvissfksqs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 314 SNGYLPIPGQQDK-EIFHETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQAS--MPDNTAA-QKLCHLLG 389
Cdd:cd14906 234 SNKNSNHNNKTESiESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 390 MNVTEFTRAILTPRIKV-GRDYVQ-KAQTKEQADFAVEALAKATYERLFRWLVHRINRALDR----------TKRQGASF 457
Cdd:cd14906 314 YIESVFKQALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 458 IGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLAL 537
Cdd:cd14906 394 IGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 538 LDEECWFPKATDKSFVEKVSQEQGTHPKFQKpRQLrDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADkf 617
Cdd:cd14906 471 LDDECIMPKGSEQSLLEKYNKQYHNTNQYYQ-RTL-AKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSN-- 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 618 taelwkdeiqNIQKVYFFDSYAVAPqgpvemdrivgldqvsgmgdlafgaSYKTKKGMFRTVGQLYKESLSKLMSTLRNT 697
Cdd:cd14906 547 ----------FLKKSLFQQQITSTT-------------------------NTTKKQTQSNTVSGQFLEQLNQLIQTINST 591
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1033370542 698 NPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPN 760
Cdd:cd14906 592 SVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
93-759 |
5.57e-114 |
|
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: 378.04 E-value: 5.57e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKR-HEMPPHIYAISEAAYRSMLQDRE--DQSI 168
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 169 LCTGESGAGKTENTKKVIQYLAHVASShkarkdhnipPEYPTEAKQGE-LERQLLQANPILEAFGNAKTVKNDNSSRFGK 247
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAAS----------PTSWESHKIAErIEQRILNSNPVMEAFGNACTLRNNNSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 248 FIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLSNGYLPIpgqqDKE 327
Cdd:cd14880 151 FIQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNL----EED 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 328 IFHETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASMPDNTA---AQKLCHLLGMNVTEFTRAILTPRI 404
Cdd:cd14880 227 CFEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQIRTI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 405 KVGRDYV--QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYT 482
Cdd:cd14880 307 RAGKQQQvfKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 483 NEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKSFVEKVSQEQGT 562
Cdd:cd14880 387 NEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTRIESALA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 563 HPKFQKPRQLRDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKDEIQNIQKVYffdsyavap 642
Cdd:cd14880 464 GNPCLGHNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEE--------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 643 qgPVEMDRIVGLDQVSGmgdlafgasyktkkgmfrtvgqlYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVL 722
Cdd:cd14880 535 --PSGQSRAPVLTVVSK-----------------------FKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVL 589
|
650 660 670
....*....|....*....|....*....|....*..
gi 1033370542 723 DQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTP 759
Cdd:cd14880 590 SQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLRR 626
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
93-797 |
2.94e-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: 361.13 E-value: 2.94e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRH-----EMPPHIYAISEAAYRSMLQDREDQ 166
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 167 SILCTGESGAGKTENTKKVIQYLAHVASShkarkdhnippeypteaKQGELERQLLQANPILEAFGNAKTVKNDNSSRFG 246
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHST-----------------SSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 247 KFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLSNGY-LPIPGQQD 325
Cdd:cd14886 144 KFIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKcYDAPGIDD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 326 KEIFHETMESMRIMgFSHEEIHCMLRMVSAVLQFGNIVFRKERN--TDQASMPDNTAA-QKLCHLLGMNVTEFTRAILTP 402
Cdd:cd14886 224 QKEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIITK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 403 RIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRAL---DRTKRqgasFIGILDIAGFEIFQLNSFEQLCI 479
Cdd:cd14886 303 VVVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfdADARP----WIGILDIYGFEFFERNTYEQLLI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 480 NYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLALLDEECWFPKATDKSFVekvsqe 559
Cdd:cd14886 379 NYANERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFT------ 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 560 QGTHPKFQKPRQLRDKA---DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKDeiqniqkvyffd 636
Cdd:cd14886 450 SSCKSKIKNNSFIPGKGsqcNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSD------------ 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 637 syaVAPQGPvemdrivgldqvsgmgdlafgasykTKKGMFrtVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKL 716
Cdd:cd14886 518 ---IPNEDG-------------------------NMKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKY 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 717 EPHLVLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILT--PNAIPKGFMDGKQACERMIKALELDPNLFRIGQSKI 794
Cdd:cd14886 568 ETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKV 647
|
...
gi 1033370542 795 FFR 797
Cdd:cd14886 648 FLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
93-754 |
2.64e-106 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 357.87 E-value: 2.64e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMY----------RGKKRHEMPPHIYAISEAAYRSMLQ 161
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 162 DREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKARKDHNIPPEYPTEAKQGELERQLLQANPILEAFGNAKTVKNDN 241
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 242 SSRFGKFIRINF-DVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVG-----AGEHMKGELLLEPFNQYRFLSN 315
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 316 GYLPI--PGQQDKEIFHETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVF-----RKERN--TDQASMPDNTAA----- 381
Cdd:cd14899 241 SLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTvfADEARVMSSTTGafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 382 QKLCHLLGMNVTEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRT----------- 450
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 451 ---KRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIER 527
Cdd:cd14899 401 vddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 528 paNPPGVLALLDEECWFPKATDKSFVEKVSQE---QGTHPKFQKPRQLRDKADFCIIHYAGKVDYKADEWLMKNMDPLND 604
Cdd:cd14899 480 --RPIGIFSLTDQECVFPQGTDRALVAKYYLEfekKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 605 NVATLLHQSADKFTAELWKdeiqniqkvyffDSYAVAPQGPVEMDRIVGLDQVSGMGDLAfgasyktkkgmFRTVGQLYK 684
Cdd:cd14899 558 SAAQLLAGSSNPLIQALAA------------GSNDEDANGDSELDGFGGRTRRRAKSAIA-----------AVSVGTQFK 614
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 685 ESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRY 754
Cdd:cd14899 615 IQLNELLSTVRATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
93-797 |
8.83e-106 |
|
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: 354.50 E-value: 8.83e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYS-GLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRG-KKRHEMPPHIYAISEAAYRSM-LQDREDQSIL 169
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 170 CTGESGAGKTENTKKVIQYL---AHVASSHKARKdhnippeypTEAKQgeLERQLLQANPILEAFGNAKTVKNDNSSRFG 246
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLgqlSYMHSSNTSQR---------SIADK--IDENLKWSNPVMESFGNARTVRNDNSSRFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 247 KFIRINFD-VAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGEL-LLEPFNQYRFLSNGYL----PI 320
Cdd:cd14875 150 KYIKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTfvrrGV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 321 PGQ--QDKEIFHETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNtDQASMPDNTAAQKLCHLLGMNVTEFTRA 398
Cdd:cd14875 230 DGKtlDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLREC 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 399 ILtprIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALD-RTKRQGASFIGILDIAGFEIFQLNSFEQL 477
Cdd:cd14875 309 FL---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 478 CINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKSFVEKVS 557
Cdd:cd14875 386 CINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLW 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 558 QE-QGTHPKFQKPRQLRDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWkdeiqniqkvyffd 636
Cdd:cd14875 463 DQwANKSPYFVLPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLL-------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 637 syavaPQGPVEMDRIvgldqvsgmgdlafgasyktkkgmfRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKL 716
Cdd:cd14875 528 -----STEKGLARRK-------------------------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFL 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 717 EPHLVLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKGFMDGK--QACERMIKALE-----LDPNlFRI 789
Cdd:cd14875 578 DNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTASLFKQEKysEAAKDFLAYYQrlygwAKPN-YAV 656
|
....*...
gi 1033370542 790 GQSKIFFR 797
Cdd:cd14875 657 GKTKVFLR 664
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
94-761 |
3.39e-95 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 320.69 E-value: 3.39e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 94 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNlpIYTEQIVEMYRGKKRHeMPPHIYAISEAAYRSMLQdREDQSILCTGE 173
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 174 SGAGKTENTKKVIQYLAHVASSHKArkdhnippeypteakqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 253
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTTS------------------IEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 254 DvaGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGElllepFNQYRF-LSNGYLPIPGQQDKEIFHET 332
Cdd:cd14898 140 D--GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKND-----FIDTSStAGNKESIVQLSEKYKMTCSA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 333 MESMRIMGFSHEEiHCMLrmvsAVLQFGNIVFRKERNTDQASmpdNTAAQKLCHLLGMNVTEFTRAILTPRIKVGRDYVQ 412
Cdd:cd14898 213 MKSLGIANFKSIE-DCLL----GILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 413 KAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTkrqGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 492
Cdd:cd14898 285 VFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIK 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 493 TMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKSFVEKVSqeqgthpKFQKPRqL 572
Cdd:cd14898 362 KMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKIK-------KYLNGF-I 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 573 RDKADFCII--HYAGKVDYKADEWLMKNMDplndnvatllhqsadkftaelwkdeiqniqkvyffdsyavapQGPVemdr 650
Cdd:cd14898 430 NTKARDKIKvsHYAGDVEYDLRDFLDKNRE------------------------------------------KGQL---- 463
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 651 ivgldqvsgmgdLAFGASYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGV 730
Cdd:cd14898 464 ------------LIFKNLLINDEGSKEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGI 531
|
650 660 670
....*....|....*....|....*....|.
gi 1033370542 731 LEGIRICRQGFPNRIIFQEFRQRYEILTPNA 761
Cdd:cd14898 532 LETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
93-797 |
6.83e-95 |
|
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: 324.68 E-value: 6.83e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYS--------GLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDRE 164
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 165 DQSILCTGESGAGKTENTKKVIQYLAHVASSHKArkdhnippeypteAKQGELERQLLQANPILEAFGNAKTVKNDNSSR 244
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHG-------------ADSQGLEARLLQSGPVLEAFGNAHTVLNANSSR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 245 FGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLvgAGEHMKGELLLEPFNQYRFLSngylpipgqq 324
Cdd:cd14887 148 FGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALC--NAAVAAATQKSSAGEGDPEST---------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 325 DKEIFHETMESMRIMGFSHEEIHcmlRMVSAVLQFGNIVFRKERNTDQASMPDNTA--------AQKLCHLL-------G 389
Cdd:cd14887 216 DLRRITAAMKTVGIGGGEQADIF---KLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSevkclssG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 390 MNVTEFTRAILT--------PRIKVGRDYV------------QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDR 449
Cdd:cd14887 293 LKVTEASRKHLKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 450 TKR-------------QGASFIGILDIAGFEIFQ---LNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFI- 512
Cdd:cd14887 373 SAKpsesdsdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDc 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 513 -DFGLDLQPCIDLIERPAN---------------------PPGVLALLDE------ECWFPKATDKSFVEKVSQEQGTHP 564
Cdd:cd14887 453 sAFPFSFPLASTLTSSPSStspfsptpsfrsssafatspsLPSSLSSLSSslssspPVWEGRDNSDLFYEKLNKNIINSA 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 565 KFQK--PRQLRDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLhQSADKFTaelwkdeiqniqkvyffdsyavap 642
Cdd:cd14887 533 KYKNitPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYT------------------------ 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 643 qgpvemdRIVGLDQVSGMGdlafgaSYKTKKgmfRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVL 722
Cdd:cd14887 588 -------RLVGSKKNSGVR------AISSRR---STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVH 651
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033370542 723 DQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIpKGFMDGKQACERMIKALELDPNLFRIGQSKIFFR 797
Cdd:cd14887 652 RQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
93-797 |
1.49e-89 |
|
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: 306.56 E-value: 1.49e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQivemYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 172
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 173 ESGAGKTENTKKVIQ-YLAHVasshkaRKDHnippeypteakqgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 251
Cdd:cd14937 77 ESGSGKTEASKLVIKyYLSGV------KEDN-------------EISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 252 NFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLSNGYLPIPGQQDKEIFHE 331
Cdd:cd14937 138 ELDEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 332 TMESMRIMGFSHEEIHCMLRMvSAVLQFGNIVFR---KERNTDQASMPDNT--AAQKLCHLLGMNVTEFTRAILTPRIKV 406
Cdd:cd14937 218 LMISFDKMNMHDMKDDLFLTL-SGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 407 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKrQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKL 486
Cdd:cd14937 297 ANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 487 QQLFNHTMFVLEQEEYQREGIEWNFIDFGLDlQPCIDLIErpaNPPGVLALLDEECWFPKATDKSFVEKVSQEQGTHPKF 566
Cdd:cd14937 376 HSIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLR---GKTSIISILEDSCLGPVKNDESIVSVYTNKFSKHEKY 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 567 QKPRQLRDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKDeiqniqkvyffdsyavapqgpV 646
Cdd:cd14937 452 ASTKKDINK-NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYED---------------------V 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 647 EMDRIVGLDQVsgmgdlafgASYKtkkgmfrtvgqlYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLR 726
Cdd:cd14937 510 EVSESLGRKNL---------ITFK------------YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLF 568
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033370542 727 CNGVLEGIRIcRQGFPNRIIFQEFRQRYEILTPNAIPKGFMDGKQACERMIKAlELDPNLFRIGQSKIFFR 797
Cdd:cd14937 569 SLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
93-797 |
1.06e-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: 304.43 E-value: 1.06e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYR---GKKRHEMPPHIYAISEAAYRSMLQDREDQSIL 169
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 170 CTGESGAGKTENTKKVIQYLAHVASSHKArkdhnippeypteakqgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFI 249
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRT-----------------TFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 250 RINF-DVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLSNGylpIPGQ----- 323
Cdd:cd14878 144 ELQFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQT---MREDvstae 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 324 --QDKEIFHETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGMNVTEFTRAILT 401
Cdd:cd14878 221 rsLNREKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 402 PRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRAL---DRTKRQGASFIGILDIAGFEIFQLNSFEQLC 478
Cdd:cd14878 301 DIQYFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLC 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 479 INYTNEKLQQLFNHTMFVLEQEEYQREGIewnfidfgldlqpCIDLIERPAN-----------PPGVLALLDEECWFPKA 547
Cdd:cd14878 381 VNMTNEKMHHYINEVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLLDEESQMIWS 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 548 TDKSFVEKVS---QEQGTHPKFQKPRQ------LRDK-ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSadkf 617
Cdd:cd14878 448 VEPNLPKKLQsllESSNTNAVYSPMKDgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTS---- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 618 taelwkdeiQNIQKVYFFDSYAVapqgpvemdrivgldqvsgmgdlafgasyktkkgmfrTVGQLYKESLSKLMSTLRNT 697
Cdd:cd14878 524 ---------ENVVINHLFQSKLV-------------------------------------TIASQLRKSLADIIGKLQKC 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 698 NPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAI-PKGFMDGKQACERM 776
Cdd:cd14878 558 TPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLgEKKKQSAEERCRLV 637
|
730 740
....*....|....*....|.
gi 1033370542 777 IKALELDPnlFRIGQSKIFFR 797
Cdd:cd14878 638 LQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
90-796 |
1.12e-85 |
|
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: 295.23 E-value: 1.12e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 90 LNEASVLHNLKDRYYSGLIYTY---SGLfcVVINPYKNLPIYTEQIVEMYR-------GKKRHEMPPHIYAISEAAYRSM 159
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 160 LQDREDQSILCTGESGAGKTENTKKVIQYLAHVaSSHKarkdhnippeyPTEAKQGElerQLLQANPILEAFGNAKTVKN 239
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRL-SSHS-----------KKGTKLSS---QISAAEFVLDSFGNAKTLTN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 240 DNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFL--SNGY 317
Cdd:cd14879 144 PNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasYGCH 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 318 -LP-IPGQQDKEIFHETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFR--KERNTDQASMpDNTAA-QKLCHLLGMNV 392
Cdd:cd14879 224 pLPlGPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTydHEGGEESAVV-KNTDVlDIVAAFLGVSP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 393 TEFtRAILTPRIK-VGRD----YVQKAQTKEQADfaveALAKATYERLFRWLVHRINRALDRTKRQGASFIGILDIAGFE 467
Cdd:cd14879 303 EDL-ETSLTYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 468 ifQL-----NSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPanPPGVLALLDEEC 542
Cdd:cd14879 378 --NRsstggNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLRGK--PGGLLGILDDQT 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 543 -WFPKATDKSFVEKVSQEQGTHPKF---QKPRQLRDKADFCIIHYAGKVDYKADEWLMKNMDPLndnvatllhqSADkft 618
Cdd:cd14879 453 rRMPKKTDEQMLEALRKRFGNHSSFiavGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVL----------SPD--- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 619 aelwkdeiqniqkvyffdsyavapqgpvemdrIVGLdqvsgmgdlafgasyktkkgmFRTVGQLyKESLSKLMSTLRNTN 698
Cdd:cd14879 520 --------------------------------FVNL---------------------LRGATQL-NAALSELLDTLDRTR 545
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 699 PNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPnaipkgFMDGKQACERMIK 778
Cdd:cd14879 546 LWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARA 619
|
730
....*....|....*...
gi 1033370542 779 ALELDPNLFRIGQSKIFF 796
Cdd:cd14879 620 NGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
93-749 |
8.29e-78 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 273.32 E-value: 8.29e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHE-------MPPHIYAISEAAYRSMLQDRE 164
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 165 DQSILCTGESGAGKTENTKKVIQYLAHVAsshkarkdhnippeypTEAKQGELERQLLQANPILEAFGNAKTVKNDNSSR 244
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQ----------------TDSQMTERIDKLIYINNILESMSNATTIKNNNSSR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 245 FGKFIRINFD---------VAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVG-AGEHMKGELLLEPFNQYRFLS 314
Cdd:cd14884 145 CGRINLLIFEeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 315 N----------GYLPIPG----------QQDKEIFHETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRkerntdqas 374
Cdd:cd14884 225 PdeshqkrsvkGTLRLGSdsldpseeekAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK--------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 375 mpdntaaqKLCHLLGMNVTEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQG 454
Cdd:cd14884 296 --------AAAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKD 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 455 A-----------SFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCID 523
Cdd:cd14884 368 EsdnediysineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLI 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 524 LIERpanppgVLALLDE-----ECWFPKATDKSFV-----EKVSQEQGTH------PKFQK---PRQLRDKADFCIIHYA 584
Cdd:cd14884 447 FIAK------IFRRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVsygfvlNHDADgtaKKQNIKKNIFFIRHYA 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 585 GKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAElwkdeiqniqkvyffdsyavapqgpvemdrivgldqvsgmgdla 664
Cdd:cd14884 521 GLVTYRINNWIDKNSDKIETSIETLISCSSNRFLRE-------------------------------------------- 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 665 fgASYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNR 744
Cdd:cd14884 557 --ANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHK 634
|
....*
gi 1033370542 745 IIFQE 749
Cdd:cd14884 635 IPKKE 639
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
94-797 |
2.63e-75 |
|
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: 265.80 E-value: 2.63e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 94 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYrgKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 172
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 173 ESGAGKTENTKKVIQYLAhvaSSHKARKDHnippeypteakqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 252
Cdd:cd14905 80 ESGSGKSENTKIIIQYLL---TTDLSRSKY--------------LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 253 FDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLSN-GYLPIPGQQDKEIFHE 331
Cdd:cd14905 143 YSLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVFDR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 332 TMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNtdQASMPDNTAAQKLCHLLGMNVTEFTRAILTPRIKVGRDYV 411
Cdd:cd14905 223 LKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 412 QKAqtkeqadfavEALAKATYERLFRWLVHRINRALDRTkrQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 491
Cdd:cd14905 301 ENR----------DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYL 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 492 HTMFVLEQEEYQREGIEW-NFIDFGlDLQPCIDLIERpanppgVLALLDEECWFPKATDKSFVEKVSQEQGTHPKF-QKP 569
Cdd:cd14905 369 QTVLKQEQREYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgKKP 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 570 RQlrdkadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTaeLWKDEIQNIQKVY-----FFDSYAVAPQG 644
Cdd:cd14905 442 NK------FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYL--FSRDGVFNINATVaelnqMFDAKNTAKKS 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 645 PVEMDRIV------GLDQVSGMGDLAFGASYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPN--FVRCIIPNHEKRAGKL 716
Cdd:cd14905 514 PLSIVKVLlscgsnNPNNVNNPNNNSGGGGGGGNSGGGSGSGGSTYTTYSSTNKAINNSNCDfhFIRCIKPNSKKTHLTF 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 717 EPHLVLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAipKGFMD-GKQACERMIKALELDPNLFRIGQSKIF 795
Cdd:cd14905 594 DVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQNQ--RNFQNlFEKLKENDINIDSILPPPIQVGNTKIF 671
|
..
gi 1033370542 796 FR 797
Cdd:cd14905 672 LR 673
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
94-784 |
2.11e-72 |
|
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: 256.19 E-value: 2.11e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 94 SVLHNLKDRYYSGLIYTYSGLFCVVINPYknlpiyteqiveMYRGKKRH-------EMPPHIYAISEAAYRSMLQDREDQ 166
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTltstrssPLAPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 167 SILCTGESGAGKTENTKKVIQYLAHVASSHkarkdhnipPEypTEAKqgeleRQLLQANPILEAFGNAKTVKNDNSSRFG 246
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAGGG---------PE--TDAF-----KHLAAAFTVLRSLGSAKTATNSESSRIG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 247 KFIRINFdVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFN--QYRFLSNGYLPIPGQQ 324
Cdd:cd14881 134 HFIEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 325 DKEIFHETMESMRIMGFSHEEIhcmLRMVSAVLQFGNIVFrKERNTDQASMPDNTAAQKLCHLLGMNVTEFTRAiLTPRI 404
Cdd:cd14881 213 DAARFQAWKACLGILGIPFLDV---VRVLAAVLLLGNVQF-IDGGGLEVDVKGETELKSVAALLGVSGAALFRG-LTTRT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 405 K-VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRaldrTKRQGAS--------FIGILDIAGFEIFQLNSFE 475
Cdd:cd14881 288 HnARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMFGFEDPKPSQLE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 476 QLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNF-IDFgLDLQPCIDLIErpANPPGVLALLDEECwFPKATDKSFVE 554
Cdd:cd14881 364 HLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVA 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 555 KVSQEQGTHPKFQKPRQLRDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQsadkftaelwkdeiQNIQkvyf 634
Cdd:cd14881 440 KIKVQHRQNPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYK--------------QNCN---- 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 635 fdsyavapqgpvemdrivgldqvsgmgdlaFGasyktkkgmFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAG 714
Cdd:cd14881 501 ------------------------------FG---------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPN 541
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1033370542 715 KLEPHLVLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAIPKGFMDGKQACERMIK--ALELDP 784
Cdd:cd14881 542 HFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALILqfLEAQPP 613
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
93-762 |
6.33e-66 |
|
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: 236.69 E-value: 6.33e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 93 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYrgkkrhemppHIYAISEAAYRSMLQDRED-QSILCT 171
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 172 GESGAGKTENTKKVIQYLAhvasshkarkdhnippeypTEAKQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 251
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT-------------------SQPKSKVTTKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 252 NFDvAGYIVGANIE-TYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLSNGYLPIPGQQDKEIFH 330
Cdd:cd14874 132 LYK-RNVLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 331 ETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKERNTD---QASMPDNTAAQK-LCHLLGMNVTEFTrAILTPRIKV 406
Cdd:cd14874 211 HLEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNPNveqDVVEIGNMSEVKwVAFLLEVDFDQLV-NFLLPKSED 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 407 GrdyvqKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKRQGAsfIGILDIAGFEIFQLNSFEQLCINYTNEKL 486
Cdd:cd14874 290 G-----TTIDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 487 QQLFNHTMFVLEQEEYQREGIEWNF-IDFGLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKSFVEKVSQEQGTHPK 565
Cdd:cd14874 363 ENLFVKHSFHDQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 566 FQKPRQlRDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKDEIQNIQkvyffdsyavapqgp 645
Cdd:cd14874 441 YGKARN-KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTS--------------- 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 646 vemDRIVgldqvsgmgdlafgasyktkkgmfrTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQL 725
Cdd:cd14874 505 ---DMIV-------------------------SQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQI 556
|
650 660 670
....*....|....*....|....*....|....*..
gi 1033370542 726 RCNGVLEGIRICRQGFPNRIIFQEFRQRYEILTPNAI 762
Cdd:cd14874 557 KNLLLAELLSFRIKGYPVKISKTTFARQYRCLLPGDI 593
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
115-258 |
5.78e-62 |
|
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: 209.51 E-value: 5.78e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 115 FCVVINPYKNLPIYTEQIV-EMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 193
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033370542 194 SSHKARKDHNIpPEYPTEaKQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 258
Cdd:cd01363 81 FNGINKGETEG-WVYLTE-ITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
96-796 |
1.91e-61 |
|
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: 226.01 E-value: 1.91e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 96 LHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYT----------EQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDRED 165
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTpdhmqaynksREQTPLYEKDTVNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 166 QSILCTGESGAGKTENTKKVIQYLAHVASSHKARKDhnippeypTEAKQGELE---RQLLQANPILEAFGNAKTVKNDNS 242
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPD--------SEGASGVLHpigQQILHAFTILEAFGNAATRQNRNS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 243 SRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAgEH---MKGELLL-EPFNQYRFLSNGYl 318
Cdd:cd14893 156 SRFAKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGV-QHdptLRDSLEMnKCVNEFVMLKQAD- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 319 PIPGQ--QDKEIFHETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVF-------------RKERNTDQASMPDNTAAQK 383
Cdd:cd14893 234 PLATNfaLDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggksvggaNSTTVSDAQSCALKDPAQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 384 L--CHLLGMNVTEFTRAILTPRI--KVGRDYVQ--KAQTKEQADFAVEALAKATYERLFRWLVHRINRAL----DRTKRQ 453
Cdd:cd14893 314 LlaAKLLEVEPVVLDNYFRTRQFfsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 454 G----ASFIGILDIAGFEIF--QLNSFEQLCINYTNEKLQQLF-NHTMFV----LEQEEYQREG--IEWNFIDFGLDLQP 520
Cdd:cd14893 394 NivinSQGVHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 521 CIDLIERPanPPGVLALLDEECWFPKATDKSFVEK---VSQEQG-----------THPKFQKPRQLRdkADFCIIHYAGK 586
Cdd:cd14893 474 CLQLFEDK--PFGIFDLLTENCKVRLPNDEDFVNKlfsGNEAVGglsrpnmgadtTNEYLAPSKDWR--LLFIVQHHCGK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 587 VDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELWKDEIQNIQkvyffdSYAVAPQgpVEMDRivgldQVSGMGDLAFG 666
Cdd:cd14893 550 VTYNGKGLSSKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAAS------SEKAAKQ--TEERG-----STSSKFRKSAS 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 667 ASYKTKKGMFRTVGQLYKESlSKLMSTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRII 746
Cdd:cd14893 617 SARESKNITDSAATDVYNQA-DALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLT 695
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1033370542 747 FQEFRQRYeiltpnaipKGFMDGKQACERMIKALE----LDPNLFRIGQSKIFF 796
Cdd:cd14893 696 YGHFFRRY---------KNVCGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
94-757 |
1.85e-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: 220.77 E-value: 1.85e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 94 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 173
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 174 SGAGKTENTKKVIQYLAhvasshkarkdhnippeYPTEAKQGELERqLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 253
Cdd:cd14882 82 SYSGKTTNARLLIKHLC-----------------YLGDGNRGATGR-VESSIKAILALVNAGTPLNADSTRCILQYQLTF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 254 DVAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVG--AGEHMKgELLLEPFNQYRflsngYLPIPG--------- 322
Cdd:cd14882 144 GSTGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYR-----YLRIPPevppsklky 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 323 -----QQDKEIFHETMESMRIMGFSHEEIHCMLRMVSAVLQFGNIVFRKerNTDQASMPDNTAAQKLCHLLGMNVTEFTR 397
Cdd:cd14882 218 rrddpEGNVERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMW 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 398 AILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKrqgASF-----IGILDIAGFEIFQLN 472
Cdd:cd14882 296 ALTNYCLIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFGFECFHRN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 473 SFEQLCINYTNEKLQQLFNHTMFV---LEQEEYQREGIEWNFIDFGLDLQPCIdlierpANPPGVLALLDEECwfPKATD 549
Cdd:cd14882 373 RLEQLMVNTLNEQMQYHYNQRIFIsemLEMEEEDIPTINLRFYDNKTAVDQLM------TKPDGLFYIIDDAS--RSCQD 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 550 KSFV-EKVSQEQGTHPKfqkprqLRDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADkftaelwkdeiqN 628
Cdd:cd14882 445 QNYImDRIKEKHSQFVK------KHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLD------------E 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 629 IQKVYFFDSyavapqgpvemdrivgldQVSGMgdlafgasyKTKKGMFRTVgqlykeSLSKLMSTLRNTNP---NFVRCI 705
Cdd:cd14882 507 SVKLMFTNS------------------QVRNM---------RTLAATFRAT------SLELLKMLSIGANSggtHFVRCI 553
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1033370542 706 IPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEIL 757
Cdd:cd14882 554 RSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFL 605
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
94-795 |
1.07e-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: 217.40 E-value: 1.07e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 94 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYR-GKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 172
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 173 ESGAGKTENTKKVIQYLAHVA---SSHKARKDHNIPPEYPTEAK---QGELERQLLQANPILEAFGNAKTVKNDNSSRFG 246
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVkgsRRLPTNLNDQEEDNIHNEENtdyQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 247 KFIRINFDvAGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLVGAGEHMKGELLLEPFNQYRFLSNGYLPIPGQQDK 326
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 327 EIFHETMESMRIMGFSHEEIHCMLRMVSAVLQFGNI----VFRKE----------------------RNTDQASMPDNTA 380
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkAFRKKsllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 381 AQKL-CHLLGMNVTEFTRAILTPRIkVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRTKR--QGASF 457
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 458 IGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANppGVLAL 537
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 538 LDEECWFPKATDKS-FVEKVSQEQGTHPKF-QKPRQLRDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSAD 615
Cdd:cd14938 478 LLENVSTKTIFDKSnLHSSIIRKFSRNSKYiKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 616 KFtaelwkdeIQNIQKVYFFDSYAvapqGPVEMDRIVGLDQVSGMgdlaFGASYKTKKGMFRTvgqLYKESLSKLMSTLR 695
Cdd:cd14938 558 EY--------MRQFCMFYNYDNSG----NIVEEKRRYSIQSALKL----FKRRYDTKNQMAVS---LLRNNLTELEKLQE 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 696 NTNPNFVRCIIPNHEKRA-GKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIIFQEFRQRYEIltPNAipkgfmDGKQACE 774
Cdd:cd14938 619 TTFCHFIVCMKPNESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDI--KNE------DLKEKVE 690
|
730 740
....*....|....*....|.
gi 1033370542 775 RMIKALELDPNLFRIGQSKIF 795
Cdd:cd14938 691 ALIKSYQISNYEWMIGNNMIF 711
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
896-1713 |
4.71e-36 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 150.25 E-value: 4.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 896 KTQMDLKELENKYQQLSEEKTILAEQLQAETELFAEAEEMRaRLAARKQELEDILheLESRVEEEEERCQQLQGDKKKMQ 975
Cdd:COG1196 176 EAERKLERTEENLERLEDLLEELEKQLEKLERQAEKAERYQ-ELKAELRELELAL--LLAKLKELRKELEELEEELSRLE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 976 QHVQDLEEQLEEEEAARQKLQLEKVSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEERLSEFTSHMAEEEEKVKSLsklr 1055
Cdd:COG1196 253 EELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEEL---- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1056 nkyeavmadmEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQAALARVEDEAAQKNAv 1135
Cdd:COG1196 329 ----------KEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRN- 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1136 lkSLRELQAQLAELQEDMESEKLARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVTELKKTIEEEVKV 1215
Cdd:COG1196 398 --ELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1216 hEAQVLDMRQRHTSALEELSEQLEQSRRFKINLEKTKQALEG------ENAEMQKEVKL---------LQAAKLESEQ-- 1278
Cdd:COG1196 476 -LQRLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLPGvygpvaELIKVKEKYETaleaalgnrLQAVVVENEEva 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1279 ------RRKKLEGQV--------QELQLRAGEGERAKAELVERLVKLQNELDGVSGTLGSTE--SKTIKLAKDLA----- 1337
Cdd:COG1196 555 kkaiefLKENKAGRAtflpldriKPLRSLKSDAAPGFLGLASDLIDFDPKYEPAVRFVLGDTlvVDDLEQARRLArklri 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1338 -----TVESHLQDTQELLQEETRQK---LNLSSRVRQLEEEKAAMLEQLEEEEAAKANFSRQMQSLQQQVMETKKKLEEd 1409
Cdd:COG1196 635 kyrivTLDGDLVEPSGSITGGSRNKrssLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEE- 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1410 agvaeaIEEARRRAAKDLESLSVRYEERVQACDKLEKGRTRLQQELDDVTVALDQQRQVVSALEKKQKKFDQMLAEEKLI 1489
Cdd:COG1196 714 ------LERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEK 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1490 SARYAEERDRAEADAREKETKVLSLSRALEEALETREEMERQNKQLRAEMDDLVSSKDDVGKNVHELERFKRALEQQVQE 1569
Cdd:COG1196 788 RQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEE 867
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1570 MRAQMEELEDELQATEDGKLRLEVNMQALKAQHERELQNRDDANDDKKKLLSKQVR-ELEAELDAERKQRAQALAGRKKL 1648
Cdd:COG1196 868 LEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERlEVELPELEEELEEEYEDTLETEL 947
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033370542 1649 ELDLQEAMAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEARAAREEI--FIQSRESEKKLKNLEA 1713
Cdd:COG1196 948 EREIERLEEEIEALGPVNLRAIEEYEEVEERYEELKSQREDLEEAKEKLleVIEELDKEKRERFKET 1014
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
1044-1891 |
6.79e-36 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 149.48 E-value: 6.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1044 EEEKVKSLSKLR------NKYEAVMADMEDRLKKEEKGRQELEKLKrKLDGEAGDLQEQVA-----ELQQQLEELRQALA 1112
Cdd:COG1196 171 KERKEEAERKLErteenlERLEDLLEELEKQLEKLERQAEKAERYQ-ELKAELRELELALLlaklkELRKELEELEEELS 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1113 RKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQEDMESEKLARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQ 1192
Cdd:COG1196 250 RLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1193 ELRSKREQEVTELKKTIEEEvkvheaqvldmrqrhTSALEELSEQLEQSRRfkiNLEKTKQALEGENAEMQKEVKLLQAA 1272
Cdd:COG1196 330 EKIEALKEELEERETLLEEL---------------EQLLAELEEAKEELEE---KLSALLEELEELFEALREELAELEAE 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1273 KLESEQRRKKLEGQVQELQLRAGEGERAKAELVERLVKLQNELDGVSGTLGSTESKTIKLAKDLATVESHLQDTQELLQE 1352
Cdd:COG1196 392 LAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1353 ETRQKLNLSSRVRQLEEEKAAMLEQLEEEEAAKAnfsrQMQSLQQQVMETKKKLEE----DAGVAEAIEEArrrAAKDLE 1428
Cdd:COG1196 472 LQEELQRLEKELSSLEARLDRLEAEQRASQGVRA----VLEALESGLPGVYGPVAElikvKEKYETALEAA---LGNRLQ 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1429 SLSVRYEERVQACDKLEKG--------------RTRLQQELDDVTVALDQQRQVVSALEKKQKKFDQMLAEEKLISARya 1494
Cdd:COG1196 545 AVVVENEEVAKKAIEFLKEnkagratflpldriKPLRSLKSDAAPGFLGLASDLIDFDPKYEPAVRFVLGDTLVVDDL-- 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1495 eERDRAEADAREKETKVLSL-----------------SRALEEALETREEMERQNKQLRAEMDDLVSSKDDVGKNVHELE 1557
Cdd:COG1196 623 -EQARRLARKLRIKYRIVTLdgdlvepsgsitggsrnKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLE 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1558 RFKRALEQQVQEMRAQMEELEDELQATEDGKLRLEVNMQALKAQHERELQNRDDANDDKKKL------LSKQVRELEAEL 1631
Cdd:COG1196 702 DLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELeeelesLEEALAKLKEEI 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1632 DAERKQRAQALAGRKKLELDLQEAMAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEARAAREEIFIQSRESEKKLKNL 1711
Cdd:COG1196 782 EELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEEL 861
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1712 EAELLQLQEDLAASERAKRQAQQERDDLADELANGNSGKSALLDEKRHLEARIgqleeeldeeqsnmELLNDRYRKLSMQ 1791
Cdd:COG1196 862 KEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERL--------------EELEAKLERLEVE 927
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1792 VETLTTELGAERSFSQKTEnARQQLERQNKDLRAkLGEMDSSVKSKYKMAIATLESKVAQLEEQLEqesrerilsgklvr 1871
Cdd:COG1196 928 LPELEEELEEEYEDTLETE-LEREIERLEEEIEA-LGPVNLRAIEEYEEVEERYEELKSQREDLEE-------------- 991
|
890 900
....*....|....*....|
gi 1033370542 1872 rAEKKLKEVILQVDEERRNA 1891
Cdd:COG1196 992 -AKEKLLEVIEELDKEKRER 1010
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
994-1890 |
8.66e-36 |
|
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: 149.44 E-value: 8.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 994 KLQLEKVSTEAKLKKMEEDLLVLEDqnskLHKERKLMEERLSeftshmaEEEEKVKSLSKLRNKYEAVMADME-DRLKKE 1072
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLED----ILNELERQLKSLE-------RQAEKAERYKELKAELRELELALLvLRLEEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1073 EKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQED 1152
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1153 MESEKLARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVTELKKTIEEEVKVHEAQVldmrqrhtSALE 1232
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR--------SKVA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1233 ELSEQLEQSRRFKINLEKTKQALEGENAEMQKEVkllqaakleSEQRRKKLEGQVQELQLRAGEGERAKAELVERLVKLQ 1312
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRRERLQQEI---------EELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1313 NELDGVSGTLGSTESKTIKLAKDLAtvesHLQDTQELLQEETRQKLNLSSRVRQLEEEKAAMLEQLEEEEAA---KANFS 1389
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELA----QLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELisvDEGYE 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1390 RQMQ-----SLQQQVMETKKK------------------LEEDAGVAEAIEEARRRAAKDLESLSVRYEERVQACDKLEK 1446
Cdd:TIGR02168 537 AAIEaalggRLQAVVVENLNAakkaiaflkqnelgrvtfLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRK 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1447 GrtrLQQELDDVTVALDQQrqvvSALE-KKQKKFDQML--AEEKLISARYAEERDRAEADAreketKVLSLSRALEEALE 1523
Cdd:TIGR02168 617 A---LSYLLGGVLVVDDLD----NALElAKKLRPGYRIvtLDGDLVRPGGVITGGSAKTNS-----SILERRREIEELEE 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1524 TREEMERQNKQLRAEMDDLVSSKDDVGKNVHELERFKRALEQQVQEMRAQMEELEDELQATEDGKLRLEVNMQALKAQHE 1603
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1604 relqnrddanddkkkllskqvrELEAELDAERKQRAQALAGRKKLELDLQEAMAQLDAANkgrdeagKQLRKLQAQMKEL 1683
Cdd:TIGR02168 765 ----------------------ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-------EALDELRAELTLL 815
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1684 WREVEEARAAREEIFIQSRESEKKLKNLEAELLQLQEDLAASERAKRQAQQERDDLADELAngnsgksALLDEKRHLEAR 1763
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE-------ALLNERASLEEA 888
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1764 IGQLEEELDEEQSNMELLNDRYRKLSMQVETLTTELGAERSFSQKTENARQQLERQNKDLRAKLGEMDSSVKSKYKMAIA 1843
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033370542 1844 TLESKVAQLEEQL---------------EQESRERILSGKL--VRRAEKKLKEVILQVDEERRN 1890
Cdd:TIGR02168 969 EARRRLKRLENKIkelgpvnlaaieeyeELKERYDFLTAQKedLTEAKETLEEAIEEIDREARE 1032
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
993-1799 |
1.35e-34 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 145.24 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 993 QKLQLEKVSTEAKLKKMEEDLLVLED----QNSKLHKERKLMEERLSEFTSHMAEEEEKVKSLSKLRNKYEAVMADMEDR 1068
Cdd:COG1196 189 ERLEDLLEELEKQLEKLERQAEKAERyqelKAELRELELALLLAKLKELRKELEELEEELSRLEEELEELQEELEEAEKE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1069 LKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAE 1148
Cdd:COG1196 269 IEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1149 LQEDMESEKLARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVTELKKTIEEEVKVHEAQVLDMRQRHT 1228
Cdd:COG1196 349 LEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELK 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1229 SALEELSEQLEQSRRFKINLEKTKQALE---GENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGERAKAELV 1305
Cdd:COG1196 429 ELEAELEELQTELEELNEELEELEEQLEelrDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1306 ERLVKLqNELDGVSGTLGSTESK-----TIKLAKDL-ATVESHLQDTQELLQEETRQKLN-----LSSRVRQLEEEKAAM 1374
Cdd:COG1196 509 ALESGL-PGVYGPVAELIKVKEKyetalEAALGNRLqAVVVENEEVAKKAIEFLKENKAGratflPLDRIKPLRSLKSDA 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1375 LEQLEEEEAAKANFSRQMQSLQQQVMetkkkleEDAGVAEAIEEARRRAAKdleslsVRYEERVQACD--KLEKGRTrlq 1452
Cdd:COG1196 588 APGFLGLASDLIDFDPKYEPAVRFVL-------GDTLVVDDLEQARRLARK------LRIKYRIVTLDgdLVEPSGS--- 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1453 qelddVTVALDQQRQVVSALEKKQKKFDQMLAEEklisaryaEERDRAEADAREKETKVLSLSRALEEALETREEMERQN 1532
Cdd:COG1196 652 -----ITGGSRNKRSSLAQKRELKELEEELAELE--------AQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQL 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1533 KQLRAEMDDLVSSKDDVGKNVHELERFKRALEQQVQEMRAQMEELEDELQATEDGKLRLEVNMQALKAQHERELQNRDDA 1612
Cdd:COG1196 719 EELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEEL 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1613 ------NDDKKKLLSKQVRELEAELDAERKQRAQALAGRKKLELDLQEAMAQLDAANKGRDEAGKQLRKLQAQMKELWRE 1686
Cdd:COG1196 799 eeeleeAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDE 878
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1687 VEEARAAREEIFIQSRESEKKLKNLEAELLQLQEDLAASERAKRQAQQERDDLADEL--ANGNSGKSALLDEKRHLEARI 1764
Cdd:COG1196 879 LKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELeeEYEDTLETELEREIERLEEEI 958
|
810 820 830
....*....|....*....|....*....|....*
gi 1033370542 1765 GQLEEELDEEQSNMELLNDRYRKLSMQVETLTTEL 1799
Cdd:COG1196 959 EALGPVNLRAIEEYEEVEERYEELKSQREDLEEAK 993
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
901-1739 |
8.53e-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: 142.89 E-value: 8.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 901 LKELENKYQQLSEEktilAEQLQAETELFAEAEEMRARLAA-RKQELEDILHELESRVEEEEERCQQLQGDKKKMQQHVQ 979
Cdd:TIGR02168 195 LNELERQLKSLERQ----AEKAERYKELKAELRELELALLVlRLEELREELEELQEELKEAEEELEELTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 980 DLEEQLEEEEAARQKLQLEKVSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEERLSEFTSHMAEEEEKVKSLSKLRNKYE 1059
Cdd:TIGR02168 271 ELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1060 AVMADMEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQAALARVEDEAAQKNAVLKSL 1139
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1140 RElqAQLAELQEDMESEKLARAKAEKQRRDLGEELEALKTELEdtldstAAQQELRSKREQE------VTELKKTIEEEV 1213
Cdd:TIGR02168 431 EE--AELKELQAELEELEEELEELQEELERLEEALEELREELE------EAEQALDAAERELaqlqarLDSLERLQENLE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1214 KVHE--AQVLDMRQRHTSALEELSEQLEqsrrFKINLEKTKQALEGENAEMQkEVKLLQAAKLESEQRRKKLEGQVQELQ 1291
Cdd:TIGR02168 503 GFSEgvKALLKNQSGLSGILGVLSELIS----VDEGYEAAIEAALGGRLQAV-VVENLNAAKKAIAFLKQNELGRVTFLP 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1292 LRAGEGERAKAELVERLvklqNELDGVSGTLGSTESKTIKLAKDLATVESHLQDTQELLQE-ETRQKLNLSSRVRQLEEE 1370
Cdd:TIGR02168 578 LDSIKGTEIQGNDREIL----KNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNAlELAKKLRPGYRIVTLDGD 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1371 KAAMLEQLEEEEAAKANfsrQMQSLQQQVMETKKKLEEDAGVAEAIEEARRRAAKDLESlsvryeervqacdkLEKGRTR 1450
Cdd:TIGR02168 654 LVRPGGVITGGSAKTNS---SILERRREIEELEEKIEELEEKIAELEKALAELRKELEE--------------LEEELEQ 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1451 LQQELDDVTVALDQQRQVVSALEKKQKKFDQMLAEEKLISARYAEERDRAEADAREKETkvlslsrALEEALETREEMER 1530
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE-------ELAEAEAEIEELEA 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1531 QNKQLRAEMDDLVSSKDDVGKNVHELERFKRALEQQVQEMRAQMEELEDELQATEDGKLRLEVNMQALKAQHERelqnrd 1610
Cdd:TIGR02168 790 QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE------ 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1611 danddkkklLSKQVRELEAELDAERKQRAQALAGRKKLELDLQEAMAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEA 1690
Cdd:TIGR02168 864 ---------LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1691 RAAREEIFIQSRESEK-KLKNLEAELLQLQEDLAASERAKRQAQQERDDL 1739
Cdd:TIGR02168 935 EVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1031-1743 |
1.28e-30 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 132.50 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1031 EERLSEFTSHMAEEEEKVKSLSKLRNK---YEAVMADMEDRLKKEEKGR-QELEKLKRKLDGEAGDLQEQVAELQQQLEE 1106
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKaerYQALLKEKREYEGYELLKEkEALERQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1107 LRQALARKEAELQAALARVEDEAA-QKNAVLKSLRELQAQLAELQEDMESEKLARAKAEKQRRDLGEELEALKTELEDTL 1185
Cdd:TIGR02169 263 LEKRLEEIEQLLEELNKKIKDLGEeEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1186 DSTAAQQELRSKREQEVTELKKtiEEEVKVHEAQVLDMRQRHT--------SALEELSEQLEQSRRFKINLEKTKQALEG 1257
Cdd:TIGR02169 343 REIEEERKRRDKLTEEYAELKE--ELEDLRAELEEVDKEFAETrdelkdyrEKLEKLKREINELKRELDRLQEELQRLSE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1258 ENAEMQKEVKLLQAAKLESEQRRKklegqvqELQLRAGEGERAKAELVERLVKLQNELDGVSGTLGSTESKTIKLAKDLA 1337
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKE-------DKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1338 TVESHLQDTQELLQEETRQKLNLSSR-------VRQLEEEKAAMLEQLEEEEAAKANFS--------------------- 1389
Cdd:TIGR02169 494 EAEAQARASEERVRGGRAVEEVLKASiqgvhgtVAQLGSVGERYATAIEVAAGNRLNNVvveddavakeaiellkrrkag 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1390 -------RQMQSLQQ---------------QVMETKKKLEE-------DAGVAEAIEEARR------------------- 1421
Cdd:TIGR02169 574 ratflplNKMRDERRdlsilsedgvigfavDLVEFDPKYEPafkyvfgDTLVVEDIEAARRlmgkyrmvtlegelfeksg 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1422 ------RAAKDLESLSVRYEERVQAC----DKLEKGRTRLQQELDDVTVALDQQRQVVSALEKK----QKKFDQMLAEEk 1487
Cdd:TIGR02169 654 amtggsRAPRGGILFSRSEPAELQRLrerlEGLKRELSSLQSELRRIENRLDELSQELSDASRKigeiEKEIEQLEQEE- 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1488 lisARYAEERDRAEADAREKETKVLSLSRALEEALETREEMERQNKQLRAEMDDLVSSKDDVGknVHELERFKRALEQQV 1567
Cdd:TIGR02169 733 ---EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEV 807
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1568 QEMRAQMEELEDELQATEDGKLRLEVNMQALKAQhERELQNRDDANDDKKKLLSKQVRELEAELdaerkqraqalagrKK 1647
Cdd:TIGR02169 808 SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ-RIDLKEQIKSIEKEIENLNGKKEELEEEL--------------EE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1648 LELDLQEAMAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEARAAREEIFIQSRESEKKLKNLEAELLQLQEDLAAsER 1727
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE-EL 951
|
810
....*....|....*.
gi 1033370542 1728 AKRQAQQERDDLADEL 1743
Cdd:TIGR02169 952 SLEDVQAELQRVEEEI 967
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
834-1687 |
4.71e-30 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 130.60 E-value: 4.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 834 KKQQQMSALKVMQRNCAAYLKLRHwqwwRLFTKVKPLLQVTRQDEVMQAKAVELQKVQEkhTKTQMDLKELENKYQQLSE 913
Cdd:COG1196 173 RKEEAERKLERTEENLERLEDLLE----ELEKQLEKLERQAEKAERYQELKAELRELEL--ALLLAKLKELRKELEELEE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 914 EKTILAEQLQAETELFAEAEEMRARLAARKQELEDILHELESRVEEEEERCQQLQGDKKKMQQHVQDLEEQLEEEEAARQ 993
Cdd:COG1196 247 ELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 994 KLQLEKVSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEERLSEF----TSHMAEEEEKVKSLSKLRNKYEAVMADMEDRL 1069
Cdd:COG1196 327 ELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALleelEELFEALREELAELEAELAEIRNELEELKREI 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1070 KKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQAALARVED-------EAAQKNAVLKSLREL 1142
Cdd:COG1196 407 ESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKElerelaeLQEELQRLEKELSSL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1143 QAQLAELQEDMESEKLARAKAEKQRRDLGEELEALKTEL-----------------------EDTLDSTAAQQELRSKRE 1199
Cdd:COG1196 487 EARLDRLEAEQRASQGVRAVLEALESGLPGVYGPVAELIkvkekyetaleaalgnrlqavvvENEEVAKKAIEFLKENKA 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1200 QEVTELKKTIEEEVKVHEAQVLDMRQRHTSALEELSEQLEQSRRFKINLEKTKQALEGENAEMQKEVKLLQAAKLESEQR 1279
Cdd:COG1196 567 GRATFLPLDRIKPLRSLKSDAAPGFLGLASDLIDFDPKYEPAVRFVLGDTLVVDDLEQARRLARKLRIKYRIVTLDGDLV 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1280 RKK---------------LEGQVQELQLRAGEGERAKAELVERLVKLQNELDGVSGTLGSTESKTIKLAKDLatveshlQ 1344
Cdd:COG1196 647 EPSgsitggsrnkrsslaQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQL-------E 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1345 DTQELLQEETRQKLNLSSRVRQLEEEKAAMLEQLEEEEAAKANFSRQMQSLQQQVMETKKKLEEDAGVAEAIEEARRRAA 1424
Cdd:COG1196 720 ELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELE 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1425 KDLESLSVRYEERVQACDKLEKGRTRLQQELddvtvaldqqrqvvSALEKKQKKFDQMLAEEKLISARYAEERDRAEADA 1504
Cdd:COG1196 800 EELEEAERRLDALERELESLEQRRERLEQEI--------------EELEEEIEELEEKLDELEEELEELEKELEELKEEL 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1505 REKETKVLSLSRALEEALETREEMERQNKQLRAEMDDLVSSKDDVGKNVHELERFKRALEQQVQEMRaqmEELEDELQAT 1584
Cdd:COG1196 866 EELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELE---EELEEEYEDT 942
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1585 EDGKLRLEVnmqalkAQHERELQNRDDANDDKKKLLsKQVRELEAELDAERKQRAQALAgrkklelDLQEAMAQLDaaNK 1664
Cdd:COG1196 943 LETELEREI------ERLEEEIEALGPVNLRAIEEY-EEVEERYEELKSQREDLEEAKE-------KLLEVIEELD--KE 1006
|
890 900
....*....|....*....|...
gi 1033370542 1665 GRDEAGKQLRKLQAQMKELWREV 1687
Cdd:COG1196 1007 KRERFKETFDKINENFSEIFKEL 1029
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
1160-1964 |
1.34e-29 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 129.06 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1160 RAKAEKQRRDLGEELEalktELEDTLDSTAAQQElRSKREQEVTELKKTIEEEVKVHEAQVLDMRQRH--------TSAL 1231
Cdd:COG1196 174 KEEAERKLERTEENLE----RLEDLLEELEKQLE-KLERQAEKAERYQELKAELRELELALLLAKLKElrkeleelEEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1232 EELSEQLEQSRRFKINLEKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGERAKAELVERLVKL 1311
Cdd:COG1196 249 SRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1312 QNELDGVSGTLGSTESKTIKLAKDLATVESHLQDTQELL----QEETRQKLNLSSRVRQLEEEKAAMLEQLEEEEAAKAN 1387
Cdd:COG1196 329 KEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLsallEELEELFEALREELAELEAELAEIRNELEELKREIES 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1388 FSRQMQSLQQQVMETKKKLEEDAGVAEAIEEARRRAAKDLESLSVRYEERVQACDKLEKGRTRLQQELDDVTVALDQQRQ 1467
Cdd:COG1196 409 LEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSSLEA 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1468 VVSALEKKQKKFDQMLAEEKLISARYAEERDRAEADAREKETKVLSLSRAL------------EEALETREEMERQNKQ- 1534
Cdd:COG1196 489 RLDRLEAEQRASQGVRAVLEALESGLPGVYGPVAELIKVKEKYETALEAALgnrlqavvveneEVAKKAIEFLKENKAGr 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1535 --------LRAEMDDLVSSKDDVGKNVHELERFKRALEQQVQEMRAQ---MEELEDELQATEDGKLRLEVNmqalkaqhe 1603
Cdd:COG1196 569 atflpldrIKPLRSLKSDAAPGFLGLASDLIDFDPKYEPAVRFVLGDtlvVDDLEQARRLARKLRIKYRIV--------- 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1604 relqNRDDANDDKKKLLSKQVRELEAELDAERKqraqalagrkkleldLQEAMAQLDAANKGRDEAGKQLRKLQAQMKEL 1683
Cdd:COG1196 640 ----TLDGDLVEPSGSITGGSRNKRSSLAQKRE---------------LKELEEELAELEAQLEKLEEELKSLKNELRSL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1684 WREVEEARAAREEIFIQSRESEKKLKNLEAELLQLQEDLAASERAKRQAQQERDDLADELANGNSGKSALLDEKRHLEAR 1763
Cdd:COG1196 701 EDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEE 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1764 IGQLEEELDEEQSNMELLNDRYRKLSMQVETLTTELGAERSFSQKTENARQQLERQNKDLRAKLGEMdssvkskyKMAIA 1843
Cdd:COG1196 781 IEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDEL--------EEELE 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1844 TLESKVAQLEEQLEQESRERILSGKLVRRAEKKLKEVILQVDEERRNADQYKDQVEKGHLRLKQLKRQLeeaEEEASRAN 1923
Cdd:COG1196 853 ELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKL---ERLEVELP 929
|
810 820 830 840
....*....|....*....|....*....|....*....|.
gi 1033370542 1924 ASRRRMQRELEDVTEsaesmnrevTSLRNRLSKVERRQRKR 1964
Cdd:COG1196 930 ELEEELEEEYEDTLE---------TELEREIERLEEEIEAL 961
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
855-1662 |
1.53e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 125.55 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 855 LRHWQWWRLftkvkpLLQVTRQDEVMQAKAVELQKVQEKHTKTQMDLKELENKYQQLSEEKTILAEQLQAETELFAEAEE 934
Cdd:TIGR02168 222 LRELELALL------VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 935 MRARLAARKQELEDILHELESRVEEEEERCQQLQGDKKKMQQHVQDLEEQLeeeeaarQKLQLEKVSTEAKLKKMEEDLL 1014
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL-------EELKEELESLEAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1015 VLEDQNSKLhkerklmEERLSEFTSHMAEEEEKVKSLSKLRNKYEAVMADMEDRLkkeEKGRQELEKLKRKLD-GEAGDL 1093
Cdd:TIGR02168 369 ELESRLEEL-------EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR---ERLQQEIEELLKKLEeAELKEL 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1094 QEQVAELQQQLEELRQALARKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQEDMES-EKLARAKAE--KQRRDL 1170
Cdd:TIGR02168 439 QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENlEGFSEGVKAllKNQSGL 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1171 GEELEALKTELE-DTLDSTAAQQELRSKREQEVTELKKTIEEEV---------KVHEAQVLDMRQRH-TSALEELSEQLE 1239
Cdd:TIGR02168 519 SGILGVLSELISvDEGYEAAIEAALGGRLQAVVVENLNAAKKAIaflkqnelgRVTFLPLDSIKGTEiQGNDREILKNIE 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1240 QSRRFKINLEKTKQALEGENAEMQKEVK--------LLQAAKLESEQRRKKLEGQ-VQELQLRAGEGERAKAELVERlvk 1310
Cdd:TIGR02168 599 GFLGVAKDLVKFDPKLRKALSYLLGGVLvvddldnaLELAKKLRPGYRIVTLDGDlVRPGGVITGGSAKTNSSILER--- 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1311 lQNELDGVSGTLGSTESKTIKLAKDLATVESHLQDTQELLQEETRQKLNLSSRVRQLEEEKAAMLEQLEEEEAAKANFSR 1390
Cdd:TIGR02168 676 -RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1391 QMQSLQQQVMETKKKLEEdagvaeaIEEARRRAAKDLESLSVRYEERVQACDKLEKGRTRLQQELDDVTVALDQQRQVVS 1470
Cdd:TIGR02168 755 ELTELEAEIEELEERLEE-------AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1471 ALEKKQKKFDQMLAEEKLISARYAEERDRAEADAREKETKVLSLSRALEEALETREEMERQNKQLRAEMDDLVSSKDDVG 1550
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1551 KNVHELERFKRALEQQVQEMRAQMEELEDELQATEDgKLRLEVNMQAlkaqheRELQNRDDANDDKKKLLSKQVRELEAE 1630
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE-RLSEEYSLTL------EEAEALENKIEDDEEEARRRLKRLENK 980
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 1033370542 1631 LDA-------------ERKQRAQALAGRKKlelDLQEAMAQLDAA 1662
Cdd:TIGR02168 981 IKElgpvnlaaieeyeELKERYDFLTAQKE---DLTEAKETLEEA 1022
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1071-1950 |
2.18e-24 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 112.08 E-value: 2.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1071 KEEKGRQELEKLKRKLDgeagDLQEQVAELQQQLEELRQALARKEaELQAALARVED-----EAAQKNAVLKSLRELQAQ 1145
Cdd:TIGR02169 171 KKEKALEELEEVEENIE----RLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREyegyeLLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1146 LAELQEDMEseklaraKAEKQRRDLGEELEALKTELEDtldstaAQQELRSKREQEVTELKKTIEEeVKVHEAQVLDMRQ 1225
Cdd:TIGR02169 246 LASLEEELE-------KLTEEISELEKRLEEIEQLLEE------LNKKIKDLGEEEQLRVKEKIGE-LEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1226 RHTSALEELSEQLEQSRRFKINLEKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGERAKAELV 1305
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1306 ERLVKLQNELDgvsgtlgstesktiklakdlatvesHLQDTQELLQEETRQklnLSSRVRQLEEEKAamleqleeeeaak 1385
Cdd:TIGR02169 392 EKLEKLKREIN-------------------------ELKRELDRLQEELQR---LSEELADLNAAIA------------- 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1386 anfsrqmqSLQQQVMETKKKLEEDAGVAEAIEEARRRAAKDLESLSVRYEERVQACDKLEKGRTRLQQELDdvtvALDQQ 1465
Cdd:TIGR02169 431 --------GIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA----EAEAQ 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1466 RQVVSALEKKQKKFDQMLaeEKLISARYAEERDRAEADAReketkvlsLSRALEEALETReemerqnkqlraeMDDLVSS 1545
Cdd:TIGR02169 499 ARASEERVRGGRAVEEVL--KASIQGVHGTVAQLGSVGER--------YATAIEVAAGNR-------------LNNVVVE 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1546 KDDVGKNVHEL---ERFKRALEQQVQEMRAQMEELEdelQATEDGKLRLEVNMQALKAQHE-------RELQNRDDANDD 1615
Cdd:TIGR02169 556 DDAVAKEAIELlkrRKAGRATFLPLNKMRDERRDLS---ILSEDGVIGFAVDLVEFDPKYEpafkyvfGDTLVVEDIEAA 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1616 KKKLLSKQVRELEAEL--------DAERKQRAQALAGRKKLElDLQEAMAQLDAANKGRDEAGKQLRKLQAQMKELWREV 1687
Cdd:TIGR02169 633 RRLMGKYRMVTLEGELfeksgamtGGSRAPRGGILFSRSEPA-ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQEL 711
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1688 EEARAAREEIFIQSRESEKKLKNLEAELLQLQEDLAASERAKRQAQQERDDLADELANGNSGKSALLDEKRHLEARIGQL 1767
Cdd:TIGR02169 712 SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS 791
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1768 EEELDEEQsnMELLNDRYRKLSMQVETLTTELGAERSFSQKTENARQQLERQNKDLRAKlgemdssvKSKYKMAIATLES 1847
Cdd:TIGR02169 792 RIPEIQAE--LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ--------IKSIEKEIENLNG 861
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1848 KVAQLEEQLEQ-ESRERILSGKLVrRAEKKLKEVILQVDEERRNADQYKDQVEKGHLRLKQLKRQLEEAEEEASRANASR 1926
Cdd:TIGR02169 862 KKEELEEELEElEAALRDLESRLG-DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK 940
|
890 900 910
....*....|....*....|....*....|
gi 1033370542 1927 RRMQRE------LEDVTESAESMNREVTSL 1950
Cdd:TIGR02169 941 GEDEEIpeeelsLEDVQAELQRVEEEIRAL 970
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
882-1732 |
5.44e-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: 110.93 E-value: 5.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 882 AKAVELQKVQEKhtKTQMDLKELENKYQQLSEEKTILAEQLQAETE----LFAEAEEMRARLAARKQELEDILHELESRV 957
Cdd:TIGR02169 208 EKAERYQALLKE--KREYEGYELLKEKEALERQKEAIERQLASLEEelekLTEEISELEKRLEEIEQLLEELNKKIKDLG 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 958 EEEEERCQ----QLQGDKKKMQQHVQDLEEQLEEEEAARQKLQLEKVSTEAKLKKMEEDLlvledqnsklhkerklmEER 1033
Cdd:TIGR02169 286 EEEQLRVKekigELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREI-----------------EEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1034 LSEFTSHMAEEEEKVKSLSKLRNKYEAVMADMEDRLKKEEKGRQELEKLKRKLD---GEAGDLQEQVAELQQQLEELRQA 1110
Cdd:TIGR02169 349 RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINelkRELDRLQEELQRLSEELADLNAA 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1111 LARKEAELQAALARVEDEAAQknavlksLRELQAQLAELQEDMESEKLARAKAEKQRRDLGEELEALKTELeDTLDSTAA 1190
Cdd:TIGR02169 429 IAGIEAKINELEEEKEDKALE-------IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL-AEAEAQAR 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1191 QQELRSKREQEVTELKKTIEEEVKVHEAQVLDMRQRHTSALEelseqLEQSRRFKiNLEKTKQALEGENAEMQKEVKLLQ 1270
Cdd:TIGR02169 501 ASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIE-----VAAGNRLN-NVVVEDDAVAKEAIELLKRRKAGR 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1271 AAKLesEQRRKKLEGQVQELQLRAGEGERAkAELVERLVKLQNELDGVSGTLGSTESktIKLAKDL------ATVESHLQ 1344
Cdd:TIGR02169 575 ATFL--PLNKMRDERRDLSILSEDGVIGFA-VDLVEFDPKYEPAFKYVFGDTLVVED--IEAARRLmgkyrmVTLEGELF 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1345 DTQELLQEETRQKLNLSSRVRQLEEEKAAMLEQLEEEEAAKANFSRQMQSLQQQVMETKKKLEEDAGVAEAIEEARRRAA 1424
Cdd:TIGR02169 650 EKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLE 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1425 KDLESLSVRYEERVQACDKLEKGRTRLQQELDDVTVALDQQRQVVSALEKKQKKFDQMLAEEKLISARyaEERDRAEADA 1504
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQ--AELSKLEEEV 807
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1505 REKETKVLSLSRALEEALETREEMERQNKQLRAEMDDLVSSKDDVGKNVHELERFKRALEQQVQEMRAQMEELEDELQAT 1584
Cdd:TIGR02169 808 SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1585 EDGKLRLEVNMQALKaqherelQNRDDANDDkkkllskqvRELEAELDAERKQRAQALAGRKKLELDLQEAMAQLDAANK 1664
Cdd:TIGR02169 888 KKERDELEAQLRELE-------RKIEELEAQ---------IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL 951
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033370542 1665 GRDEAGKQLRKLQAQMKELW-------REVEEARAAREEIfiqsresEKKLKNLEAELLQLQEDLAASERAKRQA 1732
Cdd:TIGR02169 952 SLEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDEL-------KEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
880-1592 |
6.86e-24 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 110.57 E-value: 6.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 880 MQAKAVELQKVQEKHTKTQMDLKELENKYQQLSEEKTILAEQL-QAETELFAEAEEMRARLAARKQELEDILHELESRVE 958
Cdd:COG1196 318 LEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKeELEEKLSALLEELEELFEALREELAELEAELAEIRN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 959 EEeercQQLQGDKKKMQQHVQDLEEQLEEEEAARQKLQLEKVSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEERLseft 1038
Cdd:COG1196 398 EL----EELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELEREL---- 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1039 shmAEEEEKVKSLSKLRNKYEAVMADMEDRLKKEEKGRQELEKLKRKLDGEAGdlqeQVAELQQQLEELRQALarkEAEL 1118
Cdd:COG1196 470 ---AELQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLPGVYG----PVAELIKVKEKYETAL---EAAL 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1119 QAALAR--VEDEAAQKNAV--LKSLRELQAQLAELqEDMESEKLARAKAEKQRRDLGEEL--------EALKTELEDTL- 1185
Cdd:COG1196 540 GNRLQAvvVENEEVAKKAIefLKENKAGRATFLPL-DRIKPLRSLKSDAAPGFLGLASDLidfdpkyePAVRFVLGDTLv 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1186 --DSTAAQQELRSKR--------EQEVTELKKTI-------------EEEVKVHEAQVLDMRQRHTSALEELSEQLEQSR 1242
Cdd:COG1196 619 vdDLEQARRLARKLRikyrivtlDGDLVEPSGSItggsrnkrsslaqKRELKELEEELAELEAQLEKLEEELKSLKNELR 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1243 RFKINLEKTKQALEgenaEMQKEVKLLQAAKLESEQRRKKLEGQVQELqlragegERAKAELVERLVKLQNELDGVSGTL 1322
Cdd:COG1196 699 SLEDLLEELRRQLE----ELERQLEELKRELAALEEELEQLQSRLEEL-------EEELEELEEELEELQERLEELEEEL 767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1323 GSTESKTIKLAKDLATVESHLQDTQELLQEETRQKLNLSSRVRQLEEEKAAMLEQLEEEEAAKANFSRQMQSLQQQVMET 1402
Cdd:COG1196 768 ESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDEL 847
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1403 KKKLEEDAGVAEAIEEARRRAAKDLESLSVRYEERVQACDKLEKGRTRLQQELDDVTVALDQQRQVVSALEKKQKKFDQM 1482
Cdd:COG1196 848 EEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVE 927
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1483 L--AEEKLISARYAEERDRAEADAREKETKVLSLSRALEEALETREEMERQNKQLRAEMDDLVSSKDDVGKNVHELERFK 1560
Cdd:COG1196 928 LpeLEEELEEEYEDTLETELEREIERLEEEIEALGPVNLRAIEEYEEVEERYEELKSQREDLEEAKEKLLEVIEELDKEK 1007
|
730 740 750
....*....|....*....|....*....|...
gi 1033370542 1561 R-ALEQQVQEMRAQMEELEDELQATEDGKLRLE 1592
Cdd:COG1196 1008 ReRFKETFDKINENFSEIFKELFGGGTAELELT 1040
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
841-1637 |
7.77e-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: 110.16 E-value: 7.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 841 ALKVMQRNCAAYLKLRHWQWWRLfTKVKPLLQVTRQDEVMQAKAVELQKVQEKHTKTQMDLKELENKYQQLSEEKTIL-- 918
Cdd:TIGR02169 215 ALLKEKREYEGYELLKEKEALER-QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvk 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 919 -------AEQLQAETELFAEAEEMRaRLAARKQELEDILHELESRVEEEEERCQQLQGDKKKMQQHVQDLEEQLEEEEAA 991
Cdd:TIGR02169 294 ekigeleAEIASLERSIAEKERELE-DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 992 RQKLQLEKVSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEERLSEFTSHMAEEEEKVKSLSKLRNKYEAVMADMEDRLKK 1071
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1072 EEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQE 1151
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGS 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1152 DMESEKLARAKAekqrrdLGEELEALKteLEDTLDSTAAQQELRSKREQEVT-----ELKKTIEEEVKVHEAQVLDM--- 1223
Cdd:TIGR02169 533 VGERYATAIEVA------AGNRLNNVV--VEDDAVAKEAIELLKRRKAGRATflplnKMRDERRDLSILSEDGVIGFavd 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1224 ----RQRHTSALEE------LSEQLEQSRRFKINLEKTkqALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLR 1293
Cdd:TIGR02169 605 lvefDPKYEPAFKYvfgdtlVVEDIEAARRLMGKYRMV--TLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRER 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1294 AGEGERAKAELVERLVKLQNELDGVSGTLGSTESKTIKLAKDLATVESHLQDTQELLQEETRQKLNLSSRVRQLEEEKAA 1373
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKE 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1374 MLEQLEEEEAAKANFSRQMQSLQQqvMETKKKLEEDAGVAEAIEEARRRAAKDLESLSVRYEERVQACDKLEKGRTRLQQ 1453
Cdd:TIGR02169 763 LEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE 840
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1454 ELDDVTVALDQQRQVVSALEKKQKKFDQMLAEEKLISARYAEERDRAEADAREKETKVLSLSRALEEALETREEMERQNK 1533
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1534 QLRAEMDDLVSSKDDVGKNVHELERFKRAL--EQQVQEMRaqmEELEDELQATEDgklrleVNMQALKaQHERELQNRDD 1611
Cdd:TIGR02169 921 ELKAKLEALEEELSEIEDPKGEDEEIPEEElsLEDVQAEL---QRVEEEIRALEP------VNMLAIQ-EYEEVLKRLDE 990
|
810 820
....*....|....*....|....*...
gi 1033370542 1612 ANDDKKKLL--SKQVRELEAELDAERKQ 1637
Cdd:TIGR02169 991 LKEKRAKLEeeRKAILERIEEYEKKKRE 1018
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
876-1747 |
2.16e-23 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 109.08 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 876 QDEVMQAKAVELQKVQEKHTKTQMDLKELENKYQQLSEEKTILAEQLQAETELFAEAEEMRARLAARKQelEDILHELES 955
Cdd:PTZ00121 1068 QDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKA--EDARKAEEA 1145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 956 RVEEEEERCQQLQGDKKKMQQHVQDLEEQLEEEEAARQKLQLEKVSteaKLKKMEEdllvledqNSKLHKERKLMEERLS 1035
Cdd:PTZ00121 1146 RKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAE---ELRKAED--------ARKAEAARKAEEERKA 1214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1036 EfTSHMAEEEEKVKSLSKLRnkyEAVMADMEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQV-AELQQQLEELRQALARK 1114
Cdd:PTZ00121 1215 E-EARKAEDAKKAEAVKKAE---EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIkAEEARKADELKKAEEKK 1290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1115 EAE--LQAALARVEDEAAQKNAVLKSLRELQAQLAELQEDMESEKLARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQ 1192
Cdd:PTZ00121 1291 KADeaKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1193 ELRSKREQEVTELKKTIEEEVKVHEAQvlDMRQRHTSALEELSEQLEQSRRFKinlEKTKQALEGENAEMQK----EVKL 1268
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAK--KKAEEDKKKADELKKAAAAKKKAD---EAKKKAEEKKKADEAKkkaeEAKK 1445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1269 LQAAKLESEQRRKKLEGQVQELQLRAGEGERAKAELVERLVKLQNEldgvsgtlgSTESKtiKLAKDLATVESHLQDTQE 1348
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK---------AEEAK--KKADEAKKAAEAKKKADE 1514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1349 LLQEETRQKlnlSSRVRQLEEEKAAmLEQLEEEEAAKANFSRQMQSLQQ----QVMETKKKLEEDAGVA-EAIEEARRRA 1423
Cdd:PTZ00121 1515 AKKAEEAKK---ADEAKKAEEAKKA-DEAKKAEEKKKADELKKAEELKKaeekKKAEEAKKAEEDKNMAlRKAEEAKKAE 1590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1424 AKDLESLSVRYEE----RVQACDKLEKGRTRlQQELDDVTVALDQQRQVVSALEKKQKKFDQMLAEEKLISARYAEERDR 1499
Cdd:PTZ00121 1591 EARIEEVMKLYEEekkmKAEEAKKAEEAKIK-AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1500 AEADAREKE--TKVLSLSRALEEALETREEMERQNKQLRAEMDDLVSSKDDVGKNVHELERFKRALEQQVQEMRAQMEEL 1577
Cdd:PTZ00121 1670 AEEDKKKAEeaKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA 1749
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1578 ---EDELQATEDGKLRLEVNMQALKAQHERELQNRDDANDDKKKLlskqvrELEAELDAERKQRAQALAGRKKLELDLQE 1654
Cdd:PTZ00121 1750 kkdEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRM------EVDKKIKDIFDNFANIIEGGKEGNLVIND 1823
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1655 AMAQLDAANKGRDEAGKQLRklqaqmkelwrevEEARAAREEIFIQSRESEK---KLKNLEAELLQLQEDLAASERAKRQ 1731
Cdd:PTZ00121 1824 SKEMEDSAIKEVADSKNMQL-------------EEADAFEKHKFNKNNENGEdgnKEADFNKEKDLKEDDEEEIEEADEI 1890
|
890
....*....|....*.
gi 1033370542 1732 AQQERDDLADELANGN 1747
Cdd:PTZ00121 1891 EKIDKDDIEREIPNNN 1906
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ... |
1025-1890 |
6.68e-23 |
|
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: 107.36 E-value: 6.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1025 KERKLMEERLSEFTSHMAEEEEKVKSLSKLRNKYEAVMADME-----DRLKKEEKGRQELEKLKRKLDGEAGDL------ 1093
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEElklqeLKLKEQAKKALEYYQLKEKLELEEEYLlyldyl 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1094 ---QEQVAELQQQLEELRQALARKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQEDMESEKLARAKAEKQRRDL 1170
Cdd:pfam02463 233 klnEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1171 GEELEALKTELEDTLDSTAAQQELRSKREQEVTELKKTIEEEvkvhEAQVLDMRQRHTSALEELSEQLEQsrrFKINLEK 1250
Cdd:pfam02463 313 EEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAE----EEEEEELEKLQEKLEQLEEELLAK---KKLESER 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1251 TKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEgqvqELQLRAGEGERAKAELVERLVKLQNELDGVSGTLGSTESKTI 1330
Cdd:pfam02463 386 LSSAAKLKEEELELKSEEEKEAQLLLELARQLED----LLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1331 KLAKDLATVESHLQDTQELLQEETRQKLNLSSRvrqLEEEKAAMLEQLEEEEAAKANFSRQMQSLQQQVMETKKKLEE-D 1409
Cdd:pfam02463 462 KDELELKKSEDLLKETQLVKLQEQLELLLSRQK---LEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVaV 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1410 AGVAEAIEEARRRAAKDLESLSVRYEERVQACDKLEKGRTRLQQELDDVTVALDQQRQVVSALEKKQKKFDQMLAEEKLI 1489
Cdd:pfam02463 539 ENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADED 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1490 SARYAE----ERDRAEADAREKETKVLSLSRALEEALETREEMERQNKQLRAEMDDLVSSKDDVGKNVHELERFK---RA 1562
Cdd:pfam02463 619 DKRAKVvegiLKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEilrRQ 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1563 LEQQVQEMRAQMEELEDELQATEDGKLRLEVNMQALKAQHERELQNRDDANDDKKKLLSKQVRELEAELDAERKQRAQAL 1642
Cdd:pfam02463 699 LEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAE 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1643 AGRKKLELDLQ-EAMAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEARAAREEIFIQSRESEKKLKNLEAELLQLQED 1721
Cdd:pfam02463 779 EREKTEKLKVEeEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELER 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1722 LAASERAK----RQAQQERDDLADELANGNSGKSALLDEKRHLEARIGQLEEELDEEQSNMELLNDRYRKLSMQVETLTT 1797
Cdd:pfam02463 859 LEEEITKEellqELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPE 938
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1798 ELGAERSFSQKTENARQQLERQNKDLRAKLGEMDSSVKSKYKMAIATLESKVAQLEEQLEQESRERilsgklvrraeKKL 1877
Cdd:pfam02463 939 ELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEK-----------KKL 1007
|
890
....*....|...
gi 1033370542 1878 KEVILQVDEERRN 1890
Cdd:pfam02463 1008 IRAIIEETCQRLK 1020
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
992-1581 |
2.05e-21 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 102.06 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 992 RQKLQLEKVSTEAK-LKKMEEDLLVLEDQNSKLHKERKLMEERLSEFTSHMAEEEEKVKSLSKLRNKYEAVMADMEDRLK 1070
Cdd:PRK03918 152 RQILGLDDYENAYKnLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1071 KEEKGRQELEKLKR---KLDGEAGDLQEQVAELQQQLEELRQalarKEAELQAALARvedeaaqknavLKSLRELQAQLA 1147
Cdd:PRK03918 232 ELEELKEEIEELEKeleSLEGSKRKLEEKIRELEERIEELKK----EIEELEEKVKE-----------LKELKEKAEEYI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1148 ELQEDMESEKLARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRSKREQ---EVTELKKTIE--EEVKVHEAQVLD 1222
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHElyEEAKAKKEELER 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1223 MRQRHTS-ALEELSEQLEQSRRFKINLEKTKQALEGENAEMQKEVKLLQAAKLE---------------SEQRRKKLegq 1286
Cdd:PRK03918 377 LKKRLTGlTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrelTEEHRKEL--- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1287 VQELQLRAGEGERAKAELVERLVKLQNELDGVSGTLgSTESKTIKL---AKDLATVESHLQ--DTQELLQ-----EETRQ 1356
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVL-KKESELIKLkelAEQLKELEEKLKkyNLEELEKkaeeyEKLKE 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1357 KLN-LSSRVRQLEEEkaamLEQLEEEEAAKANFSRQMQSLQQQVMETKKKLEEDAgvAEAIEEARRRAaKDLESLSVRYE 1435
Cdd:PRK03918 533 KLIkLKGEIKSLKKE----LEKLEELKKKLAELEKKLDELEEELAELLKELEELG--FESVEELEERL-KELEPFYNEYL 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1436 ERVQACDKLEKGRTRLQQELDDVTVALDQQRQVVSALEKKQKKFDQMLAeeklisaRYAEErdraeaDAREKETKVLSLS 1515
Cdd:PRK03918 606 ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK-------KYSEE------EYEELREEYLELS 672
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1033370542 1516 RALEEALETREEMERQNKQLRAEMDDLVSSKDDVGKNVHELERFKRALEqQVQEMRAQMEELEDEL 1581
Cdd:PRK03918 673 RELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALL 737
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
99-738 |
7.17e-21 |
|
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: 100.20 E-value: 7.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 99 LKDRYYSGLIYTYSGLFCV-VINPYKNL------PIYTEQIVEMYRGKKRHE--MPPHIYAISE---------------- 153
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 154 ----AAYRSMLQDReDQSILCTGESGAGKTENTKKVIQYLAHVA-------------------------------SSHKA 198
Cdd:cd14894 87 pstiSSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAqpalskgseetckvsgstrqpkiklftsstkSTIQM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 199 RKDH--------------------NIPPE-------------------------YPTEAKQGELERQL------------ 221
Cdd:cd14894 166 RTEEartialleakgvekyeivllDLHPErwdemtsvsrskrlpqvhvdglffgFYEKLEHLEDEEQLrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 222 ----LQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDVAGY---IVGANIETYLLEKSRAIRQA------KDERTFHI 286
Cdd:cd14894 246 lsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 287 FYQLLVGAGEH-----MKGELLLEPFN--QYRFLSNGYLPIPG--------QQDKEIFHETMESMRIMGFSHEEIHCMLR 351
Cdd:cd14894 326 LYAMVAGVNAFpfmrlLAKELHLDGIDcsALTYLGRSDHKLAGfvskedtwKKDVERWQQVIDGLDELNVSPDEQKTIFK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 352 MVSAVLQFGNIVFRKERNTDQASMPDN---TAAQKLCHLLGM-NVTEFTRAILTPRIKV--GRDYVQKAQTKEQADFAVE 425
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELgSVEKLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 426 ALAKATYERLFRWLVHRINRAL-------DRTKRQ---------GASFIGILDIAGFEIFQLNSFEQLCINYTNEKLqql 489
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL--- 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 490 fnhtmfvleqeeYQREGiewNFIDFGLDLQPCI-------DLIERPANPPGVLALLDEECWFPKAT----------DKSF 552
Cdd:cd14894 563 ------------YAREE---QVIAVAYSSRPHLtardsekDVLFIYEHPLGVFASLEELTILHQSEnmnaqqeekrNKLF 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 553 VEKVSQEQGTHPKfQKPRQLRDKA----------DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSADKFTAELW 622
Cdd:cd14894 628 VRNIYDRNSSRLP-EPPRVLSNAKrhtpvllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRML 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 623 KDEIQniqkvyffdsYAVAPQGPVEMdrivgldqvsgmgdlaFGASYKTKKGMFRTVGQlYKESLSKLMSTLRNTNPNFV 702
Cdd:cd14894 707 NESSQ----------LGWSPNTNRSM----------------LGSAESRLSGTKSFVGQ-FRSHVNVLTSQDDKNMPFYF 759
|
810 820 830
....*....|....*....|....*....|....*.
gi 1033370542 703 RCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICR 738
Cdd:cd14894 760 HCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICR 795
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1200-1907 |
4.13e-20 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 97.86 E-value: 4.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1200 QEVTELKKTIEEEVKVHEAQVLDMRQRHTSALEELSE-QLEQSRRFKINlEKTKQALEGENAEMQKEVKLLQAAKLESEQ 1278
Cdd:pfam15921 85 HQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEmQMERDAMADIR-RRESQSQEDLRNQLQNTVHELEAAKCLKED 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1279 RRKKLEGQVQELQLRAGEGERAKAELVERLVKLQN-------ELDGVSG----TLGSTESKTIKlakDLATVESHL---- 1343
Cdd:pfam15921 164 MLNDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEasgkkiyEHDSMSTihfrSLGSAISKILR---ELDTEISYLkgri 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1344 ---QDTQELLQEETRQKLNL-----SSRVRQL----EEEKAAMLEQLEEEEAAKANFSRQMQSLQQQV-----METKKKL 1406
Cdd:pfam15921 241 fpvEDQLEALKSESQNKIELllqqhQDRIEQLisehEVEITGLTEKASSARSQANSIQSQLEIIQEQArnqnsMYMRQLS 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1407 EEDAGVAE---AIEEARRRAAKDLESLSvryEERVQACDKLEKGRTRLQQELDDVTVALDQQRQVVSALEKKQKKFDQML 1483
Cdd:pfam15921 321 DLESTVSQlrsELREAKRMYEDKIEELE---KQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEK 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1484 AEEKLISAR-----YAEERDRAEADAREKETKVL-SLSRALEEalETREEMERQNKQLRAEMDDLV----------SSKD 1547
Cdd:pfam15921 398 EQNKRLWDRdtgnsITIDHLRRELDDRNMEVQRLeALLKAMKS--ECQGQMERQMAAIQGKNESLEkvssltaqleSTKE 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1548 DVGKNVHELERFKRALE---QQVQEMRAQMEELEDELQAT--EDGKLRLEVNMQALKAQHereLQNRDDanddkkkllsk 1622
Cdd:pfam15921 476 MLRKVVEELTAKKMTLEsseRTVSDLTASLQEKERAIEATnaEITKLRSRVDLKLQELQH---LKNEGD----------- 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1623 QVRELEAELDAERKQRAQAlagRKKLELDLQ--EAMAQLdAANKGRDEAGKQLRK--LQAQMKELWREVEEARAAREEIF 1698
Cdd:pfam15921 542 HLRNVQTECEALKLQMAEK---DKVIEILRQqiENMTQL-VGQHGRTAGAMQVEKaqLEKEINDRRLELQEFKILKDKKD 617
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1699 IQSRESEKKLKNLEAELLQLQEDLAASERAKRQAQQERDDLADELANGNSGKSALLDEKRHLEARIgqleeelDEEQSNM 1778
Cdd:pfam15921 618 AKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNF-------RNKSEEM 690
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1779 ELLNDryrKLSMQVETLTTELGAERSFSQKTENARQQLER----QNKDLRAKLGEMDSsvkskykmaiatLESKVAQLEE 1854
Cdd:pfam15921 691 ETTTN---KLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKvamgMQKQITAKRGQIDA------------LQSKIQFLEE 755
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1033370542 1855 QLEQESRERilsgKLVRRAEKKLKEVILQVDEERRNADQYKDQVEKGHLRLKQ 1907
Cdd:pfam15921 756 AMTNANKEK----HFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKE 804
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1113-1963 |
5.67e-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: 97.43 E-value: 5.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1113 RKEAEL-----QAALARVEDeaaqknavlkSLRELQAQLAELQedmeseklARAKAEKQRRDLGEELEALKTELEdTLDS 1187
Cdd:TIGR02168 174 RKETERklertRENLDRLED----------ILNELERQLKSLE--------RQAEKAERYKELKAELRELELALL-VLRL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1188 TAAQQELRSKREQEvtelkktieeevkvheAQVLDMRQRHTSALEELSEQLEQSRRFKINLEKTKQALEGENAEMQKEVK 1267
Cdd:TIGR02168 235 EELREELEELQEEL----------------KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1268 LLQAAKLESEQRRKKLEGQVQELQLRAGEGERAKAELVERLVKLQNELDGVSGTLGSTESKTIKLAKDLATVESHLQDTQ 1347
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1348 ELLQEetrqklnLSSRVRQLEEEKAAmleqleeeeaakanfsrqmQSLQQQVMETKKkleedagvaEAIEEARRRAAKDL 1427
Cdd:TIGR02168 379 EQLET-------LRSKVAQLELQIAS-------------------LNNEIERLEARL---------ERLEDRRERLQQEI 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1428 ESLSVRYEErvQACDKLEKGRTRLQQELDDVTVALDQqrqVVSALEKKQKKFDQmlAEEKLISARYAEERDRAEADAREk 1507
Cdd:TIGR02168 424 EELLKKLEE--AELKELQAELEELEEELEELQEELER---LEEALEELREELEE--AEQALDAAERELAQLQARLDSLE- 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1508 etkvlslsrALEEALETREEMERQNKQLRAEMDDLVSSkddVGKNVHELERFKRALEQQVQEmRAQMEELEDELQAtedg 1587
Cdd:TIGR02168 496 ---------RLQENLEGFSEGVKALLKNQSGLSGILGV---LSELISVDEGYEAAIEAALGG-RLQAVVVENLNAA---- 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1588 klrlevnMQALKAQHErelqnrddaNDDKKKLLSKQVRELEAELDAERKQRAQALAGRKKLELDLQEAMAQLDAANKGR- 1666
Cdd:TIGR02168 559 -------KKAIAFLKQ---------NELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLl 622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1667 ---------DEAGKQLRKLQAQMK------ELWRE--VEEARAAREEIFIQSRESEkkLKNLEAELLQLQEDLAASERAK 1729
Cdd:TIGR02168 623 ggvlvvddlDNALELAKKLRPGYRivtldgDLVRPggVITGGSAKTNSSILERRRE--IEELEEKIEELEEKIAELEKAL 700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1730 RQAQQERDDLADELangnsgksalldekrhlearigqleeeldeeqsnmELLNDRYRKLSMQVETLTTELGAERSFSQKT 1809
Cdd:TIGR02168 701 AELRKELEELEEEL-----------------------------------EQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1810 ENARQQLERQNKDLRAKLGEMDSSVkSKYKMAIATLESKVAQLEEQLEQESRERILSGKLVRRAEKKLKE-------VIL 1882
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERL-EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanLRE 824
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1883 QVDEERRNADQYKDQVEKGHLRLKQLKRQLEEAEEEASRANASRRRMQRELEDVTESAESMNREVTSLRNRLSKVERRQR 1962
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
.
gi 1033370542 1963 K 1963
Cdd:TIGR02168 905 E 905
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
888-1430 |
1.57e-19 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 95.98 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 888 QKVQEKHTKTQMDLKELENKYQQLSEEKTILAEQLQAETElfAEAEEMRARLAARKQELEDILHELESRVEEEEERCQQL 967
Cdd:COG0419 174 ELLKEVIKEAKAKIEELEGQLSELLEDIEDLLEALEEELK--ELKKLEEIQEEQEEEELEQEIEALEERLAELEEEKERL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 968 QGDKKKMQQHVQDLEEQLEEEEAARQKLQLEKVSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEERLSEFTSHMAEEEEk 1047
Cdd:COG0419 252 EELKARLLEIESLELEALKIREEELRELERLLEELEEKIERLEELEREIEELEEELEGLRALLEELEELLEKLKSLEER- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1048 vksLSKLRNKYEAVMADMEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQAALARVED 1127
Cdd:COG0419 331 ---LEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELKEELAELSAALEE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1128 EAAQKNAVLKSLRELQAQLAELQEDMESEKLARAKAEKQR-----------------RDLGEELEALKTELEDTLDSTAA 1190
Cdd:COG0419 408 IQEELEELEKELEELERELEELEEEIKKLEEQINQLESKElmiaelagagekcpvcgQELPEEHEKELLELYELELEELE 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1191 QQELRSKREQEVTELKKTIEEEVKVHEAQVLDMRQRHTSALEELSEQLEQSRRFKINLE--KTKQALEGENAEMQKEVKL 1268
Cdd:COG0419 488 EELSREKEEAELREEIEELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEELEelKEKLQLQQLKEELRQLEDR 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1269 LQAAKLESEQRRKKLE--GQVQELQLRAGEGERAKAELVERLVKLQNELDgvSGTLGSTESKTIKLAKDLATVESHLQDT 1346
Cdd:COG0419 568 LQELKELLEELRLLRTrkEELEELRERLKELKKKLKELEERLSQLEELLQ--SLELSEAENELEEAEEELESELEKLNLQ 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1347 QELLQEETRQKLNLSSRVRQLEEE------KAAMLEQLEEEEAAKANFSRQMQSLQQQVMETKKKLEEDAGVAEAIEEAR 1420
Cdd:COG0419 646 AELEELLQAALEELEEKVEELEAEirrelqRIENEEQLEEKLEELEQLEEELEQLREELEELLKKLGEIEQLIEELESRK 725
|
570
....*....|
gi 1033370542 1421 RRAAKDLESL 1430
Cdd:COG0419 726 AELEELKKEL 735
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
1406-1965 |
1.96e-19 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 95.94 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1406 LEEDAGVAEA---IEEARR---RAAKDLESLSVRYEERVQACDKLEKGRT------RLQQELDDVTVAL---------DQ 1464
Cdd:COG1196 161 IEEAAGVSKYkerKEEAERkleRTEENLERLEDLLEELEKQLEKLERQAEkaeryqELKAELRELELALllaklkelrKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1465 QRQVVSALEKKQKKFDQMLAEEKLISARYAEERDRAEadarEKETKVLSLSRALEEALETREEMERQNKQLRAEMDDLVS 1544
Cdd:COG1196 241 LEELEEELSRLEEELEELQEELEEAEKEIEELKSELE----ELREELEELQEELLELKEEIEELEGEISLLRERLEELEN 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1545 SKDDVGKNVHELERFKRALEQQVQEMRAQMEELE----------DELQATEDGKLRLEVNMQALKAQHERELQNRDDAND 1614
Cdd:COG1196 317 ELEELEERLEELKEKIEALKEELEERETLLEELEqllaeleeakEELEEKLSALLEELEELFEALREELAELEAELAEIR 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1615 DKKKLLSKQVRELEAELDAERKQRAQALAGRKKLELDLQEAMAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEARAAR 1694
Cdd:COG1196 397 NELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEEL 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1695 EEIFIQSRESEKKLKNLEAELLQLQEDLAASERAKRQ------------AQQERDDLADELANGNSGKSA---------- 1752
Cdd:COG1196 477 QRLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGlpgvygpvaeliKVKEKYETALEAALGNRLQAVvveneevakk 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1753 ----------------LLDEKRHLEARIGQLEEELDEEQSNMELLNDRYRKLSMQ-------VETLTTELGAERSFSQKT 1809
Cdd:COG1196 557 aieflkenkagratflPLDRIKPLRSLKSDAAPGFLGLASDLIDFDPKYEPAVRFvlgdtlvVDDLEQARRLARKLRIKY 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1810 ENARQQLERQNKDLRAKLGEMDSSVKSKYKMAIATLESKVAQLEEQLEQESRERILSGKLVRRAEKKLKEVILQVDEERR 1889
Cdd:COG1196 637 RIVTLDGDLVEPSGSITGGSRNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELER 716
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1033370542 1890 NADQYKDQVEKGHLRLKQLKRQLEEAEEEASRANASRRRMQRELEDVTESAESMNREVTSLRNRLSKVERRQRKRT 1965
Cdd:COG1196 717 QLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQ 792
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
1162-1745 |
2.82e-19 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 95.21 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1162 KAEKQRRDLGEELEALKTELEDTLDSTAAQQELRSKR-EQEVTELKKTIEEEVKVHEAQVLDMRQRHTSALEELSEQLEQ 1240
Cdd:COG0419 171 KLSELLKEVIKEAKAKIEELEGQLSELLEDIEDLLEAlEEELKELKKLEEIQEEQEEEELEQEIEALEERLAELEEEKER 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1241 srrfkinLEKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGERAKAELVERLvklqneldgvsg 1320
Cdd:COG0419 251 -------LEELKARLLEIESLELEALKIREEELRELERLLEELEEKIERLEELEREIEELEEELEGLR------------ 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1321 tlgstesktiKLAKDLATVESHLQDTQELLQEETRQKLNLSSRVRQLEEEKAAMLEQLeeeeaakanfSRQMQSLQQQVM 1400
Cdd:COG0419 312 ----------ALLEELEELLEKLKSLEERLEKLEEKLEKLESELEELAEEKNELAKLL----------EERLKELEERLE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1401 ETKKKLEEDAGVAEAIEEARRRAAKDLESLSVRYEERVQACDKLEKGRTRLQQELDDVTVA---LDQQRQVVSALEKKQK 1477
Cdd:COG0419 372 ELEKELEKALERLKQLEEAIQELKEELAELSAALEEIQEELEELEKELEELERELEELEEEikkLEEQINQLESKELMIA 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1478 KFDQMLAEEKLISARYAEERDRAEADAREKETKVLSLSRAL-EEALETREEMERQNKQLRAemddLVSSKDDVGKNVHEL 1556
Cdd:COG0419 452 ELAGAGEKCPVCGQELPEEHEKELLELYELELEELEEELSReKEEAELREEIEELEKELRE----LEEELIELLELEEAL 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1557 ERFKRALEQQVQEMRAQMEELEDELQA-TEDGKLR-LEVNMQALKAQHERELQNRDDANDDKK-----KLLSKQVRELEA 1629
Cdd:COG0419 528 KEELEEKLEKLENLLEELEELKEKLQLqQLKEELRqLEDRLQELKELLEELRLLRTRKEELEElrerlKELKKKLKELEE 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1630 ELDAERKQRAQALAGRKKLEL-----DLQEAMAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEARAAREEIfIQSRES 1704
Cdd:COG0419 608 RLSQLEELLQSLELSEAENELeeaeeELESELEKLNLQAELEELLQAALEELEEKVEELEAEIRRELQRIENE-EQLEEK 686
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1033370542 1705 EKKLKNLEAELLQLQEDLAASERAKRQAQQERDDLADELAN 1745
Cdd:COG0419 687 LEELEQLEEELEQLREELEELLKKLGEIEQLIEELESRKAE 727
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1286-1963 |
1.05e-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: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 93.30 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1286 QVQELQLRAGEGERAKaelvERLVKLQNELdgvsgtlGSTESKTIKLAKDLATVESHLQDTQELLQEETRQKLNLSSRVR 1365
Cdd:pfam01576 3 QEEEMQAKEEELQKVK----EKQQKAESEL-------KELEKKHQQLCEEKNILAEQLQAETELFAEAEEMRARLAARKQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1366 QLEEEKAAMLEQLEEEEAAKANFSRQMQSLQQQVMETKKKLEEDAGVAEAIEEARRRAAKDLESLSVRYEERVQACDKLE 1445
Cdd:pfam01576 72 ELEEILHELEARLEEEEERSQQLQNEKKKMQQHIQDLEEQLEEEEAARQKLQLEKVTTEAKIKKMEEDILLLEDQNNKLQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1446 KGRTRLQQELDDVTVALDQQRQVVSALEKKQKKFDQMLAEeklisaryAEERDRAEadarEKetkvlslsraleealeTR 1525
Cdd:pfam01576 152 KERKLLEERISEFTSNLAEEEEKSKSLNKLKNKHEAMISD--------LEDRLKKE----EK----------------GR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1526 EEMERQNKQLRAEMDDLVSSKDDvgknvhelerfkraLEQQVQEMRAQMEELEDELQATEDgKLRLEVNMQALKAQHERE 1605
Cdd:pfam01576 204 QELEKAKRKLEGESSDLQEQIAE--------------LQAQIAELRAQLAKKEEELQAALA-RLEEETAQKNAALKKLRE 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1606 LQNrddanddkkkllskQVRELEAELDAERKQRAQALAGRKKLELDLQ----EAMAQLDAANkgrdeAGKQLR-KLQAQM 1680
Cdd:pfam01576 269 LEA--------------QLSELQEDLESERAARAKAEKQRRDLGEELEalktELEDTLDTTA-----AQQELRsKREQEV 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1681 KELWREVEEARAAREEIFIQSRESEKK-LKNLEAELLQLQEDLAASERAKRQAQQERDDLADELANGNSGKSALLDEKRH 1759
Cdd:pfam01576 330 TELKKALEEETRSHEAQLQEMRQKHTQaLEELTEQLEQAKRNKASLEKAKQALESENAELQAELRSLQQAKQDSEHKRKK 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1760 LEARIGQLEEELDEEQSNMELLNDRYRKLSMQVETLTTELGAERSFSQKTENARQQLERQNKDLRAKLGEmDSSVKSKYK 1839
Cdd:pfam01576 410 LEGQLQELQSRLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE-ETRQKLNLS 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1840 MAIATLESKVAQLEEQLEQESRERILSGKLVRRAEKKLKEVILQVDEERRNADQYKDQVEKGHLRLKQLKRQLEEAEEEA 1919
Cdd:pfam01576 489 SRLRQLEDEKNSLQEQLEEEEEAKRNVERQLQTLQAQLSDLKKKLEEDAGAVEALEEGRKRLQRELEALTQRLEEKAAAY 568
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1033370542 1920 SRANASRRRMQRELEDVTesaesmnREVTSLRNRLSKVERRQRK 1963
Cdd:pfam01576 569 DKLEKTKNRLQQELDDLL-------VDLDHQRQLVSNLEKKQKK 605
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1025-1586 |
1.30e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 92.80 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1025 KERKLMEERLSEFTSHMAEEEEKVKSLSKLRNKYEAVMADMEDRLKKEEKGRQELEKLKRKLDG----------EAGDLQ 1094
Cdd:PRK02224 199 KEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDlretiaeterEREELA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1095 EQVAELQQQLEELRQA-------LARKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQEDMESEKLARAKAEKQR 1167
Cdd:PRK02224 279 EEVRDLRERLEELEEErddllaeAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1168 RDLGEELEALKTELEDTldstaaqQELRSKREQEVTELKKTIEE-EVKVHEAQVldMRQRHTSALEELSEQLEQSRRFKI 1246
Cdd:PRK02224 359 EELREEAAELESELEEA-------REAVEDRREEIEELEEEIEElRERFGDAPV--DLGNAEDFLEELREERDELREREA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1247 NLEKTKQALEGENAEMQkevKLLQAAKLESEQRRKKLEGQVQELqlraGEGERAKAELVERLVKLQNELDGVsgtlgste 1326
Cdd:PRK02224 430 ELEATLRTARERVEEAE---ALLEAGKCPECGQPVEGSPHVETI----EEDRERVEELEAELEDLEEEVEEV-------- 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1327 SKTIKLAKDLATVESHLQDTQEllqeetrQKLNLSSRVRQLEEEKAAMLEQLEEEEAAKANFSRQMQSLQQQVMETKKKL 1406
Cdd:PRK02224 495 EERLERAEDLVEAEDRIERLEE-------RREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEA 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1407 EEDAGVAEAIEEARRRAAKDLESLSvRYEERVQACDKLEKGRTRLQQELDDVTVALDQQRQVVSALEKKQKKFDQMLAEE 1486
Cdd:PRK02224 568 EEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEA 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1487 KLISARyaEERDRAEA----------DAREKETKVLSLSRALEEALETREEMERQNKQLRAEMDDLvsskDDVGKNVHEL 1556
Cdd:PRK02224 647 RIEEAR--EDKERAEEyleqveekldELREERDDLQAEIGAVENELEELEELRERREALENRVEAL----EALYDEAEEL 720
|
570 580 590
....*....|....*....|....*....|.
gi 1033370542 1557 ERFKRALEqqvQEMRAQ-MEELEDELQATED 1586
Cdd:PRK02224 721 ESMYGDLR---AELRQRnVETLERMLNETFD 748
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ... |
873-1700 |
1.75e-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: 92.73 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 873 VTRQDEVMQAKAVELQKVQEKHTKTQMDLKELENKYQQLSEEKTILAEQLQAETELFAEAEEMRA-RLAARKQELEDILH 951
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYlDYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 952 ELESRVEEEEERCQQLQGDKKKMQQHVQdleeQLEEEEAARQKLQLEKVSTEAKLKKMEEDLLVLEDQNSKLHKER---- 1027
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVL----KENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKlkes 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1028 ----KLMEERLSEFTSHMAEEEEKVKSLSKLRNKYEAVMADMEDRLKKEEKGRQELEKLKRK----LDGEAGDLQEQVAE 1099
Cdd:pfam02463 320 ekekKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLeserLSSAAKLKEEELEL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1100 LQQQLEELRQALARKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQEDMESEKLARAK---AEKQRRDLGEELEA 1176
Cdd:pfam02463 400 KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKdelELKKSEDLLKETQL 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1177 LKTELEDTLDSTAAQQELRSKREQEVTELKKTIEEEVKVHEAQVLDMRQRHTSALEELSE-------------------Q 1237
Cdd:pfam02463 480 VKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVEnykvaistavivevsatadE 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1238 LEQSRRFKINLEKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGERAKAELVERLVKLQNELDG 1317
Cdd:pfam02463 560 VEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKE 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1318 VSGTLGSTESKTIKLAKDLAtvESHLQDTQELLQEETRQKLNLSSRVRQLEEEKAAMLEQLEEEEAAKANFSRQMQSLQQ 1397
Cdd:pfam02463 640 SAKAKESGLRKGVSLEEGLA--EKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1398 QVMETKKKLEEDAgVAEAIEEARRRAAKDLESLSVRYEERVQACDKLEKGRTRLQQELDDVTVALDQQRQVVSALEKKQK 1477
Cdd:pfam02463 718 EAEELLADRVQEA-QDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKL 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1478 KFDQMLAEEKLISARYAEERDRAEADAREKETKVLSLSR---ALEEALETREEMERQNKQLRAEMDDLVS-SKDDVGKNV 1553
Cdd:pfam02463 797 KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELeelALELKEEQKLEKLAEEELERLEEEITKEeLLQELLLKE 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1554 HELERFKRALEQQVQEMRAQMEELEDELQATEDGKLRLEVNmqALKAQHERELQNRDDANDDKKKLLS---KQVRELEAE 1630
Cdd:pfam02463 877 EELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKEN--EIEERIKEEAEILLKYEEEPEELLLeeaDEKEKEENN 954
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1631 LDAERKQRAQALAGRKKLELDLQEAMAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEARAAREEIFIQ 1700
Cdd:pfam02463 955 KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLE 1024
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
994-1565 |
2.16e-17 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 89.05 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 994 KLQLEKVSTEAKLKKMEEDLL-VLEDQNSKLHKERKLME----ERLSEFTSHMAEEEEKVKSLSKLRNKYEAVMADMEDR 1068
Cdd:COG0419 182 EAKAKIEELEGQLSELLEDIEdLLEALEEELKELKKLEEiqeeQEEEELEQEIEALEERLAELEEEKERLEELKARLLEI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1069 LKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQaLARKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAE 1148
Cdd:COG0419 262 ESLELEALKIREEELRELERLLEELEEKIERLEELEREIEE-LEEELEGLRALLEELEELLEKLKSLEERLEKLEEKLEK 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1149 LQEDMESEKLARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVTELKKTIEEEVKVHEAQVLDMRQRHT 1228
Cdd:COG0419 341 LESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELKEELAELSAALEEIQEELEELEKELE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1229 SALEELSEQLEQ----SRRFKINLEKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGERaKAEL 1304
Cdd:COG0419 421 ELERELEELEEEikklEEQINQLESKELMIAELAGAGEKCPVCGQELPEEHEKELLELYELELEELEEELSREKE-EAEL 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1305 VERLVKLQNELDGVSGTLGSTESKTIKLAKDLATVESHLQDTQELLQEETRQKL---------NLSSRVRQLEEEKAAML 1375
Cdd:COG0419 500 REEIEELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEELEELKEKLQlqqlkeelrQLEDRLQELKELLEELR 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1376 EQLEEEEAAKANFSR--QMQSLQQQVMETKKKLEE--DAGVAEAIEEARRRAAKDLESLSVRYEERVQACDKLEKGRTRL 1451
Cdd:COG0419 580 LLRTRKEELEELRERlkELKKKLKELEERLSQLEEllQSLELSEAENELEEAEEELESELEKLNLQAELEELLQAALEEL 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1452 QQELDdvtvALDQQRQVVSALEKKQKKFDQMLAEEKLISARYAEERDRAEaDAREKETKVLSLSRALEEALETREEMERQ 1531
Cdd:COG0419 660 EEKVE----ELEAEIRRELQRIENEEQLEEKLEELEQLEEELEQLREELE-ELLKKLGEIEQLIEELESRKAELEELKKE 734
|
570 580 590
....*....|....*....|....*....|....
gi 1033370542 1532 NKQLRAEMDDLVSSKDDVGKNVHELERFKRALEQ 1565
Cdd:COG0419 735 LEKLEKALELLEELREKLGKAGLRADILRNLLAQ 768
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1136-1880 |
3.98e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 88.66 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1136 LKSLRELQAQLAELQEDMESEKLARAKAEKQRRdlgEELEALKTELEDTLDSTAAQQELRSKREQEVTELKKTIEEEVKV 1215
Cdd:PTZ00121 1084 KEDNRADEATEEAFGKAEEAKKTETGKAEEARK---AEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKA 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1216 HEAQVLDMRQRHTSALE-ELSEQLEQSRRFKiNLEKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRA 1294
Cdd:PTZ00121 1161 EDARKAEEARKAEDAKKaEAARKAEEVRKAE-ELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDA 1239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1295 GEGERAKAELVERLVKLQNELDGVSGTLGSTESKTIKLAKdlatveshlqdTQELLQEETRQKlnlSSRVRQLEEEKAAM 1374
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK-----------ADELKKAEEKKK---ADEAKKAEEKKKAD 1305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1375 LEQLEEEEAAKAN-FSRQMQSLQQQVMETKKKLEEDAGVAEAIEEARRRAAKDLESLSVRYEERVQACDKLEKGRTRLQQ 1453
Cdd:PTZ00121 1306 EAKKKAEEAKKADeAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1454 ELDDVTVAlDQQRQVVSALEKKQKKFDQMLAEEKLI--SARYAEERDRAEaDAREKETKVLSLSRALEEALETREEMERQ 1531
Cdd:PTZ00121 1386 KAEEKKKA-DEAKKKAEEDKKKADELKKAAAAKKKAdeAKKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEEAKKAEEAK 1463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1532 NKQLRAEMDDLVSSKDDVGKNVHELERFKRALEQQVQEMRAQMEELE--DELQATEDGKLRLEVNM--QALKAQHERELQ 1607
Cdd:PTZ00121 1464 KKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkaDEAKKAEEAKKADEAKKaeEAKKADEAKKAE 1543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1608 NRDDANDDKKkllSKQVRELEAELDAERKQRAQAlagRKKLELDLQEAMAQldaANKGRDEAGKQLRKLQAQMK-ELWRE 1686
Cdd:PTZ00121 1544 EKKKADELKK---AEELKKAEEKKKAEEAKKAEE---DKNMALRKAEEAKK---AEEARIEEVMKLYEEEKKMKaEEAKK 1614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1687 VEEARAAREEifIQSRESEKK----LKNLEAELLQLQEDL-AASERAKRQAQQERDDLADELANGNSGKSALLDEKRHLE 1761
Cdd:PTZ00121 1615 AEEAKIKAEE--LKKAEEEKKkveqLKKKEAEEKKKAEELkKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1762 ArigqlEEELDEEQSNMELLNDRYRKLSMQVETLTTElgaERSFSQKTENARQQLE---RQNKDLRAKLGE---MDSSVK 1835
Cdd:PTZ00121 1693 A-----LKKEAEEAKKAEELKKKEAEEKKKAEELKKA---EEENKIKAEEAKKEAEedkKKAEEAKKDEEEkkkIAHLKK 1764
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1033370542 1836 SKYKMAIATLESKVAQLEEQLEQESRERILSgklvrrAEKKLKEV 1880
Cdd:PTZ00121 1765 EEEKKAEEIRKEKEAVIEEELDEEDEKRRME------VDKKIKDI 1803
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1162-1714 |
5.32e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 87.43 E-value: 5.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1162 KAEKQRRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVTELKKTIEEEVKVheaqvldmrqrhtsaLEELSEQLEQS 1241
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSE---------------LPELREELEKL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1242 RRFKINLEKTKQALEG---ENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGE--RAKAELVERLVKLQNE-- 1314
Cdd:PRK03918 227 EKEVKELEELKEEIEElekELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEyl 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1315 --LDGVSGTLGSTESK---TIKLAKDLATVESHLQDTQELLQEETRQKLNLSSRVRQLEEEKAAMLEQLEEEEAAKANfs 1389
Cdd:PRK03918 307 deLREIEKRLSRLEEEingIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGL-- 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1390 rqmqslqqQVMETKKKLEEDAGVAEAIEEARRRAAKDLESLSVRYEERVQACDKLEKGR-------------------TR 1450
Cdd:PRK03918 385 --------TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelteehrkellEE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1451 LQQELDDVTVALDQQRQVVSALEKKQKKFDQMLAEEKLISARYAEERDRAEADAREKETKVLSLSRALEEALETREEMER 1530
Cdd:PRK03918 457 YTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIK 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1531 QNKQLRA------EMDDLVSSKDDVGKNVHELERFKRALEQQVQEMR-AQMEELEDELQATE----------DGKLRLEV 1593
Cdd:PRK03918 537 LKGEIKSlkkeleKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEpfyneylelkDAEKELER 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1594 NMQALKAQHERELQNRDDANDDKKKL--LSKQVRELEAELDAERKQRAQALagRKKLELDLQEAMAQLDAANKGRDEAGK 1671
Cdd:PRK03918 617 EEKELKKLEEELDKAFEELAETEKRLeeLRKELEELEKKYSEEEYEELREE--YLELSRELAGLRAELEELEKRREEIKK 694
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1033370542 1672 QLRKLQAQ---MKELWREVEEARAAREEIfIQSRESEKKLKNLEAE 1714
Cdd:PRK03918 695 TLEKLKEEleeREKAKKELEKLEKALERV-EELREKVKKYKALLKE 739
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1390-1965 |
1.31e-16 |
|
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: 86.65 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1390 RQMQSLQQQVMETKKKLEedagVAEAIEEARRR-AAKDLESLSVRYEERVQACDKLEKGRTRLQQELDDVTVALDQQRQV 1468
Cdd:TIGR02168 200 RQLKSLERQAEKAERYKE----LKAELRELELAlLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1469 VSALEKK----QKKFDQMLAEEKLISAR---YAEERDRAEADAREKETKVLSLSRALEEALETREEMERQNKQLRAEMDD 1541
Cdd:TIGR02168 276 VSELEEEieelQKELYALANEISRLEQQkqiLRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1542 LVSSKDDVGKNVHELERFKRALEQQVQEMRAQMEELEDELQATEDGKLRLEVNMQALKAQHERELQNRDDANddkKKLLS 1621
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL---KKLEE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1622 KQVRELEAELDAERKQRAQALAGRKKLELDLQEAMAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEARAAREEI--FI 1699
Cdd:TIGR02168 433 AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVkaLL 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1700 QSRESEKKLKNLEAELLQLQED----LAASERAKRQA-----QQERDDLADELANGNSGKSALLDEKRHLEARI-GQLEE 1769
Cdd:TIGR02168 513 KNQSGLSGILGVLSELISVDEGyeaaIEAALGGRLQAvvvenLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIqGNDRE 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1770 ELDEEQSNMELLND------RYRKL-------SMQVETLTT------ELGAERSF-----------------SQKTENAR 1813
Cdd:TIGR02168 593 ILKNIEGFLGVAKDlvkfdpKLRKAlsyllggVLVVDDLDNalelakKLRPGYRIvtldgdlvrpggvitggSAKTNSSI 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1814 QQLERQNKDLRAKLGEMDSSVKSKyKMAIATLESKVAQLEEQLEQESRERILSGKLVRRAEKKLKEVILQVDEERRNADQ 1893
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAEL-EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1033370542 1894 YKDQVEKGHLRLKQLKRQLEEAEEEASRANASRRRMQRELEDVTESAESMNREVTSLRNRLSKVERRQRKRT 1965
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1198-1964 |
1.59e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 86.73 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1198 REQEVTELKKTIEEEVKVH-EAQVLDMRQRHTSALEELSEQLEQSRRFKINLEKTKQALEGENAEMQK--EVKLLQAAKL 1274
Cdd:PTZ00121 1043 KEKDIIDEDIDGNHEGKAEaKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKaeEARKAEEAKK 1122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1275 ESEQRRKKLEGQVQELQLRAGEGERAKAELVERLVKLQNELDGVSGTLGSTESKTIKLAKDLATVeshlQDTQELLQEET 1354
Cdd:PTZ00121 1123 KAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEV----RKAEELRKAED 1198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1355 RQKLnlsSRVRQLEEEKAAmleqleeEEAAKANFSRQMQSLQQqvMETKKKLEEDAGVAEaiEEARRRAAKDLESLSVRY 1434
Cdd:PTZ00121 1199 ARKA---EAARKAEEERKA-------EEARKAEDAKKAEAVKK--AEEAKKDAEEAKKAE--EERNNEEIRKFEEARMAH 1264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1435 EERVQACDKLEKGRtrlqqelddvtvaldQQRQVVSALEKKQkkfdqmlAEEklisARYAEERDRAEADAREKETKvlsl 1514
Cdd:PTZ00121 1265 FARRQAAIKAEEAR---------------KADELKKAEEKKK-------ADE----AKKAEEKKKADEAKKKAEEA---- 1314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1515 sRALEEALETREEMERQNKQLRAEMDDlVSSKDDVGKNvhELERFKRALEQQVQEMRAQMEELEDELQATEDGKLRLEVN 1594
Cdd:PTZ00121 1315 -KKADEAKKKAEEAKKKADAAKKKAEE-AKKAAEAAKA--EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK 1390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1595 MQALKAQHERElQNRDDANDDKKKLLSKQVRElEAELDAERKQRAQALagRKKLELDLQEAMAQLDAANKGRDEAGKQLR 1674
Cdd:PTZ00121 1391 KKADEAKKKAE-EDKKKADELKKAAAAKKKAD-EAKKKAEEKKKADEA--KKKAEEAKKADEAKKKAEEAKKAEEAKKKA 1466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1675 KLQAQMKELWREVEEARAArEEIFIQSRESEKKlknleaellqlQEDLAASERAKRQAQQERDdlADELANGNSGKSAll 1754
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEAKKA-DEAKKKAEEAKKK-----------ADEAKKAAEAKKKADEAKK--AEEAKKADEAKKA-- 1530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1755 DEKRHLEarigqleeeldeeqsnmELLNDRYRKLSMQVETLTTELGAERSfsQKTENARQQLERQNKDLRaKLGEMDSSV 1834
Cdd:PTZ00121 1531 EEAKKAD-----------------EAKKAEEKKKADELKKAEELKKAEEK--KKAEEAKKAEEDKNMALR-KAEEAKKAE 1590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1835 KSKYKMAIATLESKVAQLEEQLEQESRERILSGKLVRRAE--KKLKEVILQVDEERRNADQYKDQVEKGHLRLKQLKRQL 1912
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEekKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA 1670
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1033370542 1913 EEAEEEASRAnasrrrmQRELEDVTESAESMNREVTSLRN--RLSKVERRQRKR 1964
Cdd:PTZ00121 1671 EEDKKKAEEA-------KKAEEDEKKAAEALKKEAEEAKKaeELKKKEAEEKKK 1717
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
872-1475 |
1.24e-15 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 83.29 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 872 QVTRQDEVMQAKAVELQKVQEKHTKTQMDLKELENKYQQLSEEKTilaEQLQAETELFAEAEEMRARLaarKQELEDILh 951
Cdd:pfam01576 514 NVERQLQTLQAQLSDLKKKLEEDAGAVEALEEGRKRLQRELEALT---QRLEEKAAAYDKLEKTKNRL---QQELDDLL- 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 952 eleSRVEEEEERCQQLQGDKKKMQQHVQDLEEQLEEEEAARQKLQLEKVSTEAKLKKMEEDLLVLEDQNSKLHKERKLME 1031
Cdd:pfam01576 587 ---VDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETKALSLARALEEALDAKEELERQNKQLR 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1032 ERLSEFTSHMAEEEEKVKSLSKLRNKYEAVMADM-------EDRLKKEEKGRQELE--------KLKRKLDG--EAGD-- 1092
Cdd:pfam01576 664 AEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMktqleelEDELQATEDAKLRLEvnmqalkaQFERDLQArdEQGEek 743
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1093 ---LQEQVAELQQQLEELR----QALARK---EAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQEDMESEKLARAK 1162
Cdd:pfam01576 744 rrqLVKQVRELEAELEDERkqraQAVAAKkklELDLKELEAQIEAANKGRDEAVKQLKKLQAQMKDLQRELDEARASRDE 823
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1163 AEKQRRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVTELKKTIEEEVKVHEAQVLDMRQ---RHTSALEELSEQLE 1239
Cdd:pfam01576 824 IFAQSKESEKKLKSLEAELLQLQEDLAAAERARRQAQQERDELAEEIASGNSGKSALLDEKRRleaRIAQLEEELEEEQS 903
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1240 QSRRFKINLEKTKQALEGENAEMQKEVKLLQaaklESEQRRKKLEGQVQELQLRAGEGErakaelverlvklqneldgvs 1319
Cdd:pfam01576 904 NTELLNDRLRKLTLQVEQLTTELAAERSTSQ----KSESARQQLERQNKELKAKLQEME--------------------- 958
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1320 GTLGSTESKTIklakdlATVESHLQDTQELLQEETRQKLNLSSRVRQLEEEKAAMLEQLEEEEAAKANFSRQMQSLQQQV 1399
Cdd:pfam01576 959 GTVKSKYKSSI------AALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRNADQYKDQAEKGNSRL 1032
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1033370542 1400 METKKKLEedagvaEAIEEARRRAAkdleslsvryeervqacdklekGRTRLQQELDDVTVALDQQRQVVSALEKK 1475
Cdd:pfam01576 1033 KQLKRQLE------EAEEEASRANA----------------------ARRKLQRELDDATESAEAMNREVTTLRSK 1080
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
854-1570 |
1.25e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 83.65 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 854 KLRHWQWWRLFTKVKPLLQVTRQDEVM---QAKAVELQKVQEKHTKTQMDLKELENKYQQLSEEktilAEQLQAETELFA 930
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKaeeARKADELKKAEEKKKADEAKKAEEKKKADEAKKK----AEEAKKADEAKK 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 931 EAEEMRARLAARKQELEDILHELESRVEEEEERCQQLQGDKKKMQ-QHVQDLEEQLEEeEAARQKLQLEKVSTEAKlKKM 1009
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaAEKKKEEAKKKA-DAAKKKAEEKKKADEAK-KKA 1400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1010 EEDLLVLEDQNSKLHKERKLMEERLSEFTSHMAEE----EEKVKSLSKLRNKYEAVMADMEDRLKKEEKGRQELEKLKRK 1085
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEakkkAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE 1480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1086 LDGEAGDLQEQVAELQQQLEELRQAlarKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQEDMESEKLARAKAEK 1165
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKA---AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL 1557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1166 QRRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVTELKKTIEEEVKVHEAQVLDMRQRHTSAlEELSEQLEQSRRF- 1244
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA-EELKKAEEEKKKVe 1636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1245 ---KINLEKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQElqlragEGERAKAELVERLVKLQNELDGVSgt 1321
Cdd:PTZ00121 1637 qlkKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE------EDEKKAAEALKKEAEEAKKAEELK-- 1708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1322 lgSTESKTIKLAKDLATVESHLQDTQELLQEETRQKLNLSSRVRQLEEEKAAMLEQLEEEEAAKANFSRQMQSLQQQvmE 1401
Cdd:PTZ00121 1709 --KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE--E 1784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1402 TKKKLEEDAGVAEaieearrRAAKDLES-LSVRYEERVQACDKLEKGRTRLQQELDDVTVALDQQRQVVSALEKKQKKFD 1480
Cdd:PTZ00121 1785 LDEEDEKRRMEVD-------KKIKDIFDnFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKN 1857
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1481 QMLAEEKLISARYAEERDRAEADAREKETkvlslSRALEEALETREEMERQNKQLRAEMDDLVSSKDDVGknvhelERFK 1560
Cdd:PTZ00121 1858 NENGEDGNKEADFNKEKDLKEDDEEEIEE-----ADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKD------EYIK 1926
|
730
....*....|
gi 1033370542 1561 RALEQQVQEM 1570
Cdd:PTZ00121 1927 RDAEETREEI 1936
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
1331-1897 |
1.22e-14 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 79.80 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1331 KLAKDLATVESHLQDTQELLQEETRQKLNLSS-RVRQLEEEKAAMLEQLEEEEAAKANFSRQMQSLQQQVMETKKKLEED 1409
Cdd:COG0419 189 ELEGQLSELLEDIEDLLEALEEELKELKKLEEiQEEQEEEELEQEIEALEERLAELEEEKERLEELKARLLEIESLELEA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1410 AGVAEAIEEARRRAAKDLESLSVRYEERVQACDKLEKGRTRLQQELDDVTVALDQQRQVVSALEKKQKKFDQMLAEEKLI 1489
Cdd:COG0419 269 LKIREEELRELERLLEELEEKIERLEELEREIEELEEELEGLRALLEELEELLEKLKSLEERLEKLEEKLEKLESELEEL 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1490 SARYAEERDRAEADAREKETKVLSLSRALEEALETREEMERQNKQLRAEMDDLVSSKDDVGKNVHELERFKRALEQQVQE 1569
Cdd:COG0419 349 AEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELKEELAELSAALEEIQEELEELEKELEELERELEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1570 MRAQMEELEDELQATEDGKLRLEVNMQA-------------LKAQHERELQNRDDANDDKKKLLSKQVRELEAELDAERK 1636
Cdd:COG0419 429 LEEEIKKLEEQINQLESKELMIAELAGAgekcpvcgqelpeEHEKELLELYELELEELEEELSREKEEAELREEIEELEK 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1637 QRAQALAGRKKLELDLQEAMAQLDAANKGRDEAGKQLR---------KLQAQMKELWREVEEARAAREEiFIQSRESEKK 1707
Cdd:COG0419 509 ELRELEEELIELLELEEALKEELEEKLEKLENLLEELEelkeklqlqQLKEELRQLEDRLQELKELLEE-LRLLRTRKEE 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1708 LKNLEAELLQLQEDLAASERAKRQAQQERDDLadELANGNSGKSALLDEKRHLEARIGQLEEELDEEQSNMELLNDRYRK 1787
Cdd:COG0419 588 LEELRERLKELKKKLKELEERLSQLEELLQSL--ELSEAENELEEAEEELESELEKLNLQAELEELLQAALEELEEKVEE 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1788 LSMQVETLTTELGAERSFSQKTENArQQLERQNKDLRAKLGEMDSSvKSKYKMAIATLESKVAQLEEQLEQESRERILsG 1867
Cdd:COG0419 666 LEAEIRRELQRIENEEQLEEKLEEL-EQLEEELEQLREELEELLKK-LGEIEQLIEELESRKAELEELKKELEKLEKA-L 742
|
570 580 590
....*....|....*....|....*....|
gi 1033370542 1868 KLVRRAEKKLKEVILQVDEERRNADQYKDQ 1897
Cdd:COG0419 743 ELLEELREKLGKAGLRADILRNLLAQIEAE 772
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
862-1430 |
1.68e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 79.34 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 862 RLFTKVKPLLQVTRQDEVMQAKAVELQKVQEKHTKTQMDLKELENKYQQLSEEKTILAEQLQAETELFAEAEEMRARLAA 941
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 942 RKQELEDILhelesrveeeeERCQQLQGDKKKMqqhvqdleeqleeeeaarQKLQLEKVSTEAKLKKMEEDLlvledqnS 1021
Cdd:PRK03918 274 EIEELEEKV-----------KELKELKEKAEEY------------------IKLSEFYEEYLDELREIEKRL-------S 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1022 KLHKERKLMEERLSEFTSHMAEEEEKVKSLSKLRNKYEAvmadMEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQ 1101
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEE----LEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1102 QQLEELRQALARKEAELQAALARVEDEAAQKNAVLKSLRELQAQL----AELQEDMESEKLARAKAE-----KQRRDLGE 1172
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgRELTEEHRKELLEEYTAElkrieKELKEIEE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1173 ELEALKTELEDTLDSTAAQQELRskREQEVTELKKTIEEEVKVHEAQVLDMRQRHTSALEELSEQLE-QSRRFKINLEKt 1251
Cdd:PRK03918 474 KERKLRKELRELEKVLKKESELI--KLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKgEIKSLKKELEK- 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1252 KQALEGENAEMQKEVKLLQA--AKLESEQRR------KKLEGQVQELQ------LRAGEGERAKAELVERLVKLQNELDG 1317
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEelAELLKELEElgfesvEELEERLKELEpfyneyLELKDAEKELEREEKELKKLEEELDK 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1318 VSGTLGSTESKTIKLAKDLATVESHLqdTQELLQEETRQKLNLSSRVRQLEEEKaamleqleeeeaakanfsRQMQSLQQ 1397
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELEKKY--SEEEYEELREEYLELSRELAGLRAEL------------------EELEKRRE 690
|
570 580 590
....*....|....*....|....*....|...
gi 1033370542 1398 QVMETKKKLEEDagvaeaiEEARRRAAKDLESL 1430
Cdd:PRK03918 691 EIKKTLEKLKEE-------LEEREKAKKELEKL 716
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1393-1899 |
4.25e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.16 E-value: 4.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1393 QSLQQQVMETKKKLEEDAGVAEAIEEARRRAAKDLESLSV---RYEERvqacdklekgrtrlQQELDDVTVALDQQRQVV 1469
Cdd:PRK02224 202 KDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEvleEHEER--------------REELETLEAEIEDLRETI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1470 SALEKKQKKFDQMLAEEKLISARYAEERDRAEADAreketkvlSLSRALEEALETR-EEMERQNKQLRAEMDDLVSSKDD 1548
Cdd:PRK02224 268 AETEREREELAEEVRDLRERLEELEEERDDLLAEA--------GLDDADAEAVEARrEELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1549 VGKNVHELERFKRALEQQVQEMRAQMEELEDELQATEDgklrlevnmqalkAQHERElqnrddanddkkkllsKQVRELE 1628
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEELREEAAELESELEEARE-------------AVEDRR----------------EEIEELE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1629 AELDAERKQRAQAlagrkklELDLQEAMAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEARAAREE------------ 1696
Cdd:PRK02224 391 EEIEELRERFGDA-------PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpveg 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1697 --IFIQSRESEKKLKNLEAELLQLQEDLAASErakrqaqqERDDLADELANGNSGKSALLDEKRHLEARIGQLEEELDEE 1774
Cdd:PRK02224 464 spHVETIEEDRERVEELEAELEDLEEEVEEVE--------ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEK 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1775 QSNMELLNDRyrklsmqVETLTTELGAERSFSQKTENARQQLERQNKDLRAKLGEMDSSVKSKYKMA-----IATLESKV 1849
Cdd:PRK02224 536 RERAEELRER-------AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRtllaaIADAEDEI 608
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1033370542 1850 AQLEEQLEQ------ESRERiLSGKLVRRAEKKLK---EVILQVDEERRNADQYKDQVE 1899
Cdd:PRK02224 609 ERLREKREAlaelndERRER-LAEKRERKRELEAEfdeARIEEAREDKERAEEYLEQVE 666
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1050-1739 |
7.08e-14 |
|
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: 77.57 E-value: 7.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1050 SLSKLRNKYEAVMADMEDRLKKEEKGRQELEKLKRKLDGE--------AGDLQEQVAELQQQLEELRQALARKEAELQAA 1121
Cdd:pfam12128 259 RLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQwkekrdelNGELSAADAAVAKDRSELEALEDQHGAFLDAD 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1122 LARVEDEAAQKNAVLKSLRELQAQLAEL---QEDMESEKLARAKAEKQR--RDLG----------EELEALKTELEDTLD 1186
Cdd:pfam12128 339 IETAAADQEQLPSWQSELENLEERLKALtgkHQDVTAKYNRRRSKIKEQnnRDIAgikdklakirEARDRQLAVAEDDLQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1187 stAAQQELRSKREQEVTELKktIEEEVKVHEAQVLDMRQRHTSALEELSEQLEQsrrFKINLEKTKQALEGENAEMQKEV 1266
Cdd:pfam12128 419 --ALESELREQLEAGKLEFN--EEEYRLKSRLGELKLRLNQATATPELLLQLEN---FDERIERAREEQEAANAEVERLQ 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1267 KLLQAAKLESEQRRKKLEGQVQELQLRAGEGERAKAELVER----LVKLQNELDGVSGTLGSTESKTIKLAKDLATVESH 1342
Cdd:pfam12128 492 SELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQagtlLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWD 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1343 LQDTQEL------LQEETRQKLNLSSRVRQLEEEKAAMLEQLEEEEAAKANFSRQMQSLQQQVMETKKKLEEDAGVAEAI 1416
Cdd:pfam12128 572 GSVGGELnlygvkLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNA 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1417 EEARRRAAKDLESLSvryeervqacDKLEKGRTRLQQELDDVTVALDQQRQVvsaLEKKQKKFDQMLAEEKLisaryaEE 1496
Cdd:pfam12128 652 RLDLRRLFDEKQSEK----------DKKNKALAERKDSANERLNSLEAQLKQ---LDKKHQAWLEEQKEQKR------EA 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1497 RDRAEADARE-KETKVLSLSRALEEALETREEMERQNKQLRAEMDDLVSSKDDVGKNVHELERFKRALEQQVQEMRAQME 1575
Cdd:pfam12128 713 RTEKQAYWQVvEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQ 792
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1576 ELedelqatedgkLRLEVNMQALKAQHERELQNRddanddkKKLLSKQVRELEAELdaeRKQRAQAlagrkklELDLQEA 1655
Cdd:pfam12128 793 EV-----------LRYFDWYQETWLQRRPRLATQ-------LSNIERAISELQQQL---ARLIADT-------KLRRAKL 844
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1656 MAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEARAAREEIFIQSResekklknleaeLLQLQEDLAASERAKRQAQQE 1735
Cdd:pfam12128 845 EMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGER------------LAQLEDLKLKRDYLSESVKKY 912
|
....
gi 1033370542 1736 RDDL 1739
Cdd:pfam12128 913 VEHF 916
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
992-1735 |
7.15e-14 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 77.45 E-value: 7.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 992 RQKLQLEKVSTEAKlKKMEEDLLvlEDQNSKLHKERKLM---EERLSEFTSHMAEEEEkvkslSKLRNKYEAvmaDMEDR 1068
Cdd:pfam15921 144 RNQLQNTVHELEAA-KCLKEDML--NDSNTQIEQLRKMMlshEGVLQEIRSILVDFEE-----ASGKKIYEH---DSMST 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1069 LKKEEKGrQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARK-EAELQAALARVEDEAAQKNAVLKSLRE----LQ 1143
Cdd:pfam15921 213 IHFRSLG-SAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKiELLLQQHQDRIEQLISEHEVEITGLTEkassAR 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1144 AQLAELQEDMES-EKLARAKAEKQRRDLGEelealkteledtLDSTAAQqeLRSkreqEVTELKKTIEEEVKVHEAQVLD 1222
Cdd:pfam15921 292 SQANSIQSQLEIiQEQARNQNSMYMRQLSD------------LESTVSQ--LRS----ELREAKRMYEDKIEELEKQLVL 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1223 MRQRHTSALEELSEQLEQSRrfkiNLEKTKQALEGENAEMQKEVKLlqaaklESEQRRK----------KLEGQVQELQL 1292
Cdd:pfam15921 354 ANSELTEARTERDQFSQESG----NLDDQLQKLLADLHKREKELSL------EKEQNKRlwdrdtgnsiTIDHLRRELDD 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1293 RAGEGERAKAELVERLVKLQNELDGVSGTLGSTESKTIKLAKDLATVESHLQDTQELLQEETRQKLNLSSRVRQLEEEKA 1372
Cdd:pfam15921 424 RNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTA 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1373 AMLEQLEEEEAAKANFSRQMQSLQQQVMETKKKLEEdagvaeaiEEARRRAAKDLESLSVRYEERvqacdklEKGRTRLQ 1452
Cdd:pfam15921 504 SLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE--------GDHLRNVQTECEALKLQMAEK-------DKVIEILR 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1453 QELDDVTVALDQQRQVVSALEKKQKKFDQMLAEEKLISARYAEERDRAEADAREKETKVLSLSRALEEALETREEMERQN 1532
Cdd:pfam15921 569 QQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAV 648
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1533 KQLRAEMDDLV----SSKDDVGKNVHELERFKRALEQQVQEMRAQMEELEDELQATEDgklRLEVNMQALKAQHERELQN 1608
Cdd:pfam15921 649 KDIKQERDQLLnevkTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQS---ELEQTRNTLKSMEGSDGHA 725
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1609 RDDANDDKKKLLSKqvreleaeldaerkqRAQALAGRKKLELdLQEAMAQldaANKGRDEAGKQLRKLQAQMKELWREVE 1688
Cdd:pfam15921 726 MKVAMGMQKQITAK---------------RGQIDALQSKIQF-LEEAMTN---ANKEKHFLKEEKNKLSQELSTVATEKN 786
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1033370542 1689 EARAAREEIFIQSRESEKKLKNLEAELLQLQEDLAASERAKRQAQQE 1735
Cdd:pfam15921 787 KMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQE 833
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1025-1788 |
1.48e-13 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 76.53 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1025 KERKLMEERLSEFtshMAEEEEKVKSLSKLRNKYEAVmadmEDRLKKEEKGRQELEKLKRkldgeagdLQEQVAELQQQL 1104
Cdd:PRK04863 300 RQLAAEQYRLVEM---ARELAELNEAESDLEQDYQAA----SDHLNLVQTALRQQEKIER--------YQADLEELEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1105 EElrQALARKEAELQAALARVEDEAAQKnavlkSLRELQAQLAELQEDMESEKlARAKAEKQRRDLGEELEALKTELEDT 1184
Cdd:PRK04863 365 EE--QNEVVEEADEQQEENEARAEAAEE-----EVDELKSQLADYQQALDVQQ-TRAIQYQQAVQALERAKQLCGLPDLT 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1185 LDSTAAQQELRSKREQEVTELKKTIEEEVKVHEAqvldMRQRHTSALEELS----------------EQLEQSRRFKINL 1248
Cdd:PRK04863 437 ADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQA----AHSQFEQAYQLVRkiagevsrseawdvarELLRRLREQRHLA 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1249 EKTkQALEGENAEMQKEvkllqaakLESEQRrkkLEGQVQELQLRAGEGERAKAELVERLVKLQNELDGVSGTLGStesk 1328
Cdd:PRK04863 513 EQL-QQLRMRLSELEQR--------LRQQQR---AERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSE---- 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1329 tikLAKDLATVESHLQDTQELLQEETRQK---LNLSSRVRQLEEEKAAMLEQleeeeaakanfSRQMQSLQQQVMETKKK 1405
Cdd:PRK04863 577 ---ARERRMALRQQLEQLQARIQRLAARApawLAAQDALARLREQSGEEFED-----------SQDVTEYMQQLLERERE 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1406 LEEdagVAEAIEEARRRAAKDLESLSVR---YEERVQA-CDKLekGRTRLQQELDDVTV--------ALDQQRQ--VVSA 1471
Cdd:PRK04863 643 LTV---ERDELAARKQALDEEIERLSQPggsEDPRLNAlAERF--GGVLLSEIYDDVSLedapyfsaLYGPARHaiVVPD 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1472 LEKKQkkfDQMLAEEKLISARYAEERD-------RAEADAREKETKV------LSLSRALEEALETREEMERQNKQLRAE 1538
Cdd:PRK04863 718 LSDAA---EQLAGLEDCPEDLYLIEGDpdsfddsVFSVEELEKAVVVkiadrqWRYSRFPEVPLFGRAAREKRIEQLRAE 794
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1539 MDDLVSSKDDVGKNVHELER----FKRAL------------EQQVQEMRAQMEELEDELQATEDGKLRLEVNMQALKAQH 1602
Cdd:PRK04863 795 REELAERYATLSFDVQKLQRlhqaFSRFIgshlavafeadpEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGL 874
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1603 ERELQNRDDANDDKKKLLSKQVRELEAELD----AER--KQRAQALAGRKKLELDLQEAMAQLDAANKGRDEAGKQLRKL 1676
Cdd:PRK04863 875 SALNRLLPRLNLLADETLADRVEEIREQLDeaeeAKRfvQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDA 954
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1677 QAQ----------------------------MKELWRE-VEEARAAREEIFIQSRESEKKLknleAELLQLQEDLAASER 1727
Cdd:PRK04863 955 KQQafaltevvqrrahfsyedaaemlaknsdLNEKLRQrLEQAEQERTRAREQLRQAQAQL----AQYNQVLASLKSSYD 1030
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1728 AKRQ----AQQERDDL-----ADELANGNSGKSALLDEKRHLEARIGQLEEELDEEQSNMELLNDRYRKL 1788
Cdd:PRK04863 1031 AKRQmlqeLKQELQDLgvpadSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKL 1100
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1559-1960 |
1.50e-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: 76.65 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1559 FKRALEQQVQEMrAQMEELEDELQATEDgklrlEVNMQALKAQHERELQNRDDANDDKK-----KLLSKQVRELEAELDA 1633
Cdd:TIGR02169 168 FDRKKEKALEEL-EEVEENIERLDLIID-----EKRQQLERLRREREKAERYQALLKEKreyegYELLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1634 ERKQRAQALAGRKKLELDLQEAMAQLDAANKGRDEAGKQLRKL--------QAQMKELWREVEEARAAREEIFIQSRESE 1705
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1706 KKLKNLEAELLQLQEDLAASERAKRQAQQERDDLADELANgnsgksaLLDEKRHLEARIGQLEEEldeeqsnmellNDRY 1785
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE-------LKEELEDLRAELEEVDKE-----------FAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1786 RKLSMQVETLTTELGAERSFSQKTENARQQLERQnkdLRAKLGEMdssvkskyKMAIATLESKVAQLEEQLEQESREril 1865
Cdd:TIGR02169 384 RDELKDYREKLEKLKREINELKRELDRLQEELQR---LSEELADL--------NAAIAGIEAKINELEEEKEDKALE--- 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1866 sgklVRRAEKKLKEVILQVDEERRNADQYKDQVEKGHLRLKQLKRQLeeaEEEASRANASRRRmQRELEDVTESAESMNR 1945
Cdd:TIGR02169 450 ----IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL---AEAEAQARASEER-VRGGRAVEEVLKASIQ 521
|
410
....*....|....*
gi 1033370542 1946 EVTSLRNRLSKVERR 1960
Cdd:TIGR02169 522 GVHGTVAQLGSVGER 536
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
886-1370 |
1.71e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 76.23 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 886 ELQKVQEKHTKTqmDLKELENKYQQLSEEKTILAEQLQAETELFAEAEEMRARLAARKQELEDILHELESRVEEEEERCQ 965
Cdd:PRK02224 226 EEQREQARETRD--EADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 966 QLQGDKKKMQQHVQDLEeqlEEEEAARQKLQLEKVSTEAKLKKME---EDLLVLEDQNSKLHKERKLMEERLSEFTSHMA 1042
Cdd:PRK02224 304 LDDADAEAVEARREELE---DRDEELRDRLEECRVAAQAHNEEAEslrEDADDLEERAEELREEAAELESELEEAREAVE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1043 EEEEKVKSLsklrnkyEAVMADMEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQAAL 1122
Cdd:PRK02224 381 DRREEIEEL-------EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGK 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1123 ARVEDEAAQKNAVLKSLRELQAQLAELQEDMESEKLARAKAEKqRRDLGEELEALKTELEDTLDSTAAQQELRSKREQEV 1202
Cdd:PRK02224 454 CPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEE-RLERAEDLVEAEDRIERLEERREDLEELIAERRETI 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1203 TELKKTIE---EEVKVHEAQVLDMRQRHTSALEELSEQLEQSRRFKINLEKTKQALEGENAemqkeVKLLQAAKLESEQR 1279
Cdd:PRK02224 533 EEKRERAEelrERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-----IRTLLAAIADAEDE 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1280 RKKLEGQVQELQLRAGEGERAKAELVERLVKLQNELDgvsgtlgstESKTIKLAKDLATVESHLQDTQELLQEETRQKLN 1359
Cdd:PRK02224 608 IERLREKREALAELNDERRERLAEKRERKRELEAEFD---------EARIEEAREDKERAEEYLEQVEEKLDELREERDD 678
|
490
....*....|.
gi 1033370542 1360 LSSRVRQLEEE 1370
Cdd:PRK02224 679 LQAEIGAVENE 689
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
872-1715 |
3.18e-13 |
|
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: 75.47 E-value: 3.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 872 QVTRQDEVMQAKAVELQKVQEKhtktQMDLKELENKYQQLSEEKTILAEQLQAETELFAEAEEMRAR-LAARKQELEDIL 950
Cdd:TIGR00606 232 QLESSREIVKSYENELDPLKNR----LKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKvFQGTDEQLNDLY 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 951 HELESRVEEEEERCQQLQGDKKKMQQHVQDLEEQLEEEEAARQKLQLEKVSTEAKLKKMEEDLLVLEDQNSKLHKERKLM 1030
Cdd:TIGR00606 308 HNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPF 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1031 EERLSEFTSHMAEE--EEKVKSLSKLrnkyeavMADMEDRLKKEEKGRQELE----KLKRKLDGEAGDLQEQVAELQQQL 1104
Cdd:TIGR00606 388 SERQIKNFHTLVIErqEDEAKTAAQL-------CADLQSKERLKQEQADEIRdekkGLGRTIELKKEILEKKQEELKFVI 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1105 EELRQA------LARKEAELQAALArvEDEAAQKNAVLKSLRELQAQLAELQEDMESEKLARAKAEKQrrdLGEELEALK 1178
Cdd:TIGR00606 461 KELQQLegssdrILELDQELRKAER--ELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQ---LNHHTTTRT 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1179 TELEDTLDSTAAQQELRSKREQEVTEL---------KKTIEEEVKVHEAQVLDMRQRHTSALEELsEQLEQSRRFKINLE 1249
Cdd:TIGR00606 536 QMEMLTKDKMDKDEQIRKIKSRHSDELtsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKEL-ASLEQNKNHINNEL 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1250 KTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGE------------------------RAKAELV 1305
Cdd:TIGR00606 615 ESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAvysqfitqltdenqsccpvcqrvfQTEAELQ 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1306 ERLVKLQNELDGVSGTLGSTESKTIKLAKDLATVESHLQDTQELLQEETRQKLNLSSRVRQLEEEKAamleqleeeeAAK 1385
Cdd:TIGR00606 695 EFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQ----------RLK 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1386 ANFSRQMQSLQQQVMETK--KKLEEDAGVAEAIEEARRRAAKDLESLSVRYE--ERVQACDKLEKGRTRLQQELDDVTVA 1461
Cdd:TIGR00606 765 NDIEEQETLLGTIMPEEEsaKVCLTDVTIMERFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSK 844
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1462 LDQQRQVVSALEKKQKKFDQMLAE---EKLISARYAEERDRAEADAREKETKVLSLSRALEEALETREEMERQNKQLRAE 1538
Cdd:TIGR00606 845 IELNRKLIQDQQEQIQHLKSKTNElksEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE 924
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1539 MDDLVSSKDDVGKNVH-ELERFKRALEQQVQEMRAQMEELEDelqATEDGKLRLEVNMQALKAQHERELQNRDDANDDkk 1617
Cdd:TIGR00606 925 KEELISSKETSNKKAQdKVNDIKEKVKNIHGYMKDIENKIQD---GKDDYLKQKETELNTVNAQLEECEKHQEKINED-- 999
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1618 kllskqVRELEAELDAERKQRA--QALAGRKKLELDLQEAMAQLDAANKGRDEagKQLRKLQAQMKELWREVEEARAARE 1695
Cdd:TIGR00606 1000 ------MRLMRQDIDTQKIQERwlQDNLTLRKRENELKEVEEELKQHLKEMGQ--MQVLQMKQEHQKLEENIDLIKRNHV 1071
|
890 900
....*....|....*....|
gi 1033370542 1696 EIFIQSRESEKKLKNLEAEL 1715
Cdd:TIGR00606 1072 LALGRQKGYEKEIKHFKKEL 1091
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
991-1820 |
4.27e-13 |
|
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: 75.08 E-value: 4.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 991 ARQKLQLEKVSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEERLSEFTSHMAEEEEKVKSLSKLRNKYEAV------MAD 1064
Cdd:TIGR00606 187 ALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIehnlskIMK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1065 MEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAElqaALARVEDEAAQKNavlKSLRELQA 1144
Cdd:TIGR00606 267 LDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKER---ELVDCQRELEKLN---KERRLLNQ 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1145 QLAELQEDMESEKLARAKAEKQRRDLGEELEALKTELEdtLDSTAAQQELRSKREQEVTELKKTIEEEVKVHEAQVLDMR 1224
Cdd:TIGR00606 341 EKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE--LDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1225 QRHTSALEELSEQLEQSRRFKINLEKTKQALEGENAEMQKEVKLLQAAK------LESEQRRKKLEGQ---------VQE 1289
Cdd:TIGR00606 419 SKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEgssdriLELDQELRKAERElskaeknslTET 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1290 LQLRAGEGERAKAELVERLVKLQNELDGVSGTlGSTESKTIKLAKDLATVESHLQDTQELLQEETRQKL----------- 1358
Cdd:TIGR00606 499 LKKEVKSLQNEKADLDRKLRKLDQEMEQLNHH-TTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLgyfpnkkqled 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1359 ---NLSSRVRQLEEEKAAMLEQLEEEEAAKANFSRQMQSLQQQVMETKKKLEEDAGVA------EAIEEARRRAAKDLES 1429
Cdd:TIGR00606 578 wlhSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQdeesdlERLKEEIEKSSKQRAM 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1430 LSVR---YEERVQ-----------ACDKLEKGRTRLQQELDDVT----VALDQQRQVVSALEKKQKKFDQMLAeekLISA 1491
Cdd:TIGR00606 658 LAGAtavYSQFITqltdenqsccpVCQRVFQTEAELQEFISDLQsklrLAPDKLKSTESELKKKEKRRDEMLG---LAPG 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1492 RyAEERDRAEADAREKETKVLSLSRALEealETREEMERQNKQLRAEMDDLVSSKdDVGKNVHELERFkralEQQVQEMR 1571
Cdd:TIGR00606 735 R-QSIIDLKEKEIPELRNKLQKVNRDIQ---RLKNDIEEQETLLGTIMPEEESAK-VCLTDVTIMERF----QMELKDVE 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1572 AQMEELEDELQATEDGKLRLEVNMQALKAQHE-RELQNRDDANDDKKKLLSKQVRELEA---ELDAERKQRAQALAGRKK 1647
Cdd:TIGR00606 806 RKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHElDTVVSKIELNRKLIQDQQEQIQHLKSktnELKSEKLQIGTNLQRRQQ 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1648 LELDLQEAMAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEARAAREEifiQSRESEKKLKNLEAELLQL---QEDL-- 1722
Cdd:TIGR00606 886 FEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKET---SNKKAQDKVNDIKEKVKNIhgyMKDIen 962
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1723 ---AASERAKRQAQQERDDLADELANGNSGKSALLDEKRHLEARIGQLEEELDEEQSNMELL--NDRYRKLSMQVETLTT 1797
Cdd:TIGR00606 963 kiqDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRkrENELKEVEEELKQHLK 1042
|
890 900
....*....|....*....|...
gi 1033370542 1798 ELGAERSFSQKTENARQQLERQN 1820
Cdd:TIGR00606 1043 EMGQMQVLQMKQEHQKLEENIDL 1065
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1005-1712 |
3.18e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 72.31 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1005 KLKKMEEDLLVLEDQNSKLHKERKLMEERLSEFTSHMaeeEEKVKSLSKLRNKYEAVMADMEDRLKK----EEKGRQELE 1080
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCT---PCMPDTYHERKQVLEKELKHLREALQQtqqsHAYLTQKRE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1081 KL--KRKLDGEAGDLQEQVAELQQQLEELrqALARKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQEDMESEKL 1158
Cdd:TIGR00618 251 AQeeQLKKQQLLKQLRARIEELRAQEAVL--EETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLM 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1159 ARAKAEKQRRDLGEELEALKTELedtldstaaQQELRSKREQEVTELKKTIEEEVKVHEAQVLDMRQRHTSALEE---LS 1235
Cdd:TIGR00618 329 KRAAHVKQQSSIEEQRRLLQTLH---------SQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKlqsLC 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1236 EQLEQSRRFKINLEKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGERAKAELVERLVKLQNEl 1315
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK- 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1316 dgVSGTLGSTESKTIKLAKDL-----------ATVESHLQDTQELLQE-ETRQKLNLSSRVRQLEEEKAAMLEQLEEEEA 1383
Cdd:TIGR00618 479 --EQIHLQETRKKAVVLARLLelqeepcplcgSCIHPNPARQDIDNPGpLTRRMQRGEQTYAQLETSEEDVYHQLTSERK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1384 AKANFSRQMQSLQQqvmETKKKLEEDAGVAEAIEEARRRAAKDLESLSVRYEERVQACDKLEKGRTRLQQELDDVTVALD 1463
Cdd:TIGR00618 557 QRASLKEQMQEIQQ---SFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLH 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1464 QQR------QVVSALEKKQKKFDQMLAEEKLISARYAEERDRAEADAREKEtkvlsLSRALEEALETREEMERQNKQLRA 1537
Cdd:TIGR00618 634 LQQcsqelaLKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQK-----MQSEKEQLTYWKEMLAQCQTLLRE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1538 EMDDLVSSKddvgKNVHELERFKRALEQQVQEMRAQMEELEDELQATEDGKLRLEVNMQALKAQHERELQNRDDANDDKK 1617
Cdd:TIGR00618 709 LETHIEEYD----REFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLA 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1618 KLLSKQVRELEAELDAERKQRAQAlagRKKLELDLQEAMAQLDAANKGRDEAGKQLR---KLQAQMKELWREVEEARAAR 1694
Cdd:TIGR00618 785 AEIQFFNRLREEDTHLLKTLEAEI---GQEIPSDEDILNLQCETLVQEEEQFLSRLEeksATLGEITHQLLKYEECSKQL 861
|
730
....*....|....*...
gi 1033370542 1695 EEIFIQSRESEKKLKNLE 1712
Cdd:TIGR00618 862 AQLTQEQAKIIQLSDKLN 879
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
900-1374 |
4.63e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.61 E-value: 4.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 900 DLKELENKYQQLSEEKTILAEQLQAETELFAEAEEMRARLAARKQELEDILHELESRVEeeeercqqlqgDKKKMQQHVQ 979
Cdd:PRK02224 214 ELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETER-----------EREELAEEVR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 980 DLEEQLEEEEAARQKLQLEKVSTEAKLKKMEEDLLVLEDQNSKLhkERKLMEERLS--EFTSHMAEEEEKVKslsklrnk 1057
Cdd:PRK02224 283 DLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEEL--RDRLEECRVAaqAHNEEAESLREDAD-------- 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1058 yeavmaDMEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQAALARVEDEAAQKNAVLK 1137
Cdd:PRK02224 353 ------DLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1138 SLRELQAQLAELQEDME--SEKLARAK--------AEKQRRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVTELKK 1207
Cdd:PRK02224 427 REAELEATLRTARERVEeaEALLEAGKcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1208 TiEEEVKVHEAQVLDMRQR---HTSALEELSEQLEQSRRFKINLE-------KTKQALEGENAEMQKEVKLLQAAKLESE 1277
Cdd:PRK02224 507 A-EDRIERLEERREDLEELiaeRRETIEEKRERAEELRERAAELEaeaeekrEAAAEAEEEAEEAREEVAELNSKLAELK 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1278 QRRKKLEGQVQELQLRAGEGERAKaELVERLVKLQNELDGVSGTLGSTESKTIKLAKDLAtvESHLQDTQELLQEETRQK 1357
Cdd:PRK02224 586 ERIESLERIRTLLAAIADAEDEIE-RLREKREALAELNDERRERLAEKRERKRELEAEFD--EARIEEAREDKERAEEYL 662
|
490
....*....|....*..
gi 1033370542 1358 LNLSSRVRQLEEEKAAM 1374
Cdd:PRK02224 663 EQVEEKLDELREERDDL 679
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1286-1960 |
5.60e-12 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 71.29 E-value: 5.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1286 QVQELQLRAGEG----ERAKAELVERLVKLQNELdgvsgtlgstesKTIKLAKDlATVESHLQDTQEllQEETRQKLNls 1361
Cdd:pfam15921 86 QVKDLQRRLNESnelhEKQKFYLRQSVIDLQTKL------------QEMQMERD-AMADIRRRESQS--QEDLRNQLQ-- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1362 SRVRQLEEEKAAMLEQLEeeeaakaNFSRQMQSLQQQVMETKKKLEEDAGVAEAIEEARRRAAKDLESLS-VRYEERVQA 1440
Cdd:pfam15921 149 NTVHELEAAKCLKEDMLN-------DSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMStIHFRSLGSA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1441 CDKLE----------KGRT-RLQQELDdvTVALDQQRQVVSALEKKQKKFDQMLAEEKLISARYAEERD--RAEADAREK 1507
Cdd:pfam15921 222 ISKILreldteisylKGRIfPVEDQLE--ALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASsaRSQANSIQS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1508 ETKVLSLSRALEEALETRE--EMERQNKQLRAEMDDLVSSKDDvgkNVHELERFKRALEQQVQEMRAQMEELEDELQATE 1585
Cdd:pfam15921 300 QLEIIQEQARNQNSMYMRQlsDLESTVSQLRSELREAKRMYED---KIEELEKQLVLANSELTEARTERDQFSQESGNLD 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1586 DGKLRLEVNMQ------ALKAQHERELQNRDDANddkkkllSKQVRELEAELDAERKQRAQALAGRKKLELDLQEAMAQL 1659
Cdd:pfam15921 377 DQLQKLLADLHkrekelSLEKEQNKRLWDRDTGN-------SITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQ 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1660 DAANKGRDEAGKQLRKLQAQM---KELWREVEEARAAREeifIQSRESEKKLKNLEAELLQLQEDLAASERAKRQAQQER 1736
Cdd:pfam15921 450 MAAIQGKNESLEKVSSLTAQLestKEMLRKVVEELTAKK---MTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRV 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1737 DDLADELAN-GNSGksallDEKRHLEARIGQLEEELDEEQSNMELLNDryrklsmQVETLTTELGAERSFSQKTENARQQ 1815
Cdd:pfam15921 527 DLKLQELQHlKNEG-----DHLRNVQTECEALKLQMAEKDKVIEILRQ-------QIENMTQLVGQHGRTAGAMQVEKAQ 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1816 LERQNKDLRAKLGEMdSSVKSKYKMAIATLESKVAQLEEQ---LEQESRERILSGKLVRRAEKKLKEVILQVDEERRNAD 1892
Cdd:pfam15921 595 LEKEINDRRLELQEF-KILKDKKDAKIRELEARVSDLELEkvkLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLS 673
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1033370542 1893 Q--------YKDQVEKGHLRLKQLKRQLEEAEEEASRANASRRRMQRELEDVTESAESMNREVTSLRNRLSKVERR 1960
Cdd:pfam15921 674 EdyevlkrnFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSK 749
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
994-1601 |
5.76e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 71.20 E-value: 5.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 994 KLQLEKVSTEAKLKKMEEDLLVLEDQ----NSKLHKERKLMEERLSEFTSHMAEEEEKVKSLSKLRNKYEAVMADMEDRL 1069
Cdd:TIGR04523 128 KLEKQKKENKKNIDKFLTEIKKKEKEleklNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLK 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1070 KKEEKgrqeleklKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAel 1149
Cdd:TIGR04523 208 KKIQK--------NKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELE-- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1150 qedmeseklaraKAEKQRRDLGEELEALKTELEDtldstaaqqeLRSKREQEVTelkKTIEEEVKVHEAQVLDMRQR--- 1226
Cdd:TIGR04523 278 ------------QNNKKIKELEKQLNQLKSEISD----------LNNQKEQDWN---KELKSELKNQEKKLEEIQNQisq 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1227 HTSALEELSEQLEQSRRFKINLEKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGERAKAELVE 1306
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1307 RLVKLQNELdgvsgtlgstesktiklakdlatvESHLQDTQELLQEETRQKlnlsSRVRQLEEEKAAMLEQLEeeeaaka 1386
Cdd:TIGR04523 413 QIKKLQQEK------------------------ELLEKEIERLKETIIKNN----SEIKDLTNQDSVKELIIK------- 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1387 NFSRQMQSLQQQVMETKKKLEEdagvaeaieearrrAAKDLESLSVRYEERVQACDKLEKGRTRLQQELDDVTVALDQQR 1466
Cdd:TIGR04523 458 NLDNTRESLETQLKVLSRSINK--------------IKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLK 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1467 QVVSALEKKQKKFDQMLA--EEKLISaryaeerDRAEADAREKETKVLSLSRALEEALETREEMERQNKQLRAEMDDLVS 1544
Cdd:TIGR04523 524 EKIEKLESEKKEKESKISdlEDELNK-------DDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK 596
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1033370542 1545 SKDDVGKNVHELERFKRALEQQVQEMRAQMEELEDELQATEDGKLRLEVNMQALKAQ 1601
Cdd:TIGR04523 597 EKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
1442-1954 |
8.04e-12 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 70.56 E-value: 8.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1442 DKLEKGRTRLQQELDDVTVALDQQRQVVSALEKKQKKFDQMLAEEKLisaryaEERDRAEADAREKETKVLSLSRALEEA 1521
Cdd:COG0419 167 EKYEKLSELLKEVIKEAKAKIEELEGQLSELLEDIEDLLEALEEELK------ELKKLEEIQEEQEEEELEQEIEALEER 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1522 LETREEMERQNKQLRAEMDDLVSSKDDVGKNVHELERFKRALEQQVQEMRAQMEELEDE---LQATEDGKLRLEVNMQAL 1598
Cdd:COG0419 241 LAELEEEKERLEELKARLLEIESLELEALKIREEELRELERLLEELEEKIERLEELEREieeLEEELEGLRALLEELEEL 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1599 KAQHERELQNRDDANDDKKKLlskqvRELEAELDAERKQRAQALAGR-KKLELDLQEAMAQLDAANKGRDEAGKQLRKLQ 1677
Cdd:COG0419 321 LEKLKSLEERLEKLEEKLEKL-----ESELEELAEEKNELAKLLEERlKELEERLEELEKELEKALERLKQLEEAIQELK 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1678 AQMKELWREVEEARAAREEIfiqsresEKKLKNLEAELLQLQEDLAASERAKRQAQQERDDLADELANGNS----GKSAL 1753
Cdd:COG0419 396 EELAELSAALEEIQEELEEL-------EKELEELERELEELEEEIKKLEEQINQLESKELMIAELAGAGEKcpvcGQELP 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1754 LDEKRHLEARIGQLEEELDEEQSNMELLNDRYRKLSMQVETLTTELGAERSFSQKTENARQQLERQNKDLRAKLGEMDSS 1833
Cdd:COG0419 469 EEHEKELLELYELELEELEEELSREKEEAELREEIEELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEELEEL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1834 VKSKYKMAI----ATLESKVAQLEEQLEQESRERILSGKLvRRAEKKLKEVILQVDEERRNADQYKDQVEKGHL--RLKQ 1907
Cdd:COG0419 549 KEKLQLQQLkeelRQLEDRLQELKELLEELRLLRTRKEEL-EELRERLKELKKKLKELEERLSQLEELLQSLELseAENE 627
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1033370542 1908 LKRQLEEAEEEASRANAsRRRMQRELEDVTESAESMNREVTSLRNRL 1954
Cdd:COG0419 628 LEEAEEELESELEKLNL-QAELEELLQAALEELEEKVEELEAEIRRE 673
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
872-1490 |
8.33e-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: 70.77 E-value: 8.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 872 QVTRQDEVMQA-----KAVELQKVQEKHTKTQMDLKELENKYQQLSEEKTILAEQLQAETELFAEAEEMRARLAARKQEL 946
Cdd:TIGR00618 244 YLTQKREAQEEqlkkqQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSR 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 947 EDILHELESRVEEEEERCQQLQGDKKKMQQH----VQDLEEQLEEEEAARQKLQLEKVSTEAKLKKMEEDLL-------- 1014
Cdd:TIGR00618 324 AKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEihirDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLqslckeld 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1015 -----------------VLEDQNSKLHKERKLMEERLS--------EFTSHMAEEEEKVKSLSKLRNKyEAVMADMEDRL 1069
Cdd:TIGR00618 404 ilqreqatidtrtsafrDLQGQLAHAKKQQELQQRYAElcaaaitcTAQCEKLEKIHLQESAQSLKER-EQQLQTKEQIH 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1070 KKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALArkeaeLQAALARVEDEAAQKNAVLKSLR----ELQAQ 1145
Cdd:TIGR00618 483 LQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGP-----LTRRMQRGEQTYAQLETSEEDVYhqltSERKQ 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1146 LAELQEDMESEKLARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRSKREQEvtelkKTIEEEVKVHEAQVLDMRQ 1225
Cdd:TIGR00618 558 RASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE-----QHALLRKLQPEQDLQDVRL 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1226 RHTSALEELSEQLEQSRRFKINLEKTKQALEGENAEMQKEVKLLQ-AAKLESEQRRKKLEGQVQELQLRAGEGERAKAEL 1304
Cdd:TIGR00618 633 HLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASrQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETH 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1305 VERLVKLQNELDGVSGTLGStesktiklakDLATVESHLQDTQELLQEETRQKLNLSSRVRQLEEEKAAMLEQLEEeeaa 1384
Cdd:TIGR00618 713 IEEYDREFNEIENASSSLGS----------DLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGA---- 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1385 kanfsrQMQSLQQQVMETKKKLEEDAGVAEAIEEARRRAAKDLEslsvryEERVQACDKLEKGRTRLQQELDDVTVALDQ 1464
Cdd:TIGR00618 779 ------ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDE------DILNLQCETLVQEEEQFLSRLEEKSATLGE 846
|
650 660
....*....|....*....|....*.
gi 1033370542 1465 QRQVVSALEKKQKKFDQMLAEEKLIS 1490
Cdd:TIGR00618 847 ITHQLLKYEECSKQLAQLTQEQAKII 872
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1300-1900 |
1.00e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.48 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1300 AKAELVERLVKLQNELDGVSGTLGSTESKTIKLAKDLATVESHLQD---TQELLQEETRQKLNLSSRVRQLEEekaamle 1376
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEE------- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1377 qleeeeaakanfsrQMQSLQQQVMETKKKLEEDAGVAEAIEEARRRAaKDLESLSVRYEERVQACDKLEKGRTRLQQELD 1456
Cdd:PRK03918 260 --------------KIRELEERIEELKKEIEELEEKVKELKELKEKA-EEYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1457 DVtvaldqqRQVVSALEKKQKKFDQMLAEEKLISARYAEERDRAEA--DAREKETKVLSLSRalEEALETREEMERqnkq 1534
Cdd:PRK03918 325 GI-------EERIKELEEKEERLEELKKKLKELEKRLEELEERHELyeEAKAKKEELERLKK--RLTGLTPEKLEK---- 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1535 lraEMDDLVSSKDDVGKNVHELERFKRALEQQVQEMRAQMEELEDelqatedGKLRLEVNMQALKAQHERELQNRDDAND 1614
Cdd:PRK03918 392 ---ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK-------AKGKCPVCGRELTEEHRKELLEEYTAEL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1615 DKKKLLSKQVRELEAELDAERKQRAQALAGRKKLeLDLQEAMAQLDaankgrdEAGKQLRKLQAqmKELWREVEEARAAR 1694
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESEL-IKLKELAEQLK-------ELEEKLKKYNL--EELEKKAEEYEKLK 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1695 EEifiqSRESEKKLKNLEAELLQLQE---DLAASERAKRQAQQERDDLADELanGNSGKSALLDekrhLEARIGQleeel 1771
Cdd:PRK03918 532 EK----LIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKEL--EELGFESVEE----LEERLKE----- 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1772 deeqsnMELLNDRYRKLSMQVETLTTELGAERSFSQKTENARQQLERQNKDLRAKLGEMDssvkskykmaiatlESKVAQ 1851
Cdd:PRK03918 597 ------LEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE--------------ELEKKY 656
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1033370542 1852 LEEQLEQESRERILSGKLVRRAEKKLKEVILQVDEERRNADQYKDQVEK 1900
Cdd:PRK03918 657 SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE 705
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
840-1340 |
2.57e-11 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 69.02 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 840 SALKVMQRNCAAYLKLRHWQWWRLFTKVKPLLQVTRQDEVMQAKAVELQKVQEKHTKTQMDLKELENKYQQLSEEKTILA 919
Cdd:COG0419 246 EEKERLEELKARLLEIESLELEALKIREEELRELERLLEELEEKIERLEELEREIEELEEELEGLRALLEELEELLEKLK 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 920 EQLQAETELFAEAEEMRARLAARKQELEDILHELESRVEEEEERCQQLQGDKKKMQQHVQDLEEQLEEEEAARQKLQLEK 999
Cdd:COG0419 326 SLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELKEELAELSAAL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1000 VSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEERLSEFTSH--MAEEEEKVKSL-----SKLRNKYEAVMADMEDRLKKE 1072
Cdd:COG0419 406 EEIQEELEELEKELEELERELEELEEEIKKLEEQINQLESKelMIAELAGAGEKcpvcgQELPEEHEKELLELYELELEE 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1073 EKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQAALARVEDEAAQ-----KNAVLKSLRELQAQLA 1147
Cdd:COG0419 486 LEEELSREKEEAELREEIEELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEEleelkEKLQLQQLKEELRQLE 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1148 ELQEDMESEKLARAK-------------AEKQRRDLGEELEALKTELEDTLDST----------AAQQELRSKREQ--EV 1202
Cdd:COG0419 566 DRLQELKELLEELRLlrtrkeeleelreRLKELKKKLKELEERLSQLEELLQSLelseaeneleEAEEELESELEKlnLQ 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1203 TELKKTIEEEVKVHEAQVLDMRQRhTSALEELSEQLEQSRRFKINLEKTKQALEGENAEMQKevklLQAAKLESEQRRKK 1282
Cdd:COG0419 646 AELEELLQAALEELEEKVEELEAE-IRRELQRIENEEQLEEKLEELEQLEEELEQLREELEE----LLKKLGEIEQLIEE 720
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1033370542 1283 LEGQVQELQLRAGEGERAKAELverlvklqNELDGVSGTLGSTESKTIKLAKDLATVE 1340
Cdd:COG0419 721 LESRKAELEELKKELEKLEKAL--------ELLEELREKLGKAGLRADILRNLLAQIE 770
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
1465-1968 |
3.54e-11 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 68.63 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1465 QRQVVSALEKKQKKFDQMLAEEKLIsARYAEERDRAEADAREKETKVLSLSRALEEALETREEMERQNKQLRAEMDDLVS 1544
Cdd:COG0419 142 QGEFDAFLKSKPKERKEILDELFGL-EKYEKLSELLKEVIKEAKAKIEELEGQLSELLEDIEDLLEALEEELKELKKLEE 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1545 SKDDVGKnvhelerfkRALEQQVQEMRAQMEELEDELQATEDGKLRLEvNMQALKAQHERELQNRDDANDDKKKLLSKQV 1624
Cdd:COG0419 221 IQEEQEE---------EELEQEIEALEERLAELEEEKERLEELKARLL-EIESLELEALKIREEELRELERLLEELEEKI 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1625 RELEaELDAERKQRAQALAGRKKLELDLQEAMAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEARAAREEIFiqsRES 1704
Cdd:COG0419 291 ERLE-ELEREIEELEEELEGLRALLEELEELLEKLKSLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERL---KEL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1705 EKKLKNLEAELLQLQEDLAASERAKRQAQQERDDLADELANGNSGKSALLDEKRHLEARIgqleEELDEEQSNMELLNDR 1784
Cdd:COG0419 367 EERLEELEKELEKALERLKQLEEAIQELKEELAELSAALEEIQEELEELEKELEELEREL----EELEEEIKKLEEQINQ 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1785 YRKLSMQVETLTTELGAERSFSQKTENARQQ--LERQNKDLRAKLGEMdssvksKYKMAIATLESKVAQLEEQLEQESRE 1862
Cdd:COG0419 443 LESKELMIAELAGAGEKCPVCGQELPEEHEKelLELYELELEELEEEL------SREKEEAELREEIEELEKELRELEEE 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1863 RILSGKLVRRAEKKLKEVILQVDEERRNADQYKDQVEKghLRLKQLKRQLEEAEEEASRANASRRRMQR---ELEDVTES 1939
Cdd:COG0419 517 LIELLELEEALKEELEEKLEKLENLLEELEELKEKLQL--QQLKEELRQLEDRLQELKELLEELRLLRTrkeELEELRER 594
|
490 500
....*....|....*....|....*....
gi 1033370542 1940 AESMNREVTSLRNRLSKVERRQRKRTPLS 1968
Cdd:COG0419 595 LKELKKKLKELEERLSQLEELLQSLELSE 623
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
886-1314 |
8.92e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.37 E-value: 8.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 886 ELQKVQEKHTKTQMDLKELENKYQQLSEEktiLAEQLQAETELFAEAEEMRAR----------LAARKQELEDILHELES 955
Cdd:PRK02224 252 ELETLEAEIEDLRETIAETEREREELAEE---VRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 956 RVEEEEERCQQLQGDKKKMQQHVQDLEEQLEEEEAARQKLQLEKVSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEERLS 1035
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1036 EFTSHMAEEEEkvkSLSKLRNKYEAVMADMEDRLKKEEKGRQELEKLK-----RKLDGE-----AGDLQEQVAELQQQLE 1105
Cdd:PRK02224 409 NAEDFLEELRE---ERDELREREAELEATLRTARERVEEAEALLEAGKcpecgQPVEGSphvetIEEDRERVEELEAELE 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1106 ELRQALARKEAELQAALARVEDEA----------------AQKNAVLKSLRELQAQLAELQEDMESE-KLARAKAEKQRR 1168
Cdd:PRK02224 486 DLEEEVEEVEERLERAEDLVEAEDrierleerredleeliAERRETIEEKRERAEELRERAAELEAEaEEKREAAAEAEE 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1169 DLGEELEALKT------ELEDTLDS--------------TAAQQELRSKREQ-------------EVTELKKTIEEEV-- 1213
Cdd:PRK02224 566 EAEEAREEVAElnsklaELKERIESlerirtllaaiadaEDEIERLREKREAlaelnderrerlaEKRERKRELEAEFde 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1214 -KVHEAQvlDMRQRHTSALEELSEQLEQSRRFKINLEKTKQALEGENAEMQkevkllqaaklESEQRRKKLEGQVQELQL 1292
Cdd:PRK02224 646 aRIEEAR--EDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELE-----------ELRERREALENRVEALEA 712
|
490 500 510
....*....|....*....|....*....|...
gi 1033370542 1293 RAGEGE-------RAKAEL----VERLVKLQNE 1314
Cdd:PRK02224 713 LYDEAEelesmygDLRAELrqrnVETLERMLNE 745
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
965-1288 |
9.96e-11 |
|
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: 67.07 E-value: 9.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 965 QQLQGDKKKMQQHVQDLEEQLEEEEAARQKLQLEKVSTEAKLKKmeEDLLVLEDQNSKLHKERKLMEERLSEFTSHMAE- 1043
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDR--QAAIYAEQERMAMERERELERIRQEERKRELERi 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1044 -EEEKVKSLSKLRNKYEAVMadmeDRLKKEEKGRQELE---KLKRKLDGEAGDLQEQVAELQQ---QLEELRQ-ALARKE 1115
Cdd:pfam17380 366 rQEEIAMEISRMRELERLQM----ERQQKNERVRQELEaarKVKILEEERQRKIQQQKVEMEQiraEQEEARQrEVRRLE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1116 AELQAALARVEDEAAQKNAVLKSLRELQAQLAELQEDMESEKLARAKAEKQRRDLgeeleaLKTELEDTLDSTAAQQELR 1195
Cdd:pfam17380 442 EERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI------LEKELEERKQAMIEEERKR 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1196 SKREQEVTELKKTIEEEvkvheaqvldmrQRHTSALEELSEQLEQSRRFKINLEKTKQALEGENAE-MQKEVKLLQAAKl 1274
Cdd:pfam17380 516 KLLEKEMEERQKAIYEE------------ERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEaMEREREMMRQIV- 582
|
330
....*....|....
gi 1033370542 1275 ESEQRRKKLEGQVQ 1288
Cdd:pfam17380 583 ESEKARAEYEATTP 596
|
|
| YhaN |
COG4717 |
Uncharacterized protein YhaN, contains AAA domain [Function unknown]; |
1004-1691 |
1.12e-10 |
|
Uncharacterized protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 227061 [Multi-domain] Cd Length: 984 Bit Score: 67.18 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1004 AKLKKMEEDLLVLEDQNSKLHK---ERKLMEERLSEFTS-------HMAEEEEKVKSLSKLRNK---YEAVMADMEDRLK 1070
Cdd:COG4717 188 EKLKQERNEIDEAEKEYATYHKlleSRRAEHARLAELRSelradrdHIRALRDAVELWPRLQEWkqlEQELTRRREELAT 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1071 KEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQAALARVEdeaaQKNAVLKSLRELQAQLAELQ 1150
Cdd:COG4717 268 FPRDGVLRLEKREAHLQKTEAEIDALLVRLAELKDLASQLIPAKEAVLQALVRLHQ----QLSEIKASAFELTETLAGIE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1151 EDM-ESEKLARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVTELKKtIEEEVKVHEAQVLDMRQRHTS 1229
Cdd:COG4717 344 ADLrDKEEAAGNGFEAERVHDLRSLECMLRYQSSQRELKQTEAAYCKRLDEKRLFEDE-AEEEARQRLADDEEEVRAGDE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1230 ALEELSEQLEQsrrfKINLEKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELqlragegerAKAELVERLV 1309
Cdd:COG4717 423 AREEKIAANSQ----VIDKEEVCNLYDRRDTAWQKQRFLREKQTAFERQKTEHTKIIALRL---------AGMLLVALSR 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1310 KLQNELDGVSGT-------LGSTESKTIKLAKDLATVESHLQDTQELLQEETRQKLNL----SSRVRQ-LEEEKAAMLEQ 1377
Cdd:COG4717 490 LLTSLIFQIIFAvaqivflSAEIKSSSRAVREEKAAVTDIPEELARLLITDELPELAVdllvQSRIRQhWQQLRKALDQL 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1378 LEEEEAAKANFSR---QMQSLQQQVMETKKKLEEDAGVAEAIEEARRRAAKDLeslsvryEERVQACDKLEKGRTRLQQE 1454
Cdd:COG4717 570 EAAYEALEGRFAAaeaAMAEWQSEWEEALDELGLSRELSPEQQLDILSTMKDL-------KKLMQKKAELTHQVARLREE 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1455 LDDVTVALDQQRQVVSALEKKQKKFdqMLAEEKLISARYAEERDRAEADAREKETKvlslsralEEALETREEMERQNKQ 1534
Cdd:COG4717 643 QAAFEERVEGLLAVLEAQFIDLSTL--FCVQRLRVAAELQKEEARLALEGNIERTK--------ELNDELRAELELHRKE 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1535 LRAEMDDLVSSKDDVGKNVHElerfkraLEQQVQEMRAQMEELEDELQATEDGKLRLEVNMqALKAQHERELQNrddaND 1614
Cdd:COG4717 713 ILDLFDCGTADTEDAFREAAR-------EEQQLTQRESRLESLEAQLEGVAAEAYELSASL-DQRELKEEELAL----LE 780
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1033370542 1615 DKKKLLSKQVRELEAELDAERKQRAQALAGRKKLELDLQEAMAQLDAANKGRDEAGKQL-RKLQAQMKELWREVEEAR 1691
Cdd:COG4717 781 EAIDALDEEVEELHAQVAALSRQIAQLEGGGTVAELRQRRESLKEDLEEKARKWASLRLaVQVLEEALRLFKERRLPA 858
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
864-1581 |
1.21e-10 |
|
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: 66.92 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 864 FTKVKPLLQvTRQDEVMQAKAVELQKVQEKHTKT----QMDLKELENKyQQLSEEKTILAEQLQAETELfaeAEEMRARL 939
Cdd:TIGR00618 143 FTRVVLLPQ-GEFAQFLKAKSKEKKELLMNLFPLdqytQLALMEFAKK-KSLHGKAELLTLRSQLLTLC---TPCMPDTY 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 940 AARKQELEDILHELESRVeeeeercQQLQGDKKKMQQHVQDLEEQLEEEEAARQKL-QLEKVSTEAKLKKMEEDLLVLED 1018
Cdd:TIGR00618 218 HERKQVLEKELKHLREAL-------QQTQQSHAYLTQKREAQEEQLKKQQLLKQLRaRIEELRAQEAVLEETQERINRAR 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1019 QNSKLHKERKLMEERLSEFTSHMAEEEEKVKSLSKLRNKYEAVM---ADMEDRLKKEEKGRQELEKLKRKLDGEAG--DL 1093
Cdd:TIGR00618 291 KAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVkqqSSIEEQRRLLQTLHSQEIHIRDAHEVATSirEI 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1094 QEQVAELQQQLEELRQ---ALARKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQedmESEKLARAKAEKQRRDL 1170
Cdd:TIGR00618 371 SCQQHTLTQHIHTLQQqktTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAK---KQQELQQRYAELCAAAI 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1171 GEELEALKTEledTLDSTAAQQELRSKREQEVTelKKTI---EEEVKVHEAQVLDMRQRHTSALEELSEQLEQSRRFKIN 1247
Cdd:TIGR00618 448 TCTAQCEKLE---KIHLQESAQSLKEREQQLQT--KEQIhlqETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDN 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1248 LEKTK---QALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGERAKAELVERLVKLQNELDGVSGTLGS 1324
Cdd:TIGR00618 523 PGPLTrrmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1325 TESKTIKLAKDLATVESHLQDTQELLQ-----EETRQKLNLSSRVRQLEEEKAAMLEQLEEEEAAKANFSRQMQSLQQQV 1399
Cdd:TIGR00618 603 LSEAEDMLACEQHALLRKLQPEQDLQDvrlhlQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLAL 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1400 METKKKLEEDAGVAEAIEEARRRAAKDLESLSVRYEERVQACDKLEKGRTRLQQELDDVTVALD----QQRQVVSALEKK 1475
Cdd:TIGR00618 683 QKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKelmhQARTVLKARTEA 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1476 QKKFDQMLAEEKLISARYAEERDRAEADAREKETKVLSLSRALEEALETREE----MERQNKQLRAEMDDLVSSKDDVGK 1551
Cdd:TIGR00618 763 HFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSdediLNLQCETLVQEEEQFLSRLEEKSA 842
|
730 740 750
....*....|....*....|....*....|....*.
gi 1033370542 1552 NVHELERFKRALE------QQVQEMRAQMEELEDEL 1581
Cdd:TIGR00618 843 TLGEITHQLLKYEecskqlAQLTQEQAKIIQLSDKL 878
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
993-1742 |
1.49e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 66.67 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 993 QKLQLEKVSTEAKLK----KMEEDLLVLEDQNSKLhKERKLMEERLS-EFTSHMAEEEEKVKSLSKLR---NKYEAVMAD 1064
Cdd:pfam05483 88 EKIKKWKVSIEAELKqkenKLQENRKIIEAQRKAI-QELQFENEKVSlKLEEEIQENKDLIKENNATRhlcNLLKETCAR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1065 MEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQAALARVEDEAAQK-NAVLKSLRELQ 1143
Cdd:pfam05483 167 SAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEiNDKEKQVSLLL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1144 AQLAELQEDMESEKLArakAEKQRRDLGEELEALKTELEDTLDSTAAQQELRSKRE------QEVTELKKTIEEEVKVHE 1217
Cdd:pfam05483 247 IQITEKENKMKDLTFL---LEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEdikmslQRSMSTQKALEEDLQIAT 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1218 AQVLDMRQRHTSALEELSEQLEQSRRFKINLEKTKQALEgenaemqkevkllqaAKLESEQRRkkLEGQVQELQLRAGEG 1297
Cdd:pfam05483 324 KTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLE---------------ELLRTEQQR--LEKNEDQLKIITMEL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1298 ERAKAELvERLVKLQNeldgvsgtlgsteSKTIKLaKDLATVeshLQDTQELLqEETRQKLNLSSRVRQLEEEKAAMLEQ 1377
Cdd:pfam05483 387 QKKSSEL-EEMTKFKN-------------NKEVEL-EELKKI---LAEDEKLL-DEKKQFEKIAEELKGKEQELIFLLQA 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1378 LEeeeaakanfsRQMQSLQQQVMETKKKLEEdagVAEAIEEARrraaKDLESLSVRYEERVQACDKLEKGRTRLQQELDD 1457
Cdd:pfam05483 448 RE----------KEIHDLEIQLTAIKTSEEH---YLKEVEDLK----TELEKEKLKNIELTAHCDKLLLENKELTQEASD 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1458 VTVALDQQRQVVSALEKKQKKfdqMLAEEKLISARYAEERDRAEADAREKETKVLSLSRALEEALETREEMERQNKQLRA 1537
Cdd:pfam05483 511 MTLELKKHQEDIINCKKQEER---MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEK 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1538 EMDDLVSSKDDVGKNVHELERFKRALEQQVQEMRAQMEELEDELQATEDGKLRLEVNMQALKAQHERELQNRDDANDDKK 1617
Cdd:pfam05483 588 QMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKK 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1618 klLSKQvrELEAELDAERKQRAQALAGRKKLELDLQEAMAQLDA-ANKGRDEAGKQLRKLQAQMKELWREVEEARAAREE 1696
Cdd:pfam05483 668 --ISEE--KLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVAlMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAA 743
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1697 IfiqsresEKKLKNLEAELLQLQEDLAAS----ERAKRQAQQERDDLADE 1742
Cdd:pfam05483 744 L-------EIELSNIKAELLSLKKQLEIEkeekEKLKMEAKENTAILKDK 786
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ... |
881-1621 |
1.53e-10 |
|
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: 66.53 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 881 QAKAVELQKVQEKHTKTQMDLKELENKYQQLSEEKTILAEQLQAETELFAEAEEMRARLAARKQELEDILHELESRVEEE 960
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 961 EERCQQLQgdkKKMQQHVQDLEEQLEEEEAARQKLQLEKVSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEERLSEFTSH 1040
Cdd:pfam02463 387 SSAAKLKE---EELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKD 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1041 MAEEEEKVKSLSKLRNKYEAVM-ADMEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQ 1119
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQlELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKV 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1120 AALARVEDEAAQKNAVLKSLRELQAQLAELQEDMESEKLARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRSKRE 1199
Cdd:pfam02463 544 AISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAK 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1200 QEVTELKKTIEEEVKVHEAQVLDMRQRHTSALEELSEQLEQSRrfkiNLEKTKQALEGENAEMQKEVKLLQAAKLESEQR 1279
Cdd:pfam02463 624 VVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKA----SLSELTKELLEIQELQEKAESELAKEEILRRQL 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1280 RKKLEGQVQELQLR--AGEGERAKAELVERLVKLQNE----LDGVSGTLGSTESKTIKLAKDLATVESHLQDTQELLQEE 1353
Cdd:pfam02463 700 EIKKKEQREKEELKklKLEAEELLADRVQEAQDKINEelklLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEE 779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1354 TRQKLNLSSRVRQLEEEKAAMLEQLEEEEAAKANFSRQMQSLQQQVMETKKKLEEDAGVAEAIEEARRRAAKDLESLSVR 1433
Cdd:pfam02463 780 REKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERL 859
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1434 YEERVQACDKLEKGRTRLQQELDDVTVALDQQRQVVS----ALEKKQKKFDQMLAEEKLISARYAEERDRAEADAREKET 1509
Cdd:pfam02463 860 EEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKeekkELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEE 939
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1510 KVLSLSRALEEALETREEMERQNKQLRAEMDDLVSSKDDVGKNVHELERFKRALEQQVQEMRAQMEELEDELQATEDGKL 1589
Cdd:pfam02463 940 LLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRL 1019
|
730 740 750
....*....|....*....|....*....|..
gi 1033370542 1590 RLEVNMQALKAQHERELQNRDDANDDKKKLLS 1621
Cdd:pfam02463 1020 KEFLELFVSINKGWNKVFFYLELGGSAELRLE 1051
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1433-1964 |
2.06e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.24 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1433 RYEERVQACDKLEKGRTRLQQELDDVTVALDQQRQVVSALEKKQKKFDQMLAEEKLISARYAEERDRAEadarEKETKVL 1512
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE----ELKKEIE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1513 SLSRALEEALETREEMERQNKqLRAEMDDLVSSKDDVGKNVHELERFKRALEQQVQE---MRAQMEELEDELQATEDGKL 1589
Cdd:PRK03918 277 ELEEKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEleeKEERLEELKKKLKELEKRLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1590 RLEVNMQALkaqhERELQNRDDANDDKKKLLSKQVRELEAELDAERKQRAQALAGRKKLEldlqEAMAQLDAANKGRDEA 1669
Cdd:PRK03918 356 ELEERHELY----EEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKIT----ARIGELKKEIKELKKA 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1670 GKQLRKLQAQMKELWREVEEARaaREEIFiqsRESEKKLKNLEAELLQLQEDLAASERAKRQAQQERDDLADELANgnsg 1749
Cdd:PRK03918 428 IEELKKAKGKCPVCGRELTEEH--RKELL---EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL---- 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1750 kSALLDEKRHLEARIGQLEEELDEEQSN-MELLNDRYRKLSMQVETLTTELGAERSFsqktENARQQLERQNKDLRAKLG 1828
Cdd:PRK03918 499 -KELAEQLKELEEKLKKYNLEELEKKAEeYEKLKEKLIKLKGEIKSLKKELEKLEEL----KKKLAELEKKLDELEEELA 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1829 EMDSSVKSKYKMAIATLESKVAQLEEqLEQESRERILSGKLVRRAEKKLKEVILQVDEERRNADQYKDQVEKGHLRLKQL 1908
Cdd:PRK03918 574 ELLKELEELGFESVEELEERLKELEP-FYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL 652
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1033370542 1909 KRQLEEAEEEasRANASRRRMQRELEDVTESAESMNREVTSLRNRLSKVERRQRKR 1964
Cdd:PRK03918 653 EKKYSEEEYE--ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
881-1744 |
2.59e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.13 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 881 QAKAVELQKVQEKHTKTQMDLKELEnkyqqlseektilaEQLQAETELFAEAEEMRARLAARKQELEdilhelesrveee 960
Cdd:PRK04863 337 LNLVQTALRQQEKIERYQADLEELE--------------ERLEEQNEVVEEADEQQEENEARAEAAE------------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 961 eercQQLQGDKKKMQQHVQDLEEQLEEEEAARQKLQ-LEKVSTEAKLKKMEEDLLvledqnsklhkerklmEERLSEFTs 1039
Cdd:PRK04863 390 ----EEVDELKSQLADYQQALDVQQTRAIQYQQAVQaLERAKQLCGLPDLTADNA----------------EDWLEEFQ- 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1040 hmAEEEEKVKSLSKLRNKyeavMADMEDRLKKEEKGRQelekLKRKLDGE--AGDLQEQVAELQQQLEELRqALARKEAE 1117
Cdd:PRK04863 449 --AKEQEATEELLSLEQK----LSVAQAAHSQFEQAYQ----LVRKIAGEvsRSEAWDVARELLRRLREQR-HLAEQLQQ 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1118 LQAALARVEDEAAQKNAVLKSLRELQaQLAELQEDMESEklarakAEKQRRDLGEELEALKTELEDtldstaaQQELRSK 1197
Cdd:PRK04863 518 LRMRLSELEQRLRQQQRAERLLAEFC-KRLGKNLDDEDE------LEQLQEELEARLESLSESVSE-------ARERRMA 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1198 REQEVTELKKTIEEEVKV----HEAQvldmrqrhtSALEELSEQLEQSrrfkinlEKTKQALEGENAEMQKEVKLLQAAK 1273
Cdd:PRK04863 584 LRQQLEQLQARIQRLAARapawLAAQ---------DALARLREQSGEE-------FEDSQDVTEYMQQLLERERELTVER 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1274 LESEQRRKKLEGQVQELQLRAG-EGERAKAeLVERL-----------VKLQ------------------NELDGVSGTLG 1323
Cdd:PRK04863 648 DELAARKQALDEEIERLSQPGGsEDPRLNA-LAERFggvllseiyddVSLEdapyfsalygparhaivvPDLSDAAEQLA 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1324 STESktikLAKDLATVESHLQ-------DTQELLQEETRQKLNLSSRVRQL-----------EEEKAAMLEQLEEEEAAK 1385
Cdd:PRK04863 727 GLED----CPEDLYLIEGDPDsfddsvfSVEELEKAVVVKIADRQWRYSRFpevplfgraarEKRIEQLRAEREELAERY 802
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1386 ANFSRQMQSLQQQVMETKKKLEEDAGVA------EAIEEARRRaakdleslsvryeeRVQACDKLEKGRTRLQQelddVT 1459
Cdd:PRK04863 803 ATLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpeAELRQLNRR--------------RVELERALADHESQEQQ----QR 864
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1460 VALDQQRQVVSALEKKQKKFDqMLAEEKLIsARYAE---ERDRAEADAR---------EKETKVLSLSRALEEALET--- 1524
Cdd:PRK04863 865 SQLEQAKEGLSALNRLLPRLN-LLADETLA-DRVEEireQLDEAEEAKRfvqqhgnalAQLEPIVSVLQSDPEQFEQlkq 942
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1525 -----REEMERQNKQLRAeMDDLVS---------SKDDVGKNVHELERFKRALEQQVQEMRAQMEEL-EDELQATEDGKL 1589
Cdd:PRK04863 943 dyqqaQQTQRDAKQQAFA-LTEVVQrrahfsyedAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLrQAQAQLAQYNQV 1021
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1590 rlevnMQALKAQHERELQNRDDANDDKKKL-----------LSKQVRELEAELDAERKQRAQALAGRKKLELDLqeamaq 1658
Cdd:PRK04863 1022 -----LASLKSSYDAKRQMLQELKQELQDLgvpadsgaeerARARRDELHARLSANRSRRNQLEKQLTFCEAEM------ 1090
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1659 ldaankgrDEAGKQLRKLQAQMKELWREVEEARAAREEIFIQSRES--EKKLKNLEAELLQLQEDLAASERAK---RQAQ 1733
Cdd:PRK04863 1091 --------DNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNgvERRLHRRELAYLSADELRSMSDKALgalRLAV 1162
|
970
....*....|.
gi 1033370542 1734 QERDDLADELA 1744
Cdd:PRK04863 1163 ADNEHLRDVLR 1173
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ... |
1225-1964 |
3.30e-10 |
|
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: 65.76 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1225 QRHTSALEELSEQLEQSRRfKINLEKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGERAKAEL 1304
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKK-KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1305 VERLVKLQNELDGVSGTLGSTESKTIKLAKDlatVESHLQDTQELLQEETRQKLNLSSRVRQLEEEKAAMLEQLEEEEAA 1384
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEK---EEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1385 KANFSRQMQSLQQQVMETKKKLEEDAGVAEAIEearrraaKDLESLSVRYEERVQACDKLEKGRTRLQQELDDVTVALDQ 1464
Cdd:pfam02463 309 KVDDEEKLKESEKEKKKAEKELKKEKEEIEELE-------KELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1465 QRQVVSALEKKQKKFDQMLAEEKLISARYAEERDRAEADAREKETKVLSLSRALEEALETREEmerqNKQLRAEMDDLVS 1544
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQG----KLTEEKEELEKQE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1545 SKDDVGKNVHELERFKRALEQQVQEMRAQMEELEDELQATEDGKLRLEVNMQALK--------------AQHERELQNRD 1610
Cdd:pfam02463 458 LKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLlalikdgvggriisAHGRLGDLGVA 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1611 DANDDKKKLLSKQVRELEAELDAERKQRAQALAGRKKLELDLQEAMAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEA 1690
Cdd:pfam02463 538 VENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADE 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1691 RAAREEIFIQSRESEKKLKNLEAELLQLQEDLAASERAKRQAQQERDDLADELANGNSGKSALLDEKRHLEARIGQLEEE 1770
Cdd:pfam02463 618 DDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRR 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1771 LDEEQSNMELLNDRYRKLSMQVETLTTELgaersfsqKTENARQQLERQNKDLRAKLGEMDSSVKSKYKMAIATLESKVA 1850
Cdd:pfam02463 698 QLEIKKKEQREKEELKKLKLEAEELLADR--------VQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSEL 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1851 QLEEQLEQESRERILSGKLVRRAEKKLKEvilQVDEERRNADQYKDQVEKGHlrlKQLKRQLEEAEEEASRANASRRRMQ 1930
Cdd:pfam02463 770 SLKEKELAEEREKTEKLKVEEEKEEKLKA---QEEELRALEEELKEEAELLE---EEQLLIEQEEKIKEEELEELALELK 843
|
730 740 750
....*....|....*....|....*....|....
gi 1033370542 1931 RELEDVTESAESMNREVTSLRNRLSKVERRQRKR 1964
Cdd:pfam02463 844 EEQKLEKLAEEELERLEEEITKEELLQELLLKEE 877
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1236-1982 |
3.65e-10 |
|
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: 65.38 E-value: 3.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1236 EQLEQSRRFKINLEKTKQALEGENAEMQKEVKLLqaaKLESEQRRKKLEGQVQELQLRAGEGERAKAELVERLVKLQNEL 1315
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLL---TLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1316 dgvsgTLGSTESKTIKLAKDLATVESHLQdTQELLQEETRQKLNLSSRVRQLEEEKAAMLEQLEEEEAAKANFSRQMQSL 1395
Cdd:TIGR00618 250 -----EAQEEQLKKQQLLKQLRARIEELR-AQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSR 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1396 QQQVMETKKKLEEDAgvaeAIEEARRRaakdLESLSVRYEERVQACDKLEKGRTRLQQELDDVTVALDQQRQVVSALEKK 1475
Cdd:TIGR00618 324 AKLLMKRAAHVKQQS----SIEEQRRL----LQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKL 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1476 Q---KKFDQMLAEEKLISARYAEERDRAEADAREKETKVLSLSRALEEALETREEMERQnKQLRAEMDDLVSSKDDVGKN 1552
Cdd:TIGR00618 396 QslcKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCE-KLEKIHLQESAQSLKEREQQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1553 VHELERFKRALEQQVQEMRAQMEELEDELQATEDGKLRLEVNMQAlkAQHERELQNRDDANDDKKKLLSKQVRELEAELD 1632
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQD--IDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLT 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1633 AERKQRaqalagrKKLELDLQEAMAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEaraareeifiQSRESEKKLKNLE 1712
Cdd:TIGR00618 553 SERKQR-------ASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK----------LSEAEDMLACEQH 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1713 AELLQLQEDLAASERAKRQAQQERDDLADELANGNSGKSALLDEKRHLEARIGQLEEELDEEQSNME-LLNDRYRKLSMQ 1791
Cdd:TIGR00618 616 ALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALqKMQSEKEQLTYW 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1792 VETLTTELGAERSFSQKTENARQQLERQNKDLraklgemdSSVKSKYKMAIATLESKVAQLEEQLEQESRERILSGKLVR 1871
Cdd:TIGR00618 696 KEMLAQCQTLLRELETHIEEYDREFNEIENAS--------SSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNN 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1872 RAEKKLKEVILQVDEERRNADQYKDQVEKGHLRLKQLKRQLEEAEEEASRA-NASRRRMQRELEDVTESAESMNREVTSL 1950
Cdd:TIGR00618 768 EEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDIlNLQCETLVQEEEQFLSRLEEKSATLGEI 847
|
730 740 750
....*....|....*....|....*....|...
gi 1033370542 1951 RNRLSKV-ERRQRKRTPLSFTTRTVRQVFRLDG 1982
Cdd:TIGR00618 848 THQLLKYeECSKQLAQLTQEQAKIIQLSDKLNG 880
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1195-1839 |
3.82e-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: 65.04 E-value: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1195 RSKREQEVTELKKTIEEEVKVHEAQVLDMRQRHTSALE---------ELSEQLEQSRRFKINLEKTK-QALEGENAEMQK 1264
Cdd:TIGR04523 31 QDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEkinnsnnkiKILEQQIKDLNDKLKKNKDKiNKLNSDLSKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1265 EVKLLQAAKLESEQRRKKLEGQVQELqlragegERAKAELVERLVKLQNELDGVSGTLGSTESKTIKLAKDLATVESHLQ 1344
Cdd:TIGR04523 111 EIKNDKEQKNKLEVELNKLEKQKKEN-------KKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1345 DTQELLQEETRQKLNLS---SRVRQLEEEKAAMLEQLEEEEAAKANFSRQMQSLQQQVMETKKKLEEDAGVAEAIEEARR 1421
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1422 RAAKDLESLSVRYEERVQACDKLEKGRTRLQQELDDvtvaLDQQRQ------VVSALEKKQKKFDQMLAE----EKLISa 1491
Cdd:TIGR04523 264 KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD----LNNQKEqdwnkeLKSELKNQEKKLEEIQNQisqnNKIIS- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1492 RYAEERDRAEADAREKETKVLSLSRALEEALETREEMERQNKQLRAEMDDLVSSKDDvgknvhelerfkraLEQQVQEMR 1571
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND--------------LESKIQNQE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1572 AQMEELEDELQATEDGKLRLEVNMQALKAQHERELQNRDDANdDKKKLLSKQVRELEAELDAERKQRAQALAGRKKLELD 1651
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT-NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1652 LQEAMAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEARAAREEIFIQSRESEKKLKNLEAELLQLQEDLAAS--ERAK 1729
Cdd:TIGR04523 484 LEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEnlEKEI 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1730 RQAQQERDDLA---DELANGNSGKSALLD----EKRHLEARIGQLEEELDEEQSNMELLNDRYRKLSMQVETLttelgae 1802
Cdd:TIGR04523 564 DEKNKEIEELKqtqKSLKKKQEEKQELIDqkekEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNI------- 636
|
650 660 670
....*....|....*....|....*....|....*...
gi 1033370542 1803 RSFSQKTENARQQLERQNKDLRAKLGEMDSSVK-SKYK 1839
Cdd:TIGR04523 637 KSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKeSKTK 674
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1093-1527 |
3.82e-10 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 429718 [Multi-domain] Cd Length: 488 Bit Score: 64.52 E-value: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1093 LQEQVAELQQQLEELRQALarkEAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQEDMESEKLARAKAEKQRRDLGE 1172
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQ---EAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKVEELEEKYKELSR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1173 ELEALKTELedtlDSTAAQQELRSKREQEVTELKKTIEEEVKVHEAQVLDMRQRHTSALEELSEQLEQSRRFKINLEKTk 1252
Cdd:pfam07888 109 SGEELAEEK----DALLAQRAESEARIRELEEDIKTLTQRVLERETELERMKERVKKAGAQRKEEEAERKQLQAKLQQT- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1253 qalEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGERAKAELVErlvkLQNELDGVSGTLGSTESKTIKL 1332
Cdd:pfam07888 184 ---EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEA----LLEELRSLQERLNASERKVEGL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1333 AKDLATVESHLQDTQELLQeetRQKLNLSSRVRQLEEEKAAMLEQleeeeaaKANFSRQMQSLQQQVMETKKKLEEDAGV 1412
Cdd:pfam07888 257 GEELSSMAAQRDRTQAELH---QARLQAAQLTLQLADASLALREG-------RARWAQERETLQQSAEADKDRIEKLSAE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1413 AEAIEEARRraakdleslsvryEERVQAcdklEKGRTRLQQELDDVTVALDQQRQVV----SALEKKQKKFDQMLAE--E 1486
Cdd:pfam07888 327 LQRLEERLQ-------------EERMER----EKLEVELGREKDCNRVQLSESRRELqelkASLRVAQKEKEQLQAEkqE 389
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1033370542 1487 KLISARYAEERDRAEADAREKETKVLSLSRALEEALETREE 1527
Cdd:pfam07888 390 LLEYIRQLEQRLETVADAKWSEAALTSTERPDSPLSDSEDE 430
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
25-70 |
4.18e-10 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 426949 Cd Length: 45 Bit Score: 56.67 E-value: 4.18e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1033370542 25 TAKRLVWVPSERHGFEAAGLREERGDEVMVELaENGRQVLVAKDDI 70
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1063-1303 |
7.91e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 63.20 E-value: 7.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1063 ADMEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQAALARVEDEAAQKNAVLKSLREL 1142
Cdd:COG4942 34 AADDKQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARLNALEVQEREQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1143 QAQLAELQedmeseklarAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVTELKKTIEEEVKVhEAQVLD 1222
Cdd:COG4942 114 RRRLAEQL----------AALQRSGRNPPPALLVSPEDAQRSVRLAIYYGALNPARAERIDALKATLKQLAAV-RAEIAA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1223 MRQRHTSALEELSEQLEQSRRFKINLEKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGERAKA 1302
Cdd:COG4942 183 EQAELTTLLSEQRAQQAKLAQLLEERKKTLAQLNSELSADQKKLEELRANESRLKNEIASAEAAAAKAREAAAAAEAAAA 262
|
.
gi 1033370542 1303 E 1303
Cdd:COG4942 263 R 263
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
887-1316 |
1.22e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.50 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 887 LQKVQEKHTKTQMDLKELENKYQQLSEEKTILAEQLQAETELFAEAEEMRARLAARKQELEDILHELESRVEEEEERCQQ 966
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 967 LQGDKKKMQQHVQDLEEQLEEEEAARQKLQLE-----KVSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEERLSEFTSHM 1041
Cdd:TIGR04523 286 LEKQLNQLKSEISDLNNQKEQDWNKELKSELKnqekkLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1042 AEEEEKVKSLSKLRNKYEAVMADMEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQaa 1121
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK-- 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1122 laRVEDEAAQKNAVLKSLR----ELQAQLAELQEDMESEKLARAKAEKQRRDLGEELEAL---KTELEDTLDSTAAQQEL 1194
Cdd:TIGR04523 444 --DLTNQDSVKELIIKNLDntreSLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLneeKKELEEKVKDLTKKISS 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1195 RSKREQEVTELKKTIEEEVKVHEAQVLDMRQRHTSalEELSEQLEQSRRFKINLEKTKQALEGENAEMQKEVKLLQAAKL 1274
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDLEDELNKDDFELKK--ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKK 599
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1033370542 1275 ESEQRRKKLEGQVQELQLRAGEGERAKAELVERLVKLQNELD 1316
Cdd:TIGR04523 600 DLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKN 641
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
790-1155 |
4.52e-09 |
|
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: 62.00 E-value: 4.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 790 GQSKIFFRAGVLAHLEEERDLKITDIIVSFQAAARgylARKAFMKKQQQMSALKVMQRNCAAYLKLRHWQWWRLFTKVKP 869
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEKIAELEKALAE---LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 870 LLQ-VTRQDEVMQAKAVELQKVQEKHTKTQMDLKELENKYQQLSEEKTILAEQLQAETELFAEAEEMRARLAARKQELED 948
Cdd:TIGR02168 745 LEErIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 949 ILHELESRVEEEEERCQQLQGDKKKMQQHVQDLEEQLEEEEAARQKLQLEKVSTEAKLKKMEEDLLVLEDQNSKLHKERK 1028
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1029 LMEERLSEFTSHMAEEEEKVKSLSKLRNKYEAVMADMEDRLKKEEK-GRQELEKLKRKLDGEAGDLQEQVAELQQQLEEL 1107
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1033370542 1108 RQALARKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQEDMES 1155
Cdd:TIGR02168 985 GPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1413-1958 |
4.83e-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: 61.66 E-value: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1413 AEAIEEARRRAAKDLESLSVRYEERVQACDKLEKGRTRLQQELDDVTVALDQQRQVVSALEKKQKKFDQMLAEEKLISAR 1492
Cdd:pfam05483 87 AEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCAR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1493 YAEERDRAEADAREKETKVLSLSRALEEALETREEMERQNKQLRAEMDdlVSSKDDVGKNVHELERFKRAL---EQQVQE 1569
Cdd:pfam05483 167 SAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMH--FKLKEDHEKIQHLEEEYKKEIndkEKQVSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1570 MRAQMEELEDELQateDGKLRLEVNMQALKaqherELQNRDDANDDKKKLLSKQVRELEAELDAERKQRAQALAGRKKLE 1649
Cdd:pfam05483 245 LLIQITEKENKMK---DLTFLLEESRDKAN-----QLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1650 LDLQEAMAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEARAAREEIFIQSRE----SEKKLKNLEAELLQLQEDLAAS 1725
Cdd:pfam05483 317 EDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQrlekNEDQLKIITMELQKKSSELEEM 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1726 ERAKRQAQQERDDLADELANgnsgKSALLDEKRHLEARIGQLEEELDEEQSNMELLNDRYRKLSMQVETLTTelgAERSF 1805
Cdd:pfam05483 397 TKFKNNKEVELEELKKILAE----DEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKT---SEEHY 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1806 SQKTENARQQLERQ-----------------NKDLRAKLGEMDSSVKSKYK-------------MAIATLESKVAQLEEQ 1855
Cdd:pfam05483 470 LKEVEDLKTELEKEklknieltahcdkllleNKELTQEASDMTLELKKHQEdiinckkqeermlKQIENLEEKEMNLRDE 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1856 LEQESRERIlsgklvrraeKKLKEVILQVDEERRNADQYKDQVEKGHLRLKQLKRQLEEAEEEASRANASRRRMQRELED 1935
Cdd:pfam05483 550 LESVREEFI----------QKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKA 619
|
570 580
....*....|....*....|...
gi 1033370542 1936 VTESAESMNREVTSLRNRLSKVE 1958
Cdd:pfam05483 620 LKKKGSAENKQLNAYEIKVNKLE 642
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1025-1279 |
5.64e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 60.51 E-value: 5.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1025 KERKLMEERLSEFTSHMAEEEEKVKSLSKLRNKYEAVMADMEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQL 1104
Cdd:COG4942 38 KQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARLNALEVQEREQRRRL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1105 EELRQALARKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQEDMEseklaraKAEKQRRDLGEELEALKTELEDT 1184
Cdd:COG4942 118 AEQLAALQRSGRNPPPALLVSPEDAQRSVRLAIYYGALNPARAERIDALK-------ATLKQLAAVRAEIAAEQAELTTL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1185 LDSTAAQQELRSKREQEVTELKKTIEEEVKVHEaQVLDMRQRHTSALEELSEQLEqsrrfkinLEKTKQALEGENAEMQK 1264
Cdd:COG4942 191 LSEQRAQQAKLAQLLEERKKTLAQLNSELSADQ-KKLEELRANESRLKNEIASAE--------AAAAKAREAAAAAEAAA 261
|
250
....*....|....*
gi 1033370542 1265 EVKLLQAAKLESEQR 1279
Cdd:COG4942 262 ARARAAEAKRTGETY 276
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1101-1946 |
7.59e-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: 61.22 E-value: 7.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1101 QQQLEELRQALARKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQEDMESEKLARAKAEKQRRDLGEELEALKtE 1180
Cdd:TIGR00606 188 LETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIM-K 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1181 LEDTLDSTAAQQElrsKREQEVTELKKTIEEEVKVHEAQVLDMRQRHTSALEELSEQLEQSRRFKINLEKTKQALEGENA 1260
Cdd:TIGR00606 267 LDNEIKALKSRKK---QMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKT 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1261 EMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRA------------------------GEGERAK------AELVERLVK 1310
Cdd:TIGR00606 344 ELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLeldgfergpfserqiknfhtlvieRQEDEAKtaaqlcADLQSKERL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1311 LQNELDGV----SGTLGSTESKTIKLAK----------DLATVESHLQDTQELLQEETRQKLNLS------------SRV 1364
Cdd:TIGR00606 424 KQEQADEIrdekKGLGRTIELKKEILEKkqeelkfvikELQQLEGSSDRILELDQELRKAERELSkaeknsltetlkKEV 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1365 RQLEEEKAAMLEQLEEEEAAKANFSRQMQSLQQQVMETKKKLEEDagvaEAIEEARRRAAKDLESLSVRYEERVQACDKL 1444
Cdd:TIGR00606 504 KSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKD----EQIRKIKSRHSDELTSLLGYFPNKKQLEDWL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1445 EKGRTRLQQ---ELDDVTVALDQQRQVVSALEKKQKKFDQMLA--EEKLISARYAE------ERDRAEADAREKETKVLS 1513
Cdd:TIGR00606 580 HSKSKEINQtrdRLAKLNKELASLEQNKNHINNELESKEEQLSsyEDKLFDVCGSQdeesdlERLKEEIEKSSKQRAMLA 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1514 LSRALEEALETreemerqnkQLRAEMDDLVSSKDDVGKNVHELERFKRALEQQVQEMRAQMEELEDELQATED------G 1587
Cdd:TIGR00606 660 GATAVYSQFIT---------QLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKrrdemlG 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1588 KLRLEVNMQALKAQHERELQNRD-DANDDKKKL---LSKQVRELEA----ELDAERKQRAQALAGRKKLEL-DLQEAMAQ 1658
Cdd:TIGR00606 731 LAPGRQSIIDLKEKEIPELRNKLqKVNRDIQRLkndIEEQETLLGTimpeEESAKVCLTDVTIMERFQMELkDVERKIAQ 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1659 LDAANKGRD------EAGKQLRKLQAQMKELWREVEEARAAREEIFIQSRESEKKLKNLEAELLQLQEDLAaserakrQA 1732
Cdd:TIGR00606 811 QAAKLQGSDldrtvqQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQ-------RR 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1733 QQERDDLADELANGNSGKSALLDEKRHLEARIGQLEEELDEEQSNMELLNDRYRKLSMQVETLTTELGAERSFSQKTENA 1812
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENK 963
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1813 RQQ-LERQNKDLRAKLGEMDSSVKSKYKMAIATLESKVAQLEEQLEQESRERILSGKLVRRaekKLKEVILQVDEERRNA 1891
Cdd:TIGR00606 964 IQDgKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLR---KRENELKEVEEELKQH 1040
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*
gi 1033370542 1892 DQYKDQVEKghLRLKQLKRQLEEAEEEASRANASRRRMQRELEDVTESAESMNRE 1946
Cdd:TIGR00606 1041 LKEMGQMQV--LQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE 1093
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1039-1424 |
9.88e-09 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteristic 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: 59.70 E-value: 9.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1039 SHMAEEEEKVKSLSKLRNKYEAVMADMEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAEL 1118
Cdd:pfam19220 13 GEMADRLEDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1119 QAALARVEDEAAQKNAVLKSLRELQAQLAELQEDMESEKLARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRSKR 1198
Cdd:pfam19220 93 AKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1199 EQEVTELKKTIEEEVkvheAQVLdmrqRHTSALEELSEQLEQSRRfkiNLEKTKQALEGENAEMQKEVKLLQAAKLESEQ 1278
Cdd:pfam19220 173 EQENRRLQALSEEQA----AELA----ELTRRLAELETQLDATRA---RLRALEGQLAAEQAERERAEAQLEEAVEAHRA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1279 RRKKLEGQVQELQLRAGEGERAKAELVERLVKLQNELDGVSGTLGSTESKTIKLAKDLATVESHLQDTQELLQEETRQKL 1358
Cdd:pfam19220 242 ERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARA 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1033370542 1359 NLSSRVRQLEEEKAAMLEQLEEEEAAKANFSRQMQSLQQQVMETKKKLEedAGVAEAIEEARRRAA 1424
Cdd:pfam19220 322 ELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEVERAALE--QANRRLKEELQRERA 385
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
903-1487 |
1.28e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 60.12 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 903 ELENKYQQLS---EEKTILAEQLQAETELFAE-AEEMRARLAARKQELEDILHELESRVEEEEERCQQLQGDKKKMQQHV 978
Cdd:pfam05483 251 EKENKMKDLTfllEESRDKANQLEEKTKLQDEnLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLT 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 979 QDLEEQLEEEEAARQKLQLEKVSTEAKLKKMEEdllVLEDQNSKLHKErklmEERLSEFTSHMAEEEEKVKSLSKLRNKY 1058
Cdd:pfam05483 331 EEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE---LLRTEQQRLEKN----EDQLKIITMELQKKSSELEEMTKFKNNK 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1059 EAvmadmedrlkkeekgrqELEKLKRKLDGEAGDLQEqvaelQQQLEELRQALARKEAE----LQAALARVEDEAAQKNA 1134
Cdd:pfam05483 404 EV-----------------ELEELKKILAEDEKLLDE-----KKQFEKIAEELKGKEQEliflLQAREKEIHDLEIQLTA 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1135 VLKSLRELQAQLAELQEDMESEKLARAKAEKQRRDLGEELEALKTELED-TLDSTAAQQELRSKREQEVTELKKTieEEV 1213
Cdd:pfam05483 462 IKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDmTLELKKHQEDIINCKKQEERMLKQI--ENL 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1214 KVHEAQVLDmrqrhtsALEELSEQLEQSR-RFKINLEKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQl 1292
Cdd:pfam05483 540 EEKEMNLRD-------ELESVREEFIQKGdEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIE- 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1293 ragegerakaELVERLVKLQNELDGVSGTLGSTESKTIKLAKDLATVESHLQDTQELLQEETRQKlNLSSRVRQLEEEKA 1372
Cdd:pfam05483 612 ----------ELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDK-KISEEKLLEEVEKA 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1373 AMLEQLEEEEAAKANFSRQMQSLQQQVMETKKKLEEDAGVAEAIEEARRRAAKDLESLSVRYeervqacdKLEKGRTRLQ 1452
Cdd:pfam05483 681 KAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKA--------ALEIELSNIK 752
|
570 580 590
....*....|....*....|....*....|....*
gi 1033370542 1453 QELDDVTVALDQQRQVVSALEKKQKKFDQMLAEEK 1487
Cdd:pfam05483 753 AELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1389-1958 |
1.65e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 59.79 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1389 SRQMQSLQQQVMETKKkleedagvaeaIEEARRRAAKDLESLSVRYEErvqacdkLEKGRTRLQQELDDVTVALDQQRQV 1468
Cdd:pfam01576 1 TRQEEEMQAKEEELQK-----------VKEKQQKAESELKELEKKHQQ-------LCEEKNILAEQLQAETELFAEAEEM 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1469 VSALEKKQKKFDQMLAEeklISARYAEERDRAEADAREK---ETKVLSLSRALEEALETREEMERQNKQLRAEM----DD 1541
Cdd:pfam01576 63 RARLAARKQELEEILHE---LEARLEEEEERSQQLQNEKkkmQQHIQDLEEQLEEEEAARQKLQLEKVTTEAKIkkmeED 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1542 LVSSKDDVGKnvheLERFKRALEQQVQEMRAQMEELEDELQATEDGKLRLEVNMQALKAQHERELQNRDDANDDKKKL-- 1619
Cdd:pfam01576 140 ILLLEDQNNK----LQKERKLLEERISEFTSNLAEEEEKSKSLNKLKNKHEAMISDLEDRLKKEEKGRQELEKAKRKLeg 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1620 ----LSKQVRELEAELDAERKQRAqalagrkKLELDLQEAMAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEARAARE 1695
Cdd:pfam01576 216 essdLQEQIAELQAQIAELRAQLA-------KKEEELQAALARLEEETAQKNAALKKLRELEAQLSELQEDLESERAARA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1696 EIFIQSRESEKKLKNLEAELLQLQEDLAASERAKRQAQQERDDLadelangnsgKSALLDEKRHLEARigqleeeldeeq 1775
Cdd:pfam01576 289 KAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTEL----------KKALEEETRSHEAQ------------ 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1776 snmelLNDRYRKLSMQVETLTTELGAERSFSQKTENARQQLERQNKDLRAKLgemdssvkskykmaiatleskvaqleeq 1855
Cdd:pfam01576 347 -----LQEMRQKHTQALEELTEQLEQAKRNKASLEKAKQALESENAELQAEL---------------------------- 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1856 leqesrerilsgklvrraeKKLKEVILQVDEERRNADQykdQVEKGHLRLKQLKRQLEEAEEEASranasrrRMQRELED 1935
Cdd:pfam01576 394 -------------------RSLQQAKQDSEHKRKKLEG---QLQELQSRLSESERQRAELAEKLS-------KLQSELES 444
|
570 580
....*....|....*....|...
gi 1033370542 1936 VTESAESMNREVTSLRNRLSKVE 1958
Cdd:pfam01576 445 VSSLLNEAEGKNIKLSKDVSSLE 467
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1209-1614 |
2.26e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.59 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1209 IEEEVKVHEAQVLDMRQrhtsALEELSEQLEQSRRFKINLEKTKQALEGENAEMQKEvklLQAAK------LESEQRRKK 1282
Cdd:PRK04863 277 HANERRVHLEEALELRR----ELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQD---YQAASdhlnlvQTALRQQEK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1283 LE---GQVQELQLRAGEGERAKAELVERLVKLQNELDgvsgtlgSTESKTIKLAKDLATVESHLqDTQELLQEETRQKLN 1359
Cdd:PRK04863 350 IEryqADLEELEERLEEQNEVVEEADEQQEENEARAE-------AAEEEVDELKSQLADYQQAL-DVQQTRAIQYQQAVQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1360 LSSRVRQLeeeKAAMLEQLEEEEAAKANFSRQMQSLQQQVMETKKKLeedaGVAEAIEEARRRAAKDLESL------SVR 1433
Cdd:PRK04863 422 ALERAKQL---CGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKL----SVAQAAHSQFEQAYQLVRKIagevsrSEA 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1434 YEERVQACDKLEKGRTR------LQQELDDVTVALDQQRQVVSALEKKQKKFDQMLAEEklisaryaeerDRAEADAREK 1507
Cdd:PRK04863 495 WDVARELLRRLREQRHLaeqlqqLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDE-----------DELEQLQEEL 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1508 ETKVLSLSRALEEALETREEMERQNKQLRAEMDDLvSSKDDVGKNVHE-LER----FKRALE--QQVQEMRAQMEELEDE 1580
Cdd:PRK04863 564 EARLESLSESVSEARERRMALRQQLEQLQARIQRL-AARAPAWLAAQDaLARlreqSGEEFEdsQDVTEYMQQLLERERE 642
|
410 420 430
....*....|....*....|....*....|....
gi 1033370542 1581 LQATEDgklRLEVNMQALKAQHEReLQNRDDAND 1614
Cdd:PRK04863 643 LTVERD---ELAARKQALDEEIER-LSQPGGSED 672
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1137-1529 |
2.55e-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: 58.98 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1137 KSLRELQAQlaELQEDMESEKLARAKAEK-----QRRDLGEELEALKTELEDTLDSTAAQQELRSKREQEvteLKKTIEE 1211
Cdd:pfam17380 282 KAVSERQQQ--EKFEKMEQERLRQEKEEKareveRRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERE---LERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1212 EVKVHEAQVldmRQrhtsalEELSEQLEQSRRfkinLEKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELq 1291
Cdd:pfam17380 357 ERKRELERI---RQ------EEIAMEISRMRE----LERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEM- 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1292 lragegERAKAElverlvklqneldgvsgtlgstesktiklakdlatveshlqdtqellQEETRQKlnlssRVRQLEEEK 1371
Cdd:pfam17380 423 ------EQIRAE-----------------------------------------------QEEARQR-----EVRRLEEER 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1372 AAMLEQLEEEEAAKanfSRQMQSLQQQVMETKKK---LEEDAGVAEAIEEARRRAakdlesLSVRYEERVQACDKLEKGR 1448
Cdd:pfam17380 445 AREMERVRLEEQER---QQQVERLRQQEEERKRKkleLEKEKRDRKRAEEQRRKI------LEKELEERKQAMIEEERKR 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1449 TRLQQELDDVTVALDQQRQVVSALEKKQKKfdQMLAEEKLISARY---AEERDRAEADAREKEtkvlsLSRALEEALETR 1525
Cdd:pfam17380 516 KLLEKEMEERQKAIYEEERRREAEEERRKQ--QEMEERRRIQEQMrkaTEERSRLEAMERERE-----MMRQIVESEKAR 588
|
....
gi 1033370542 1526 EEME 1529
Cdd:pfam17380 589 AEYE 592
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ... |
1076-1735 |
2.81e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 225638 [Multi-domain] Cd Length: 1480 Bit Score: 59.13 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1076 RQELEKLKRKLDGEagdlQEQVAELQQQLEELRQALARKEAELQAALARVedeaaqkNAVLKSLRE------LQAQLAEL 1149
Cdd:COG3096 292 RRELYTSRQQLAAE----QYRHVDMSRELAELNGAEGDLEADYQAASDHL-------NLVQTALRQqekierYQADLEEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1150 QEDMESEKLARAKAEKQRRD-------LGEELEALKTELEDTLDSTAAQQELRSKREQEVTELKKTIE---------EEV 1213
Cdd:COG3096 361 TIRLEEQNEVVEEANERQEEnearaeaAELEVDELKSQLADYQQALDVQQTRAIQYQQAIAALERAKElchlpdltaDSA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1214 KVHEAQVLDMRQRHTSALEELSEQLEQSRRFKINLEKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQ-VQELQL 1292
Cdd:COG3096 441 EEWLETFQAKEEEATEKLLSLEQKMSMAQAAHSQFEQAYQLVVAIAGELARSEAWDVARELLREGPDQRHLAEqVQPLRM 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1293 RAGEGER--AKAELVERLVKLQNELDGVSGTLGSTESKTIKLAKDLATVESHLQDTQELLQEETRQKLNLSSRVRQLEEE 1370
Cdd:COG3096 521 RLSELEQrlRQQQSAERLLADFCKRQGKNLDAEELEALHQELEALIESLSDSVSNAREQRMALRQEQEQLQSRIQSLMQR 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1371 -------KAAMLEQLEEEEAAKANFSRQMQSLQQQ-VMETKKKLEEDAgvaeaIEEARRRAAKDLESLSVRYEERVQACD 1442
Cdd:COG3096 601 apvwlaaQNALEQLSEQSGEEFTDSQDVTEYMQQLlEREREATVERDE-----LGARKNALDEEIERLSQPGGSEDQRLN 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1443 KLEK--GRTRLQQELDDVTV-------AL---DQQRQVVSALEKKQKKFDQMlaeEKLISARYAEERDRAEAD-----AR 1505
Cdd:COG3096 676 ALAErfGGVLLSEIYDDVTIedapyfsALygpSRHAIVVPDLSQVKEHLEGL---TDCPEDLYLIEGDPQSFDdsvfsVD 752
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1506 EKETKV--------LSLSRALEEALETREEMERQNKQLRAEMDDLVSSKDDVGKNVHELERFKRAL-------------- 1563
Cdd:COG3096 753 ELEKAVvvkiadrqWRYSRFPEIPLFGRAAREQRLESLHAERDVLSERHATLSFDVQKTQRLHQAFsrfigshlavafea 832
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1564 --EQQVQEMRAQMEELEDELQATEDGKLRLEVNMQALKA--QHERELQNRDDANDDKKklLSKQVRELEAELD-AERKQR 1638
Cdd:COG3096 833 dpEAEIRQLNSRRNELERALSNHENDNQQQRIQFDQAKEgvTALNRLIPQLNLLADES--LADRVEEIRERLDeAQEAAR 910
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1639 AQALAGRKKLELD-----LQEAMAQLDAANKGRDEAGKQLRKLQAQMKELwREVEEARA--AREEIFIQSRESEKKLKNL 1711
Cdd:COG3096 911 FIQQHGNTLSKLEpiasvLQSDPEQFEQLKEDYAQAQQMQRQARQQAFAL-TEVVQRRAhfSYSDSAEMLSENSDLNEKL 989
|
730 740
....*....|....*....|....
gi 1033370542 1712 EAELLQLQEDLAASERAKRQAQQE 1735
Cdd:COG3096 990 RQRLEQAEAERTRAREQLRQHQAQ 1013
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1137-1368 |
3.70e-08 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 58.11 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1137 KSLRELQAQLAELQEDMESEKLARAKAEKQRRDLGEELEALKTELEDT-LDSTAAQQELRSKREqevtELKKTIEEEVKV 1215
Cdd:COG4372 67 RNLRSGVFQLDDIRPQLRALRTELGTAQGEKRAAETEREAARSELQKArQEREAVRQELAAARQ----NLAKAQQELARL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1216 hEAQVLDMRQRhtsaLEELSEQLEQsrrfkinLEKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAg 1295
Cdd:COG4372 143 -TKQAQDLQTR----LKTLAEQRRQ-------LEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLATRA- 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1033370542 1296 egeRAKAELVERLVKLQNELDGVSGTLGSTESKTIKLAKDLATVESHLQDTQELLQEETRQKLNLSSRVRQLE 1368
Cdd:COG4372 210 ---NAAQARTEELARRAAAAQQTAQAIQQRDAQISQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQLE 279
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1503-1964 |
3.81e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1503 DAREKETK-VLSLSRaLEEALETREEMERQNKQLRAEMDDLVSSKDDVGKNVHELERFKRALEQQVQEMRAQMEELEDEL 1581
Cdd:PRK03918 145 ESREKVVRqILGLDD-YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1582 QATEDGKLRLEVNMQALKAQHERELQNRDDAN--DDKKKLLSKQVRELEAELDaERKQRAQALAGRKKLELDLQEAMAQL 1659
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRklEEKIRELEERIEELKKEIE-ELEEKVKELKELKEKAEEYIKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1660 DAANKGRDEAGKQLRKLQAQMKELWREVEEARAAREEIfiqsRESEKKLKNLEAELLQLQEDLAASERAK---------- 1729
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL----EELKKKLKELEKRLEELEERHELYEEAKakkeelerlk 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1730 -RQAQQERDDLADELANGNSGKSALLDEKRHLEARIGQLEEELDEEQSNMELLNDRYRKLSMQVETLTTELGAE--RSFS 1806
Cdd:PRK03918 379 kRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKEllEEYT 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1807 QKTENAR---QQLERQNKDLRAKLGEMDSSVKSK------YKMA--IATLESKVAQLE-EQLEQESRERilsgKLVRRAE 1874
Cdd:PRK03918 459 AELKRIEkelKEIEEKERKLRKELRELEKVLKKEseliklKELAeqLKELEEKLKKYNlEELEKKAEEY----EKLKEKL 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1875 KKLKEVILQVDEERRNADQYKDQVEKGHLRLKQLKRQLEEAEEEASRANASRrrmQRELEDVTESAESMNREVTSLRNRL 1954
Cdd:PRK03918 535 IKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFES---VEELEERLKELEPFYNEYLELKDAE 611
|
490
....*....|
gi 1033370542 1955 SKVERRQRKR 1964
Cdd:PRK03918 612 KELEREEKEL 621
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1277-1722 |
4.32e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.82 E-value: 4.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1277 EQRRKKLEgqvQELQLRAG--EGERAKAELVERLVKLQNELDGVSGTLGSTESktiklakDLATVESHLQDTQELL---Q 1351
Cdd:PRK04863 279 NERRVHLE---EALELRRElyTSRRQLAAEQYRLVEMARELAELNEAESDLEQ-------DYQAASDHLNLVQTALrqqE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1352 EETRQKLNLSSRVRQLEEEKAAMLEQLEEEEAAKAnfsrQMQSLQQQVMETKKKLeedAGVAEAIEEARRRAakdlesls 1431
Cdd:PRK04863 349 KIERYQADLEELEERLEEQNEVVEEADEQQEENEA----RAEAAEEEVDELKSQL---ADYQQALDVQQTRA-------- 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1432 VRYEERVQAcdkLEKGRTRLQqeLDDVTvaLDQQRQVVSALEKKQKKFDQML--AEEKLISAryaeerdraeADAREKET 1509
Cdd:PRK04863 414 IQYQQAVQA---LERAKQLCG--LPDLT--ADNAEDWLEEFQAKEQEATEELlsLEQKLSVA----------QAAHSQFE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1510 KVLSLSRAL------EEALETREEMERQNKQLRAEMDdlvsskddvgkNVHELERFKRALEQQVQEMRAQmEELEDELQA 1583
Cdd:PRK04863 477 QAYQLVRKIagevsrSEAWDVARELLRRLREQRHLAE-----------QLQQLRMRLSELEQRLRQQQRA-ERLLAEFCK 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1584 TEDGKLRLEVNMQALKAQHERELQNrddanddkkklLSKQVRELEAELDAERKQRAQALAGRKKLELDLQEAMAQLDAAN 1663
Cdd:PRK04863 545 RLGKNLDDEDELEQLQEELEARLES-----------LSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALA 613
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1033370542 1664 KGRDEAGKQL---RKLQAQMKELWREVEEARAAREEIFIQSRESEKKLKNL-------EAELLQLQEDL 1722
Cdd:PRK04863 614 RLREQSGEEFedsQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLsqpggseDPRLNALAERF 682
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
866-1586 |
6.67e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 57.80 E-value: 6.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 866 KVKPLLQV--TRQDEVMQAKAVELQKVQEKHTKTQMDLKELENKYQQLSEE-KTILAEQLQAETELFAEAEEMRARLAAR 942
Cdd:pfam15921 257 KIELLLQQhqDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQaRNQNSMYMRQLSDLESTVSQLRSELREA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 943 KQELEDILHELESRVEEEEERCQQLQGDKKKMQQhvqdleeqleeeeaarqklqlEKVSTEAKLKKMEEDllvledqnsk 1022
Cdd:pfam15921 337 KRMYEDKIEELEKQLVLANSELTEARTERDQFSQ---------------------ESGNLDDQLQKLLAD---------- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1023 LHKerklmeerlseftshmaeeEEKVKSLSKLRNKyeavmadmedRLKKEEKGRQ-ELEKLKRKLDGEAGDLQEQVAELQ 1101
Cdd:pfam15921 386 LHK-------------------REKELSLEKEQNK----------RLWDRDTGNSiTIDHLRRELDDRNMEVQRLEALLK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1102 QQLEELRQALARKEAELQAALARVEdEAAQKNAVLKSLRELqaqLAELQEDMESEKLARAKAEKQRRDLGEELEalktEL 1181
Cdd:pfam15921 437 AMKSECQGQMERQMAAIQGKNESLE-KVSSLTAQLESTKEM---LRKVVEELTAKKMTLESSERTVSDLTASLQ----EK 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1182 EDTLDSTAAQ-QELRSKREQEVTELKKTIEEEVKVHEAQV------LDMRQRhTSALEELSEQLEQSRRFKINLEKTKQA 1254
Cdd:pfam15921 509 ERAIEATNAEiTKLRSRVDLKLQELQHLKNEGDHLRNVQTecealkLQMAEK-DKVIEILRQQIENMTQLVGQHGRTAGA 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1255 LEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGERAKAELV----ERL--VK-LQNELDGVSGTLGSTES 1327
Cdd:pfam15921 588 MQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVnagsERLraVKdIKQERDQLLNEVKTSRN 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1328 KTIKLAKDLATVESHLQDTQELLQEETRQ-KLNLSSRVRQLEEEKAAMleqlEEEEAAKANFSRQMQSLQQQVMETKKKL 1406
Cdd:pfam15921 668 ELNSLSEDYEVLKRNFRNKSEEMETTTNKlKMQLKSAQSELEQTRNTL----KSMEGSDGHAMKVAMGMQKQITAKRGQI 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1407 EEDAGVAEAIEEARRRAAKDLESLSVRYEERVQACDKLEKGRTRLQQELDDVTVALDQQRQVVSALEKKQKKFDQMLAEE 1486
Cdd:pfam15921 744 DALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAEC 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1487 KLISARYAEERDRAE----ADAREKE----TKVLSLS-RALEEALETREEMERQNKQLRAEMDDLVSSKDDVGKnvhelE 1557
Cdd:pfam15921 824 QDIIQRQEQESVRLKlqhtLDVKELQgpgyTSNSSVKpRLLQPASFTRPHSNVPSSQSTASFLSHHSIKCEMLK-----E 898
|
730 740 750
....*....|....*....|....*....|
gi 1033370542 1558 RFKRALEQQVQEMRAQM-EELEDELQATED 1586
Cdd:pfam15921 899 DPTRDLKQLLQELRSVInEEPNVKLSKAEL 928
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1513-1662 |
8.30e-08 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 225288 [Multi-domain] Cd Length: 652 Bit Score: 57.41 E-value: 8.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1513 SLSRALEEALETREEMERQNKQLRAEMDDLVSSKD--DVGKNVHELERFKRALEQQVQEMRAQMEELEDELQatedgKLR 1590
Cdd:COG2433 389 PLAEALSKVKEEERPREKEGTEEEERREITVYEKRikKLEETVERLEEENSELKRELEELKREIEKLESELE-----RFR 463
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1033370542 1591 LEVNMQALKaqhERELQNRDDANDDKKKLL---SKQVRELEAELDAERKQRAQALAGR----KKLELDLQEAMAQLDAA 1662
Cdd:COG2433 464 REVRDKVRK---DREIRARDRRIERLEKELeekKKRVEELERKLAELRKMRKLELSGKgtpvKVVEKLTLEAIEEAEEE 539
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ... |
1212-1967 |
8.40e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 225638 [Multi-domain] Cd Length: 1480 Bit Score: 57.59 E-value: 8.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1212 EVKVHEAQVLDMRQRHTSALEELSeqLEQSRRFKINLEKTKQA-----LEGENAEMQKEVKLLQAAkLESEQRRKKLEGQ 1286
Cdd:COG3096 280 ERRVHLDQALEFRRELYTSRQQLA--AEQYRHVDMSRELAELNgaegdLEADYQAASDHLNLVQTA-LRQQEKIERYQAD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1287 VQELQLRAGEGERAKAELVERLVKlqneldgvsgtlgsTESKTIKLAKDLATVESHLQDTQELLQEETRQKLNLSSRVRQ 1366
Cdd:COG3096 357 LEELTIRLEEQNEVVEEANERQEE--------------NEARAEAAELEVDELKSQLADYQQALDVQQTRAIQYQQAIAA 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1367 LEEEKAAMLEQLEEEEAAKA---NFSRQMQSLQQQVMETKKKLEEDAGVAEAIEEARRRAAKDLESLSvRYEERVQACDK 1443
Cdd:COG3096 423 LERAKELCHLPDLTADSAEEwleTFQAKEEEATEKLLSLEQKMSMAQAAHSQFEQAYQLVVAIAGELA-RSEAWDVAREL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1444 LEKGRTR---------LQQELDDVTVALDQQRQVVSALEKKQKKFDQMLAEEKLisaryaeerdraEADAREKETKVLSL 1514
Cdd:COG3096 502 LREGPDQrhlaeqvqpLRMRLSELEQRLRQQQSAERLLADFCKRQGKNLDAEEL------------EALHQELEALIESL 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1515 SRALEEALETREEMERQNKQLRAEMDDLVSSKDDVGKNVHELERFKR------ALEQQVQEMRAQMEELEDELQATEDgk 1588
Cdd:COG3096 570 SDSVSNAREQRMALRQEQEQLQSRIQSLMQRAPVWLAAQNALEQLSEqsgeefTDSQDVTEYMQQLLEREREATVERD-- 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1589 lRLEVNMQALKAQHEReLQNRDDANDDKKKLLSKQ-----VRELEAELDAERKQRAQALAGRKKLEL---DLQEAMAQLd 1660
Cdd:COG3096 648 -ELGARKNALDEEIER-LSQPGGSEDQRLNALAERfggvlLSEIYDDVTIEDAPYFSALYGPSRHAIvvpDLSQVKEHL- 724
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1661 aanKGRDEAGKQLRKLQAQMKELWREVEEARAAREEIFIQSRESEKKLKNLEAELLQLQedlAASERAKRQAQQERDDLA 1740
Cdd:COG3096 725 ---EGLTDCPEDLYLIEGDPQSFDDSVFSVDELEKAVVVKIADRQWRYSRFPEIPLFGR---AAREQRLESLHAERDVLS 798
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1741 DELANGNSGKSALLDEKRHLEARIGQLEEELDEE--QSNMELLNDRYRKLsmqvetlttelgaERSFSQkTENARQQLER 1818
Cdd:COG3096 799 ERHATLSFDVQKTQRLHQAFSRFIGSHLAVAFEAdpEAEIRQLNSRRNEL-------------ERALSN-HENDNQQQRI 864
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1819 QNKDLRAKLGEMDSSVKSKYKMAIATLESKVAQLEEQLEQ-ESRERILSGKLVRRAEKKLKEVILQVDEErrNADQYKDQ 1897
Cdd:COG3096 865 QFDQAKEGVTALNRLIPQLNLLADESLADRVEEIRERLDEaQEAARFIQQHGNTLSKLEPIASVLQSDPE--QFEQLKED 942
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033370542 1898 VEKGHLRLKQLKRQLeeaeeeASRANASRRRMQRELEDVTESAESMNREVTSLRNRLSKVE-RRQRKRTPL 1967
Cdd:COG3096 943 YAQAQQMQRQARQQA------FALTEVVQRRAHFSYSDSAEMLSENSDLNEKLRQRLEQAEaERTRAREQL 1007
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ... |
891-1665 |
8.91e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 225638 [Multi-domain] Cd Length: 1480 Bit Score: 57.59 E-value: 8.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 891 QEKHTKTQMDLKELENKyqqLSEEKTILAEQLQAETELFAEAEEMRARLAARKQELEDILHELESRVEEEEERCQQLQG- 969
Cdd:COG3096 347 QEKIERYQADLEELTIR---LEEQNEVVEEANERQEENEARAEAAELEVDELKSQLADYQQALDVQQTRAIQYQQAIAAl 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 970 DKKKMQQHVQDLEEQLEEEEAArqKLQLEKVSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEERLSEFTSHMAEEEEKV- 1048
Cdd:COG3096 424 ERAKELCHLPDLTADSAEEWLE--TFQAKEEEATEKLLSLEQKMSMAQAAHSQFEQAYQLVVAIAGELARSEAWDVAREl 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1049 -------KSLSKLRNKYEAVMADMEDRLKKEEKGRQELEKLKRK--LDGEAGDLQEQVAELQQQLEEL----------RQ 1109
Cdd:COG3096 502 lregpdqRHLAEQVQPLRMRLSELEQRLRQQQSAERLLADFCKRqgKNLDAEELEALHQELEALIESLsdsvsnareqRM 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1110 ALARKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAE-----------LQEDMESEK---LARAKAEKQRRDLGEELE 1175
Cdd:COG3096 582 ALRQEQEQLQSRIQSLMQRAPVWLAAQNALEQLSEQSGEeftdsqdvteyMQQLLEREReatVERDELGARKNALDEEIE 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1176 ALKTEledtldSTAAQQELRSKREQEVTELKKTIEEEVKVHEA---QVLDMRQRHTSALEELS---EQLEQsrrfkinLE 1249
Cdd:COG3096 662 RLSQP------GGSEDQRLNALAERFGGVLLSEIYDDVTIEDApyfSALYGPSRHAIVVPDLSqvkEHLEG-------LT 728
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1250 KTKQAL---EGENAEMQKEVkllqaakLESEQRRKKLEGQVQELQLRAGE-------GERAKAELVERLVKLQNELDGVS 1319
Cdd:COG3096 729 DCPEDLyliEGDPQSFDDSV-------FSVDELEKAVVVKIADRQWRYSRfpeiplfGRAAREQRLESLHAERDVLSERH 801
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1320 GTLGSTESKTIKLAKDLAT-VESHLQDTQELLQEETRQKLNlsSRVRQLEEEkaamleqleeeeaaKANFSRQMQSLQQQ 1398
Cdd:COG3096 802 ATLSFDVQKTQRLHQAFSRfIGSHLAVAFEADPEAEIRQLN--SRRNELERA--------------LSNHENDNQQQRIQ 865
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1399 VMETKKkleedaGVAEAIEEARRRAAKDLESLSVRYEERVQACDKLEKGRTRLQQElddvTVALDQQRQVVSALEKKQKK 1478
Cdd:COG3096 866 FDQAKE------GVTALNRLIPQLNLLADESLADRVEEIRERLDEAQEAARFIQQH----GNTLSKLEPIASVLQSDPEQ 935
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1479 FDQMLAEEKLISARYAEERDRAEADAREKETKVlslSRALEEALETREEMERQNKQLRAEMDDLVS----SKDDVGKNVH 1554
Cdd:COG3096 936 FEQLKEDYAQAQQMQRQARQQAFALTEVVQRRA---HFSYSDSAEMLSENSDLNEKLRQRLEQAEAertrAREQLRQHQA 1012
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1555 ELERFKRALEQQVQEMRAQMEELEDELQATEDGKLRLEVNMQALKAQHERELQNRDDANDDKKKLLSKQVRELEAELDAE 1634
Cdd:COG3096 1013 QLSQYNQVLASLKSSYDTKKELLNELQQELQDIGVRADSGAEERARIRRDELHAQLSTNRSRRNQLEKQLTFCEAEMDNL 1092
|
810 820 830
....*....|....*....|....*....|.
gi 1033370542 1635 RKQraqalagRKKLELDLQEAMAQLDAANKG 1665
Cdd:COG3096 1093 TRK-------LRKLERDYFEMREQVVTAKAG 1116
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1025-1319 |
1.02e-07 |
|
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: 57.06 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1025 KERKLMEERLSEftshmaEEEEKVKSLSKLRNKYEAVMAdMEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQvaELQQQL 1104
Cdd:pfam17380 292 KFEKMEQERLRQ------EKEEKAREVERRRKLEEAEKA-RQAEMDRQAAIYAEQERMAMERERELERIRQE--ERKREL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1105 EELRQALARKEAELQAALARVEDEAAQKNAVLKslRELQAqlAELQEDMESEKLARAKAEKQrrdlgeELEALKTELEDt 1184
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELERLQMERQQKNERVR--QELEA--ARKVKILEEERQRKIQQQKV------EMEQIRAEQEE- 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1185 ldstAAQQELRSKREQEVTELKKTIEEEVKvheaqvldmRQRHtsaLEELSEQLEQSRRFKINLEKTKQ----ALEGENA 1260
Cdd:pfam17380 432 ----ARQREVRRLEEERAREMERVRLEEQE---------RQQQ---VERLRQQEEERKRKKLELEKEKRdrkrAEEQRRK 495
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033370542 1261 EMQKEVKLLQAAKLESEQRRKKLEGQVQELQ--------LRAGEGERAKAELVERLVKLQNELDGVS 1319
Cdd:pfam17380 496 ILEKELEERKQAMIEEERKRKLLEKEMEERQkaiyeeerRREAEEERRKQQEMEERRRIQEQMRKAT 562
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
885-1649 |
1.26e-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: 57.16 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 885 VELQKVQEKHTKTQMDLKELENKYQQLSE-EKTILAEQLQAETELfaeaEEMRARLAARKQELedilhelESRVEEEEER 963
Cdd:pfam12128 234 AGIMKIRPEFTKLQQEFNTLESAELRLSHlHFGYKSDETLIASRQ----EERQETSAELNQLL-------RTLDDQWKEK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 964 CQQLQGDKKkmqqhvqdleeqleeeeAARQKLQlekvSTEAKLKKMEEDLLVLEDQNSklhKERKLMEERLSEFTSHMAE 1043
Cdd:pfam12128 303 RDELNGELS-----------------AADAAVA----KDRSELEALEDQHGAFLDADI---ETAAADQEQLPSWQSELEN 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1044 EEEKVKSLSKLRNKYEAvmADMEDRLKKEEKGRQELEKLKRKLDG--EAGDLQEQVAE--LQQQLEELRQalarkeaELQ 1119
Cdd:pfam12128 359 LEERLKALTGKHQDVTA--KYNRRRSKIKEQNNRDIAGIKDKLAKirEARDRQLAVAEddLQALESELRE-------QLE 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1120 AALARVEDEAAQKNAVLKSLRELQAQLAELQEDMESEKLARAKAEKQRrdlgEELEALKTELEDTLDSTAAqqeLRSKRE 1199
Cdd:pfam12128 430 AGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAR----EEQEAANAEVERLQSELRQ---ARKRRD 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1200 QEVTELKktiEEEVKVHEAQvldmrqrhtSALEELSEQLEQSRRFKINLEKTKQALEGENAEmqkevKLLQAAKLeseqR 1279
Cdd:pfam12128 503 QASEALR---QASRRLEERQ---------SALDELELQLFPQAGTLLHFLRKEAPDWEQSIG-----KVISPELL----H 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1280 RKKLEGQVQElqlragegERAKAELVERLVKLQNELDGVSGTLGSTESKTIKLAKdlatVESHLQDTQELLQEETRQkln 1359
Cdd:pfam12128 562 RTDLDPEVWD--------GSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDK----AEEALQSAREKQAAAEEQ--- 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1360 LSSRVRQLEEEKAAMLEQLEEEEAAKANFSR---QMQSLQQQVMETKKKLEEDAgvaeaiEEARRRAAKDLESLSVRYEE 1436
Cdd:pfam12128 627 LVQANGELEKASREETFARTALKNARLDLRRlfdEKQSEKDKKNKALAERKDSA------NERLNSLEAQLKQLDKKHQA 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1437 RVQAC-DKLEKGRTRLQQELDDVTVALD-QQRQVVSALEKKQKKFDqmlAEEKLISARYAEERDRAEAD-------AREK 1507
Cdd:pfam12128 701 WLEEQkEQKREARTEKQAYWQVVEGALDaQLALLKAAIAARRSGAK---AELKALETWYKRDLASLGVDpdviaklKREI 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1508 ETKVLSLSRALEEALETREEMERQNKQLRAEMDDLVSSKDDVGKnvhELERFKRALEQQVQEMRAQMEELEDELQATEDG 1587
Cdd:pfam12128 778 RTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIER---AISELQQQLARLIADTKLRRAKLEMERKASEKQ 854
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1033370542 1588 KLRLEVNMQALKAQHERELQNRDDANDDKKKL-LSKQVRELEaelDAERKQRAQALAGRKKLE 1649
Cdd:pfam12128 855 QVRLSENLRGLRCEMSKLATLKEDANSEQAQGsIGERLAQLE---DLKLKRDYLSESVKKYVE 914
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1656-1995 |
1.29e-07 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 56.57 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1656 MAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEARAAREEIFIQSRESEKKLKNLEAELLQLQEDLAASERAKRQAQQE 1735
Cdd:COG4372 59 LAILFLLNRNLRSGVFQLDDIRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQQE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1736 RDDLADELANGNSGKSALLDEKRHLEARIGQLEEELDEEQSNMELLNDRYRKLSM---QVETLTTELGAERSFSQKTENA 1812
Cdd:COG4372 139 LARLTKQAQDLQTRLKTLAEQRRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLrsaQIEQEAQNLATRANAAQARTEE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1813 RQQLERQNKDLRAKLGEMDSSVKSKyKMAIATLESKVAQLEEQLEQESRERILSGKLVRRAEK--------KLKEVILQV 1884
Cdd:COG4372 219 LARRAAAAQQTAQAIQQRDAQISQK-AQQIAARAEQIRERERQLQRLETAQARLEQEVAQLEAyyqayvrlRQQAAATQR 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1885 DEERRNADQYKDQVEKGHLRLKQLKRQLEEAEEEASRANASRRRMQREL-EDVTESAESMNREVTSLRNRLSKV-----E 1958
Cdd:COG4372 298 GQVLAGAAQRVAQAQAQAQAQAQLLSSANRPAALRLRRSPRRGRRQRPVtRHTTRRRRPATRQSPSGREYVTRVtsagnY 377
|
330 340 350
....*....|....*....|....*....|....*..
gi 1033370542 1959 RRQRKRTPLSFTTRTVRQVFRLDGVSDEETEDPESDS 1995
Cdd:COG4372 378 VTGERLIPRFCDRATNRCVFATGEGRATPRCGPSSGS 414
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1073-1350 |
1.30e-07 |
|
Intermediate filament protein;
Pssm-ID: 425436 [Multi-domain] Cd Length: 313 Bit Score: 55.69 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1073 EKGRQeLEKLKRKLDGEAGDLQEQ---------------VAELQQQLEELRQALARKEAELQAALARVEDEAAQKNAVLK 1137
Cdd:pfam00038 18 DKVRF-LEQQNKDLETKISELRQKkgaepsrlyslyereIRELRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1138 SLRELQAQLAELQEDMESEKLARAKAEKQRRDLGEELEALKTEledtldstaaqqelrskREQEVTELKKTIEEE---VK 1214
Cdd:pfam00038 97 LRQSAEADIVGLRKDLDEATLARVDLEMKIESLKEELAFLKKN-----------------HEEEVRELQSQVSDTqvnVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1215 VHEAQVLDMrqrhTSALEELSEQLE-QSRRFKINLEKTKQA-LEGENAEMQKEVKLLQAAKLE-SEQRR--KKLEGQVQE 1289
Cdd:pfam00038 160 MDAARKLDL----TSALAEIRAQYEeIAEKNREEAEEWYQSkLEELQQAAARNGDALRSAKEEiTELRRqiQSLEIELQS 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033370542 1290 LQLRAGEGERAKAELVERlvkLQNELDGVSGTLGSTESktiKLAKDLATVESHLQDTQELL 1350
Cdd:pfam00038 236 LKKQKASLERQLAETEER---YELQLADYQELISELEA---ELQQIRQEMARQLREYQELL 290
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1391-1958 |
1.31e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.95 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1391 QMQSLQQQVMETKKKLEEDAGVAEAIEEARRRAAKDLESLSVRY-------EERVQACDKLEKGRTRLQQELDDVTVALD 1463
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYndlkkqkEELENELNLLEKEKLNIQKNIDKIKNKLL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1464 QQRQVVSALEKKQKKFDQMLAEEKLISARYAEERDRAEADAREKETKVLSLSRALEEALETREEMERQNKQLRAEmddlv 1543
Cdd:TIGR04523 198 KLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK----- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1544 sskddvgknvhelerfkralEQQVQEMRAQMEELEDELQatedgklRLEVNMQALKAQHERELQNRDDANDDKKKllsKQ 1623
Cdd:TIGR04523 273 --------------------QKELEQNNKKIKELEKQLN-------QLKSEISDLNNQKEQDWNKELKSELKNQE---KK 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1624 VRELEAELDAERKQRAQALAGRKKLELDLQEamaqLDAANKGRDEagkQLRKLQAQMKELWREVEEARAAREEIFIQSRE 1703
Cdd:TIGR04523 323 LEEIQNQISQNNKIISQLNEQISQLKKELTN----SESENSEKQR---ELEEKQNEIEKLKKENQSYKQEIKNLESQIND 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1704 SEKKLKNLEAELLQLQEDLAASERAKRQAQQERDDLADELANGNSGKSALLDEKRHLEARIGQLEEELDEEQSNMELLND 1783
Cdd:TIGR04523 396 LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1784 RYRKLSMQVETLTTELGAERSFSQKTENARQQLERQNKDLRAKLGEMDSSVKsKYKMAIATLESKVAQLEEQLE------ 1857
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE-KLESEKKEKESKISDLEDELNkddfel 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1858 ---------QESRERILSGKLVRRA-EKKLKEVILQVDEERRNADQYKDQVEKGHLRLKQLKRQLEEAEEEASRANASRR 1927
Cdd:TIGR04523 555 kkenlekeiDEKNKEIEELKQTQKSlKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIK 634
|
570 580 590
....*....|....*....|....*....|.
gi 1033370542 1928 RMQRELEDVTESAESMNREVTSLRNRLSKVE 1958
Cdd:TIGR04523 635 NIKSKKNKLKQEVKQIKETIKEIRNKWPEII 665
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
892-1541 |
1.35e-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: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 892 EKHTKTQMDLKELENKYQQLSE--EKTILAEQlqaetELFAEAEEMRARLAAR-KQELEDILHELESRVEEEEERCQQ-- 966
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNniEKMILAFE-----ELRVQAENARLEMHFKlKEDHEKIQHLEEEYKKEINDKEKQvs 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 967 -LQGDKKKMQQHVQDLEEQLEEEEAARQKLqlekvstEAKLKKMEEDLLVLEDQNSKLHKERKLMEERLSEFTSHMAEEE 1045
Cdd:pfam05483 244 lLLIQITEKENKMKDLTFLLEESRDKANQL-------EEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1046 EKVKSLSKLRNKyeaVMADMEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQAALARV 1125
Cdd:pfam05483 317 EDLQIATKTICQ---LTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1126 EDEAAQKNAVLKSLRELQAQLAELQEDMESeklarakaEKQRRDLGEELEAlkteledtldstaaqqelrskREQEVTEL 1205
Cdd:pfam05483 394 EEMTKFKNNKEVELEELKKILAEDEKLLDE--------KKQFEKIAEELKG---------------------KEQELIFL 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1206 KKTIEEEVKVHEAQVLDMR---QRHTSALEELSEQLEQSRRFKINLEKTKQALEGENAEMQKEV-----------KLLQA 1271
Cdd:pfam05483 445 LQAREKEIHDLEIQLTAIKtseEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEAsdmtlelkkhqEDIIN 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1272 AKLESEQRRKKLEG-QVQELQLRaGEGERAKAELVERLVKLQNELDGVSGTLGSTESKTIKLAKDLATVESHLQDTQell 1350
Cdd:pfam05483 525 CKKQEERMLKQIENlEEKEMNLR-DELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLK--- 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1351 qeetRQKLNLSSRVRQLEEEKAAMLEQLEEEEAAKANFSRQMQSLQQQVMETKKKLEEDAGVAEAIEEARRRAAKDLesl 1430
Cdd:pfam05483 601 ----KQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKL--- 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1431 svryEERVQACDKLEKGRTRLQQELDdvTVALDQQRQVVSALEKKQKKFDQMLAEEK----LISARYAEE---RDRAEAD 1503
Cdd:pfam05483 674 ----LEEVEKAKAIADEAVKLQKEID--KRCQHKIAEMVALMEKHKHQYDKIIEERDselgLYKNKEQEQssaKAALEIE 747
|
650 660 670
....*....|....*....|....*....|....*...
gi 1033370542 1504 AREKETKVLSLSRALEEALETREEMERQNKQLRAEMDD 1541
Cdd:pfam05483 748 LSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1455-1860 |
1.36e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.89 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1455 LDDVTVALDQQRQVVSALEKKQKKFD--QMLAEEKL--ISARYAeerdRAEADAREKETKVLSLSRALEEALETREEMER 1530
Cdd:PRK04863 232 FQDMEAALRENRMTLEAIRVTQSDRDlfKHLITESTnyVAADYM----RHANERRVHLEEALELRRELYTSRRQLAAEQY 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1531 QNKQLRAEMDDLVSSKDD------------------------VGKNVHELERFKRALEQQ---VQEMRAQMEELEDELQA 1583
Cdd:PRK04863 308 RLVEMARELAELNEAESDleqdyqaasdhlnlvqtalrqqekIERYQADLEELEERLEEQnevVEEADEQQEENEARAEA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1584 TEDGKLRLEVNM----QALKAQHERELQNRD--DANDDKKKLLS------KQVRELEAELDAERKQRAQALagrkkleLD 1651
Cdd:PRK04863 388 AEEEVDELKSQLadyqQALDVQQTRAIQYQQavQALERAKQLCGlpdltaDNAEDWLEEFQAKEQEATEEL-------LS 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1652 LQEAMAQLDAANKGRDEAGKQLRKLQAQM---------KELWREVEEAR--AAR-----------EEIFIQSRESEKKLK 1709
Cdd:PRK04863 461 LEQKLSVAQAAHSQFEQAYQLVRKIAGEVsrseawdvaRELLRRLREQRhlAEQlqqlrmrlselEQRLRQQQRAERLLA 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1710 NLEAELLQLQEDLAASERAKRQAQQERDDLADELANGNSGKSALLDEKRHLEARIGQleeeldeeqsnMELLNDRYRKLS 1789
Cdd:PRK04863 541 EFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQR-----------LAARAPAWLAAQ 609
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033370542 1790 MQVETLTTELGAERSFSQKTENARQQLERQNKDLRaklgemdssvkskykMAIATLESKVAQLEEQLEQES 1860
Cdd:PRK04863 610 DALARLREQSGEEFEDSQDVTEYMQQLLERERELT---------------VERDELAARKQALDEEIERLS 665
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
993-1358 |
1.66e-07 |
|
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: 56.37 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 993 QKLQLEKVSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEERLSEFTSHMAEEEEKVKSLSKLRNKYEAVMADMEDRLKKE 1072
Cdd:pfam10174 369 QDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEK 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1073 EKgrqELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQaalarvedeaaQKNAVLKSLRELQAQLAELQED 1152
Cdd:pfam10174 449 ER---IIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELT-----------EKESSLIDLKEHASSLASSGLK 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1153 MESEKLARAKAEKQRRdlgEELEALKTELEdtldsTAAQQELRSKREQEVTELKKTIEEEVKVHEaqvlDMRQRHTSALE 1232
Cdd:pfam10174 515 KDSKLKSLEIAVEQKK---EECSKLENQLK-----KAHNAEEAVRTNPEINDRIRLLEQEVARYK----EESGKAQAEVE 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1233 ELSEQLEQSRRFKINLEKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGERAKA------ELVE 1306
Cdd:pfam10174 583 RLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSqqlqleELMG 662
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1033370542 1307 RLVKLQNELDGVSGTLGSTESKtiklakdLATVESHLQDtqelLQEETRQKL 1358
Cdd:pfam10174 663 ALEKTRQELDATKARLSSTQQS-------LAEKDGHLTN----LRAERRKQL 703
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1347-1713 |
1.81e-07 |
|
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: 56.29 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1347 QELLQEETRQKLNLSSRVRQLEEEKAAMLEQLEEEEAAKANFSRQmqslqqqVMETKKKLEEdagvaeAIEEARRRAAKD 1426
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERM-------AMERERELER------IRQEERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1427 LESLSVRYE-ERVQACDKLEKGRtrlQQELDDVTVALDQQRQVVSALEKKQKKFDQMLAEEKLISARyaeerdraEADAR 1505
Cdd:pfam17380 365 IRQEEIAMEiSRMRELERLQMER---QQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE--------QEEAR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1506 EKETKVLSLSRALEEALETREEMERQnkqlraemddlvsskddvgknvHELERFKRALEQQVQEMRAQMEELEDELQATE 1585
Cdd:pfam17380 434 QREVRRLEEERAREMERVRLEEQERQ----------------------QQVERLRQQEEERKRKKLELEKEKRDRKRAEE 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1586 DGKLRLEVNMQALKAQHERElqnrddanDDKKKLLSKQVRELEAELDAERKQRAQALAGRKKLELDlqeamaqldaankg 1665
Cdd:pfam17380 492 QRRKILEKELEERKQAMIEE--------ERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEME-------------- 549
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1666 rdeagkQLRKLQAQMKELWREVE--EARAAREEIFIQSRESEKKLKNLEA 1713
Cdd:pfam17380 550 ------ERRRIQEQMRKATEERSrlEAMEREREMMRQIVESEKARAEYEA 593
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ... |
1094-1753 |
1.95e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 225638 [Multi-domain] Cd Length: 1480 Bit Score: 56.43 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1094 QEQVAELQQQLEELRQALARKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQEDMESEKlARAKAEKQRRDLGEE 1173
Cdd:COG3096 347 QEKIERYQADLEELTIRLEEQNEVVEEANERQEENEARAEAAELEVDELKSQLADYQQALDVQQ-TRAIQYQQAIAALER 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1174 LEALKTELEDTLDSTAAQQELRSKREQEVTELKKTIEEEVKVHEAQVLDMRQRH------------TSALEELSEQLEQS 1241
Cdd:COG3096 426 AKELCHLPDLTADSAEEWLETFQAKEEEATEKLLSLEQKMSMAQAAHSQFEQAYqlvvaiagelarSEAWDVARELLREG 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1242 RRFKINLEKTKQ------ALEGENAEMQKEVKLL-----------QAAKLESEQRRkkLEGQVQELQLRAGEGERAKAEL 1304
Cdd:COG3096 506 PDQRHLAEQVQPlrmrlsELEQRLRQQQSAERLLadfckrqgknlDAEELEALHQE--LEALIESLSDSVSNAREQRMAL 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1305 VERLVKLQNELD----------GVSGTLGSTESKTIKLAKDLATVESHLQDTQELLQEETRQKLNLSSRVRQLEEEKAAM 1374
Cdd:COG3096 584 RQEQEQLQSRIQslmqrapvwlAAQNALEQLSEQSGEEFTDSQDVTEYMQQLLEREREATVERDELGARKNALDEEIERL 663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1375 LEQLEEEEAAKANFSRQMQSLQQQVMETKKKLeEDAGVAEAIEEARRRA--AKDLESLSVRYEERVQACDKLEKGRTRLQ 1452
Cdd:COG3096 664 SQPGGSEDQRLNALAERFGGVLLSEIYDDVTI-EDAPYFSALYGPSRHAivVPDLSQVKEHLEGLTDCPEDLYLIEGDPQ 742
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1453 QELDDVTVALDQQRQVVSALEKKQKKFDQM--------LAEEKLISARYAEERDRAEA------DAREKETKVLSLSR-- 1516
Cdd:COG3096 743 SFDDSVFSVDELEKAVVVKIADRQWRYSRFpeiplfgrAAREQRLESLHAERDVLSERhatlsfDVQKTQRLHQAFSRfi 822
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1517 --------------ALEEALETREEMER-------QNKQLRAEMDDLVSSKDDVGKNVHELERF-KRALEQQVQEMRAQM 1574
Cdd:COG3096 823 gshlavafeadpeaEIRQLNSRRNELERalsnhenDNQQQRIQFDQAKEGVTALNRLIPQLNLLaDESLADRVEEIRERL 902
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1575 EEL-EDELQATEDG----KLRLEVNMQALKAQHERELQNRDDANDDKKKLLSKQVRELEAELdaERK------QRAQALA 1643
Cdd:COG3096 903 DEAqEAARFIQQHGntlsKLEPIASVLQSDPEQFEQLKEDYAQAQQMQRQARQQAFALTEVV--QRRahfsysDSAEMLS 980
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1644 GRKKLELDLQEAMAQLDAAnkgRDEAGKQLRKLQAQMKELwreveearaarEEIFIQSRESEKKLKNLEAELLQLQEDLA 1723
Cdd:COG3096 981 ENSDLNEKLRQRLEQAEAE---RTRAREQLRQHQAQLSQY-----------NQVLASLKSSYDTKKELLNELQQELQDIG 1046
|
730 740 750
....*....|....*....|....*....|..
gi 1033370542 1724 --ASERAKRQAQQERDDLADELANGNSGKSAL 1753
Cdd:COG3096 1047 vrADSGAEERARIRRDELHAQLSTNRSRRNQL 1078
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteristic of the AAA ... |
995-1238 |
2.86e-07 |
|
AAA domain; This family of domains contain a P-loop motif that is characteristic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 433006 [Multi-domain] Cd Length: 712 Bit Score: 55.84 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 995 LQLEKVSTEAKLKKMEEDLLVLE--DQNSKLHKE---------RKLMEERLSEFTSHMAEE-EEKVKSLSKLRNKYEAVM 1062
Cdd:pfam13166 220 LKQKVIGKSSAIAELIKNPDLADwvEEGLELHKAhldtcpfcgQPLPAERKAALEAHFDDEfTEFQRRLQKLIEKYESAI 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1063 ADMEDRLKK---EEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEElrqalARKEAELQAALARVEDEAAQKNAVLKSL 1139
Cdd:pfam13166 300 SSLLAQLPAvsdLASLLSAFELDVEDLKAEAEVLNSQLDGLRQALEA-----KRKEPFKSIELDSVDAKIESIKDLVAAI 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1140 RELQAQLAELQEDMESEKlarAKAEKQ-RRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVTELKKTIEEEVKVHEA 1218
Cdd:pfam13166 375 NELIAKHNEITDNLEEEK---NKAKKKlWLFLVEEFKAEIDEYKDAYAGLEKAINSLTKEIKNATAEIKKLRAEIRELEK 451
|
250 260
....*....|....*....|
gi 1033370542 1219 QVLDmrqrHTSALEELSEQL 1238
Cdd:pfam13166 452 QLRD----HKPGADEINKLL 467
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1514-1735 |
3.05e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 55.11 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1514 LSRALEEALETREEMERQNKQLRAEMDDLVSSKDDVGKNVHELERFKRALEQQVQEMRAQMEELEDELQATEDGKLRLEV 1593
Cdd:COG4942 22 LSAAVLAAAFSAAADDKQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1594 NMQALKAQHERE----------------------LQNRDDANDDKK---------KLLSKQVRELEAELDAERKQRAQAL 1642
Cdd:COG4942 102 RLNALEVQEREQrrrlaeqlaalqrsgrnpppalLVSPEDAQRSVRlaiyygalnPARAERIDALKATLKQLAAVRAEIA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1643 AGRKKLELDLQEAMAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEARAAREEIfiqsresEKKLKNLEAELLQLQEDL 1722
Cdd:COG4942 182 AEQAELTTLLSEQRAQQAKLAQLLEERKKTLAQLNSELSADQKKLEELRANESRL-------KNEIASAEAAAAKAREAA 254
|
250
....*....|...
gi 1033370542 1723 AASERAKRQAQQE 1735
Cdd:COG4942 255 AAAEAAAARARAA 267
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1495-1959 |
3.14e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1495 EERDRAeADAREKETKVLSLSRALEEALETREEmERQNKQLRAEMDDLVSSKDDVGKnvhELERFkralEQQVQEMRAQM 1574
Cdd:PRK02224 166 EYRERA-SDARLGVERVLSDQRGSLDQLKAQIE-EKEEKDLHERLNGLESELAELDE---EIERY----EEQREQARETR 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1575 EELEDELQATEDGKLRLEVNMQALkaqheRELQNRDDANDDKKKLLSKQVRELEAELDAERKQRAQALAGRKKLELDLQE 1654
Cdd:PRK02224 237 DEADEVLEEHEERREELETLEAEI-----EDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1655 AMAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEARAAREEIFIQSRESEKKLKNLEAELlqlqeDLAASERAKRQAQQ 1734
Cdd:PRK02224 312 VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESEL-----EEAREAVEDRREEI 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1735 ErddladelangnsgksALLDEKRHLEARIGQLEEELDEEQSNMELLNDRYRKLSMQVETLTTELgaeRSFSQKTENARQ 1814
Cdd:PRK02224 387 E----------------ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL---RTARERVEEAEA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1815 QLERQN-----KDLRaklGEMDSSVKSKYKMAIATLESKVAQLEEQLEqESRERILSGKLVRRAEKKLKEVILQVDEERR 1889
Cdd:PRK02224 448 LLEAGKcpecgQPVE---GSPHVETIEEDRERVEELEAELEDLEEEVE-EVEERLERAEDLVEAEDRIERLEERREDLEE 523
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1890 NADQYKDQVEKGHLRLKQLKRQLEEAEEEASRANASRRRMQRELEDVTESAESMNREVTSLRNRLSKVER 1959
Cdd:PRK02224 524 LIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER 593
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
833-1367 |
3.49e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 55.49 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 833 MKKQQQMSALKVMQRNCAAYLKLrhwQWWRLFTKVKPLLQVTRQDEVMQAKAVELQKVQEKHTKTQMdlkELENKYQQLS 912
Cdd:pfam15921 426 MEVQRLEALLKAMKSECQGQMER---QMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKM---TLESSERTVS 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 913 EEKTILAEQLQAETELFAEAEEMRARLAARKQELEDIL----HELESRVEEEEERCQQLQGDK--KKMQQHVQDLEEQLE 986
Cdd:pfam15921 500 DLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKnegdHLRNVQTECEALKLQMAEKDKviEILRQQIENMTQLVG 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 987 EEEAARQKLQLEKVSTEAKL--KKME-EDLLVLEDQNSKLHKErklMEERLSEFtshmaeEEEKVKSLSKLRNKYEAVMA 1063
Cdd:pfam15921 580 QHGRTAGAMQVEKAQLEKEIndRRLElQEFKILKDKKDAKIRE---LEARVSDL------ELEKVKLVNAGSERLRAVKD 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1064 DMEDR---LKKEEKGRQEL-------EKLKR-------KLDGEAGDLQEQVAELQQQLEELRQALARKEAELQAALARVE 1126
Cdd:pfam15921 651 IKQERdqlLNEVKTSRNELnslsedyEVLKRnfrnkseEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAM 730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1127 DEAAQKNAVLKSLRELQAQLAELQEDMESEKLARAKAEKQRRDLGEELEALKTEledtldSTAAQQELRSKREQEVTELK 1206
Cdd:pfam15921 731 GMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE------KNKMAGELEVLRSQERRLKE 804
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1207 KTIEEEVKVHEAQVldmrqRHTSALEELSEQLEQSRRFKINLEKTKQALEGENAEMQKEVK--LLQ-AAKLESEQRRKKL 1283
Cdd:pfam15921 805 KVANMEVALDKASL-----QFAECQDIIQRQEQESVRLKLQHTLDVKELQGPGYTSNSSVKprLLQpASFTRPHSNVPSS 879
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1284 EGQVQELQLRAGEGERAKAELVERLVKLQNELDGV---SGTLGSTESKTIKLAKDLATVESHLQD--TQELLQEETRQKL 1358
Cdd:pfam15921 880 QSTASFLSHHSIKCEMLKEDPTRDLKQLLQELRSVineEPNVKLSKAELVGRQTSLGALEDRVRDciIESSLRSDICHSS 959
|
....*....
gi 1033370542 1359 NLSSRVRQL 1367
Cdd:pfam15921 960 STVFETECL 968
|
|
| HEC1 |
COG5185 |
Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, ... |
908-1266 |
3.73e-07 |
|
Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227512 [Multi-domain] Cd Length: 622 Bit Score: 55.37 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 908 YQQLSEEKTILAEQLQAETELFAEaeEMRARLAARKQELEDILHELESRVEEEEERcQQLQGDKKKMQQhvqDLEEQLEE 987
Cdd:COG5185 244 FLKLEDNYEPSEQELKLGFEKFVH--IINTDIANLKTQNDNLYEKIQEAMKISQKI-KTLREKWRALKS---DSNKYENY 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 988 EEAARQKLQ-----LEKVSTEAKLKkmEEDLLVLEDQNSKLHKERKLMEERLSEFTSHMAEEEEKVKSLSKLRNKYEAVM 1062
Cdd:COG5185 318 VNAMKQKSQewpgkLEKLKSEIELK--EEEIKALQSNIDELHKQLRKQGISTEQFELMNQEREKLTRELDKINIQSDKLT 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1063 ADMEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQqleelrqalARKEAELQAALARV-EDEAAQKNAVLKSLRE 1141
Cdd:COG5185 396 KSVKSRKLEAQGIFKSLEKTLRQYDSLIQNITRSRSQIGH---------NVNDSSLKINIEQLfPKGSGINESIKKSILE 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1142 LQAQLAELQEDMESEKLARAKAEKQRRDLGEELEALKTELEDTLdSTAAQQELRSKREQEVTELKKTIEEEVKVHEAQVL 1221
Cdd:COG5185 467 LNDEIQERIKTEENKSITLEEDIKNLKHDINELTQILEKLELEL-SEANSKFELSKEENERELVAQRIEIEKLEKELNDL 545
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1033370542 1222 DMrQRHTSALEelSEQLEQSRRfkINLEKTKQALEGENAEMQKEV 1266
Cdd:COG5185 546 NL-LSKTSILD--AEQLVQSTE--IKLDELKVDLNRKRYKIHKQV 585
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
1634-1963 |
3.83e-07 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 55.49 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1634 ERKQRAQALAGRKKLELDLQEAMAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEAraareeifiqsreseKKLKNLEA 1713
Cdd:COG1196 156 ERRKLIEEAAGVSKYKERKEEAERKLERTEENLERLEDLLEELEKQLEKLERQAEKA---------------ERYQELKA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1714 ELLQLQEDLAASEraKRQAQQERDDLADELANGNSGKSALLDEKRHLEARIgqleeeldeeqsnmELLNDRYRKLSMQVE 1793
Cdd:COG1196 221 ELRELELALLLAK--LKELRKELEELEEELSRLEEELEELQEELEEAEKEI--------------EELKSELEELREELE 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1794 TLTTELGAERSFSQKTENARQQLERQNKDLRAKLGEMDSSVKsKYKMAIATLESKVAQLEEQLEQESRERILSGKLVRRA 1873
Cdd:COG1196 285 ELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLE-ELKEKIEALKEELEERETLLEELEQLLAELEEAKEEL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1874 EKKLKEVILQVDEE----RRNADQYKDQVEKGHLRLKQLKRQLEEAEEEASRANASRRRMQRELEDVTESAESMNREVTS 1949
Cdd:COG1196 364 EEKLSALLEELEELfealREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEE 443
|
330
....*....|....
gi 1033370542 1950 LRNRLSKVERRQRK 1963
Cdd:COG1196 444 LNEELEELEEQLEE 457
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
998-1536 |
5.53e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 428520 [Multi-domain] Cd Length: 660 Bit Score: 54.74 E-value: 5.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 998 EKVSTEAKLKKMEEDLlvleDQNSKLHK-ERKLMEERLSEFTSHMAEEEEK-------VKSLSKLRNKYEAVMADMEDRL 1069
Cdd:pfam05557 3 ELIESKARLSQLQNEK----KQMELEHKrARIELERKASALARQLERESDRnqelqkrIRLLEKREAEAEEALREQAELN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1070 KKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQAALARVEDEAAQknavLKSLRELQAQLAEL 1149
Cdd:pfam05557 79 RLKKKNLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRQELELSSTNSELEELQER----LDLQKAKAQEAEQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1150 QEDMESEKLARAKAEKQRRDL----------GEELEALKTELEDTLDSTAAQQELRSKREQ-------------EVTELK 1206
Cdd:pfam05557 155 RQNLEAQQSSLAEAEQRIKELefeiqsqeqdSEIVKNSKSELARIPELERELERLREHNKHlnenienklllkeEVEDLK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1207 KTIEEEVKVH-EAQVLDMRQRHTSALEELSEQLEQS-----------RRFKINLEKTKQALEGENAEMQKEVKLLQAAKL 1274
Cdd:pfam05557 235 RKLEREEGYReELATLELEKEKLEQELKSWEKLAQDtglnlrspedlSRRIEQLQQREITLKEENSSLTSSARQLEKAQR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1275 ESEQRRKKLEGQVQELQLRAGEGERAKAELVERLVKLQNELDGVSGTLGSTEsktiklaKDLATVESHLQDTQ------E 1348
Cdd:pfam05557 315 ELEQELAQYLKNIEDLNKKLKRHKALVRRLQRRVLLLTKERDGMRAILESYD-------KELTPSNYSPQLLErieeaeD 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1349 LLQEETRQKLNLSSRVRQLEEEKAAMLEQLeeeeaakANFSRQMQSLQQQVmetkkkLEEDAGVAEAIEEARRRAAKDLE 1428
Cdd:pfam05557 388 MTQDMQAHNEEMEAQLSVAEEELGGYKQQA-------TTLERELQALRQQE------SLADPSYSKEEVDSLRRKLETLE 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1429 SLSVRYEERVQACDkLEKGRTRLQQELDDVTVALDQQRQVVSALEKKQKKFDQMLAEEKLISARyaeERDRAEADAREKE 1508
Cdd:pfam05557 455 AERQRLREQKNELE-MELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRANDLEKLQAEIERLK---RRLKKLEDDLEQV 530
|
570 580 590
....*....|....*....|....*....|
gi 1033370542 1509 TKVL--SLSRALEEALETREEMERQNKQLR 1536
Cdd:pfam05557 531 GSLPetTSTMNFKEVLELRKELESAELKNQ 560
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1097-1373 |
5.79e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 54.34 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1097 VAELQQQLEELRQALARKEAElqaaLARVEDEAAQknavlkslreLQAQLAELQEDMeseklarAKAEKQRRDLGEELEA 1176
Cdd:COG4942 33 AAADDKQLKQIQKEIAALEKK----IREQQDQRAK----------LEKQLKSLETEI-------ASLEAQLIETADDLKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1177 LKTELEDTLDSTAAQQELRSKREQEVTELkktieeevkvheAQVLDMRQRHTSALEELS-EQLEQSRRFKINLEKTKQAL 1255
Cdd:COG4942 92 LRKQIADLNARLNALEVQEREQRRRLAEQ------------LAALQRSGRNPPPALLVSpEDAQRSVRLAIYYGALNPAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1256 EGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGERAKAELVERLVKLQNELDGVSGTLGSTESKTIKLAKD 1335
Cdd:COG4942 160 AERIDALKATLKQLAAVRAEIAAEQAELTTLLSEQRAQQAKLAQLLEERKKTLAQLNSELSADQKKLEELRANESRLKNE 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 1033370542 1336 LATVEshLQDTQELLQEETRQKLNLssRVRQLEEEKAA 1373
Cdd:COG4942 240 IASAE--AAAAKAREAAAAAEAAAA--RARAAEAKRTG 273
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
880-1314 |
5.83e-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: 54.73 E-value: 5.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 880 MQAKAVELQKVQEKHTKTQMDLKELEnkyQQLSEEKTILAEQLQAET---ELFAEAEEMRARLAARKQELEDIlhelesr 956
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEVELEELK---KILAEDEKLLDEKKQFEKiaeELKGKEQELIFLLQAREKEIHDL------- 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 957 veeeeercqqlqgdkkKMQQHVQDLEEQLEEEEAARQKLQLEKvsteAKLKKMEedllvLEDQNSKLHKERKLMEERLSE 1036
Cdd:pfam05483 456 ----------------EIQLTAIKTSEEHYLKEVEDLKTELEK----EKLKNIE-----LTAHCDKLLLENKELTQEASD 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1037 FTSHMAEEEEKVKSLSKlrnKYEAVMADMEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEA 1116
Cdd:pfam05483 511 MTLELKKHQEDIINCKK---QEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEK 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1117 ELQAALARVEDEAAQKNAVLKSLRELQAQLAELQEDMESEKLARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRS 1196
Cdd:pfam05483 588 QMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKK 667
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1197 KREQ----EVTELKKTIEEEVKVHEAqvLDMRQRHTSAlEELSEQLEQSRRFKINLEKTKQALEGENAEMQKEVKLLQAA 1272
Cdd:pfam05483 668 ISEEklleEVEKAKAIADEAVKLQKE--IDKRCQHKIA-EMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAAL 744
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1033370542 1273 KLESEQRRKKLEGQVQELQLRAGEGERAKAELVERLVKLQNE 1314
Cdd:pfam05483 745 EIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1104-1880 |
8.43e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.46 E-value: 8.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1104 LEELRQALARKEAELQAA----LARVEDEAAQKNAVLKSLRELQAQLAELQEDMESEKLaRAKAEKQRRDLgEELEALKT 1179
Cdd:pfam12128 181 IDKIAKAMHSKEGKFRDVksmiVAILEDDGVVPPKSRLNRQQVEHWIRDIQAIAGIMKI-RPEFTKLQQEF-NTLESAEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1180 ELEDTLDSTAAQQELRSKREQEVTELKKTIEEEVKVHEAQVLDMRQRHTSALEELSEQLEQSRRFKINLEKTKQALEGEN 1259
Cdd:pfam12128 259 RLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDAD 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1260 AEM----QKEVKLLQAAKLESEQRRKKLEGQVQELQlragegerAKAELVERLVKLQNELDgVSGTLGSTESKTIKLAKD 1335
Cdd:pfam12128 339 IETaaadQEQLPSWQSELENLEERLKALTGKHQDVT--------AKYNRRRSKIKEQNNRD-IAGIKDKLAKIREARDRQ 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1336 LATVESHLQDTQELLQEETRQKLNLSSRVRQLEEEKAAmleqleeeeaakanfsrQMQSLQQQVMETKKKLEEDAGVAEA 1415
Cdd:pfam12128 410 LAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLG-----------------ELKLRLNQATATPELLLQLENFDER 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1416 IEEARrraakdlESLSVRYEERVQACDKLEKGRTRLQQelddvtvALDQQRQVVSALEKKQKKFDQmlAEEKLISARYA- 1494
Cdd:pfam12128 473 IERAR-------EEQEAANAEVERLQSELRQARKRRDQ-------ASEALRQASRRLEERQSALDE--LELQLFPQAGTl 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1495 EERDRAEA-DAREKETKVLSlsraleealetREEMERQnkqlraemdDLVSSKDDvGKNVHELERFKRALeqqvqemRAQ 1573
Cdd:pfam12128 537 LHFLRKEApDWEQSIGKVIS-----------PELLHRT---------DLDPEVWD-GSVGGELNLYGVKL-------DLK 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1574 MEELEDELQATEDGKLRLEVNMQALKAQHERELQnrddanddkkklLSKQVRELEAELDAERKQRAQALAGRKKLELDLQ 1653
Cdd:pfam12128 589 RIDVPEWAASEEELRERLDKAEEALQSAREKQAA------------AEEQLVQANGELEKASREETFARTALKNARLDLR 656
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1654 ----EAMAQLDAANKGR----DEAGKQLRKLQAQMKELWREVEEARAAREEIFIQSR-ESEKKLKNLEAELlQLQEDLAA 1724
Cdd:pfam12128 657 rlfdEKQSEKDKKNKALaerkDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARtEKQAYWQVVEGAL-DAQLALLK 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1725 SERAKRQAQQERDDLADELANGNSGKSALLDEkrhlearigqleeeldeeqsnmellnDRYRKLSMQVETLTTELGAERS 1804
Cdd:pfam12128 736 AAIAARRSGAKAELKALETWYKRDLASLGVDP--------------------------DVIAKLKREIRTLERKIERIAV 789
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1033370542 1805 FSQKTENARQQLERQNKDLRAKLGEMDSSVKSKYKMAIATLESKVAQLEEQLEQESRERILSGKLVRRAEKKLKEV 1880
Cdd:pfam12128 790 RRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGL 865
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
886-1270 |
1.00e-06 |
|
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: 53.87 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 886 ELQKVQEKHTKTQMDLKELENKYQQLSEEKTILAEQLQAETelfaeAEEMRARLAARKQELEDI---LHELESRVEEEEE 962
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDW-----NKELKSELKNQEKKLEEIqnqISQNNKIISQLNE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 963 RCQQLQGDKKKMQQHVQDLEEQLEEEEAARQKLQLEKVSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEERLSEFTSHMA 1042
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1043 EEEEKVKSLSKLRNKYEAVMADMEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQaAL 1122
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELK-KL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1123 ARVEDEAAQKNAVLKSlreLQAQLAELQEDMESEKLaraKAEKQRRDLGEELEALKTELEDTL--DSTAAQQELRSKREQ 1200
Cdd:TIGR04523 502 NEEKKELEEKVKDLTK---KISSLKEKIEKLESEKK---EKESKISDLEDELNKDDFELKKENleKEIDEKNKEIEELKQ 575
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1033370542 1201 EVTELKKT---IEEEVKVHEAQVLDMRQR---HTSALEELSEQLEQSRRFKINLEKTKQALEGENAEMQKEVKLLQ 1270
Cdd:TIGR04523 576 TQKSLKKKqeeKQELIDQKEKEKKDLIKEieeKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
835-1508 |
1.16e-06 |
|
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: 53.90 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 835 KQQQMSALKVMQRNCAAYLKLRHWqwwRLFTKVKPLLQVTRQDEVMQAKAVELQKVQEKHTKTQMDLKELE---NKYQQL 911
Cdd:TIGR00606 424 KQEQADEIRDEKKGLGRTIELKKE---ILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEknsLTETLK 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 912 SEEKTILAEQLQAETELFAEAEEMrarlaARKQELEDILHELESRVEEEEERCQQLQGDKKKMQQHVQDLEEQ---LEEE 988
Cdd:TIGR00606 501 KEVKSLQNEKADLDRKLRKLDQEM-----EQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYfpnKKQL 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 989 EAARQKLQLEKVSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEERLSEFTSHMAE----EEEKVKsLSKLRNKYE----- 1059
Cdd:TIGR00606 576 EDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDvcgsQDEESD-LERLKEEIEksskq 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1060 --------AVMADMEDRLKKEEKGR----QELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQAALARVED 1127
Cdd:TIGR00606 655 ramlagatAVYSQFITQLTDENQSCcpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPG 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1128 EAAQKNAVLKSLRELQAQLAELQEDMESEKLARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRskreqevtELKK 1207
Cdd:TIGR00606 735 RQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELK--------DVER 806
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1208 TIEEEVKvhEAQVLDMRQRHTSALEELSEQLEQSRRFKINLEKTKQALEgenaEMQKEVKLLQAAKLESEQRRkklegqv 1287
Cdd:TIGR00606 807 KIAQQAA--KLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQ----DQQEQIQHLKSKTNELKSEK------- 873
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1288 qelqLRAGEGERAKAELVERLVKLQNELDGVSGTLGSTESKTIKLAKdlaTVESHLQDTQELLQEETRQKLNLSSRVRQL 1367
Cdd:TIGR00606 874 ----LQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLET---FLEKDQQEKEELISSKETSNKKAQDKVNDI 946
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1368 EEE-KAAMLEQLEEEEAAKANFSRQMQSLQQQVMETKKKLEEDAGVAEAIEEARRRAAKDLESLSVRYE------ERVQA 1440
Cdd:TIGR00606 947 KEKvKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERwlqdnlTLRKR 1026
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033370542 1441 CDKLEKGRTRLQQELDDvtVALDQQRQVVSALEKKQKKFDQMLAEEKLISAR---YAEERDRAEADAREKE 1508
Cdd:TIGR00606 1027 ENELKEVEEELKQHLKE--MGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRqkgYEKEIKHFKKELREPQ 1095
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1173-1726 |
1.74e-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: 428520 [Multi-domain] Cd Length: 660 Bit Score: 53.19 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1173 ELEALKTELEDtLDSTAAQQELRSKREQ-----EVTELKKTIEEEVKVHEAQVLDMRQ---RHTSALEELSEQLEQSRRF 1244
Cdd:pfam05557 3 ELIESKARLSQ-LQNEKKQMELEHKRARielerKASALARQLERESDRNQELQKRIRLlekREAEAEEALREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1245 KINLEKTKQALEgenaemQKEVKLLQAAKLES----EQRRKKLEGQVQELQLRAGEGEraKAELVERLVKLQNELDGVSG 1320
Cdd:pfam05557 82 KKNLEALNKKLN------EKESQLADAREVISclknELSELRRQIQRQELELSSTNSE--LEELQERLDLQKAKAQEAEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1321 TLGSTESKTiklaKDLATVESHLQDTQELLQEETRQKL---NLSSRVRQLEEekaamleqleeeeaakanfsrqMQSLQQ 1397
Cdd:pfam05557 154 LRQNLEAQQ----SSLAEAEQRIKELEFEIQSQEQDSEivkNSKSELARIPE----------------------LERELE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1398 QVMETKKKLEEDAGVAEAIEEArrraAKDLESLSVRYEERVQACDKLEKGRTRLQQELDD-VTVALDQQRQVVSAlEKKQ 1476
Cdd:pfam05557 208 RLREHNKHLNENIENKLLLKEE----VEDLKRKLEREEGYREELATLELEKEKLEQELKSwEKLAQDTGLNLRSP-EDLS 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1477 KKFDQMLAEEKLISAR-YAEERD--RAEADAREKETKVLSLSRALEEALETREEMERQNKQL----------RAEMDDLV 1543
Cdd:pfam05557 283 RRIEQLQQREITLKEEnSSLTSSarQLEKAQRELEQELAQYLKNIEDLNKKLKRHKALVRRLqrrvllltkeRDGMRAIL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1544 SSKDD----------VGKNVHELERFKRALEQQVQEMRAQMEELEDELQATEDGKLRLEVNMQALKAQherELQNRDDAN 1613
Cdd:pfam05557 363 ESYDKeltpsnyspqLLERIEEAEDMTQDMQAHNEEMEAQLSVAEEELGGYKQQATTLERELQALRQQ---ESLADPSYS 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1614 DDKKKLLSKQVRELEAELD--AERKQRAQALAGRKKLELDLQEAMA-----QLDAANKGRDEAGKQLRKLQAQMKELWRE 1686
Cdd:pfam05557 440 KEEVDSLRRKLETLEAERQrlREQKNELEMELERRCLQGDYDPKKTkvlhlSMNPAAEAYQQRANDLEKLQAEIERLKRR 519
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1033370542 1687 VEEARAAREEIfiqSRESEKKLKNLEAELLQLQEDLAASE 1726
Cdd:pfam05557 520 LKKLEDDLEQV---GSLPETTSTMNFKEVLELRKELESAE 556
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1092-1614 |
3.07e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.60 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1092 DLQEQVAELQQQLEELRQALARKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAEL--QEDMESEKLARAKAEKQRRD 1169
Cdd:PRK01156 187 YLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELssLEDMKNRYESEIKTAESDLS 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1170 LGEELEALKTELEDTLDSTAAQQELRSKRE-QEVTELKKTIEEEVKV-----HEAQVLDMRQRHTSALEELSEQLEQSRR 1243
Cdd:PRK01156 267 MELEKNNYYKELEERHMKIINDPVYKNRNYiNDYFKYKNDIENKKQIlsnidAEINKYHAIIKKLSVLQKDYNDYIKKKS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1244 FKINLEKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGERAKAELVERLVKLQNELDGVSGTLG 1323
Cdd:PRK01156 347 RYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVS 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1324 STESKTIKLAKDLATVE----------------SHLQD--TQELLQEETRQKLNLSSRVRQLEEEKAAMLEQLEEEEAAK 1385
Cdd:PRK01156 427 SLNQRIRALRENLDELSrnmemlngqsvcpvcgTTLGEekSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRK 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1386 A-----------NFSRQMQSLQQQVMETKKKLEEDAGVAEAIEEARRR-AAKDLESLSVRYEERVQAcdklekgrtrlQQ 1453
Cdd:PRK01156 507 EyleseeinksiNEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRyKSLKLEDLDSKRTSWLNA-----------LA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1454 ELDDVTVALDQQRQvvsalEKKQKKFDQMLAEEKLISARYAEERDRAEADAREKETKVLSLSRALEEAletrEEMERQNK 1533
Cdd:PRK01156 576 VISLIDIETNRSRS-----NEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEI----QENKILIE 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1534 QLRAEMDDLvssKDDVGKnvhelerfKRALEQQVQEMRAQMEELEDELQATEDGKLRLEVNMQALKAQHERELQNRDDAN 1613
Cdd:PRK01156 647 KLRGKIDNY---KKQIAE--------IDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELS 715
|
.
gi 1033370542 1614 D 1614
Cdd:PRK01156 716 D 716
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1031-1183 |
3.32e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 51.51 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1031 EERLSEFTSHMAEEEEKVkSLSKLRNkyeavmADMEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQA 1110
Cdd:PRK09039 52 DSALDRLNSQIAELADLL-SLERQGN------QDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQE 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033370542 1111 LARKEAELQAALARVEDEAAQknavlksLRELQAQLAELQEDMESEKLARAKAEKQRRDLGEELE-ALKTELED 1183
Cdd:PRK09039 125 LDSEKQVSARALAQVELLNQQ-------IAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNvALAQRVQE 191
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1060-1291 |
3.36e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.22 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1060 AVMADME---DRLKKEEKGRQELEKLKRKLDgeagDLQEQVAELQQQLEELRQALArkeaelqaalarveDEAAQKNAVL 1136
Cdd:PRK11281 60 LVQQDLEqtlALLDKIDRQKEETEQLKQQLA----QAPAKLRQAQAELEALKDDND--------------EETRETLSTL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1137 kSLRELQAQLAELQEDMESEKLARAKAEKQrrdlgeeLEALKTELEDtldstaAQQEL--RSKREQEVTELKKTIEEEVK 1214
Cdd:PRK11281 122 -SLRQLESRLAQTLDQLQNAQNDLAEYNSQ-------LVSLQTQPER------AQAALyaNSQRLQQIRNLLKGGKVGGK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1215 VHEAQVLDMRQRHTSALEELSEQLEQSRRFKINLEKTKQA----LEGENAEMQKEVKLLQAAKleSEQRRKKLEGQVQEL 1290
Cdd:PRK11281 188 ALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKqrdyLTARIQRLEHQLQLLQEAI--NSKRLTLSEKTVQEA 265
|
.
gi 1033370542 1291 Q 1291
Cdd:PRK11281 266 Q 266
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1462-1863 |
3.49e-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: 429718 [Multi-domain] Cd Length: 488 Bit Score: 51.81 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1462 LDQQRQVVSALEKKQKKFDQMLAEEKlisARYAEERDRAEADAREKETKVLSLSRALEEALETREEMERQNKQLRAEMDD 1541
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEK---ERYKRDREQWERQRRELESRVAELKEELRQSREKVEELEEKYKELSRSGEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1542 LVSSKDdvgknvhelerfkrALEQQVQEMRAQMEELEDELQATEDGKLRLEVNMQALKAQHERELQNRDDANDDKKKLLS 1621
Cdd:pfam07888 113 LAEEKD--------------ALLAQRAESEARIRELEEDIKTLTQRVLERETELERMKERVKKAGAQRKEEEAERKQLQA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1622 K--QVRELEAELDAERKQRAQALAGRKKLELDLQEAMAQLdaankgrdeagkQLRKLQAQMKELWRE--VEEARAAREEI 1697
Cdd:pfam07888 179 KlqQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTL------------TQKLTTAHRKEAENEalLEELRSLQERL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1698 FIQSRESEKKLKNLEAELLQLQEDLAASERAKRQAQQERDDLADELANGNSGKSALLDEKRHLEARIGQLEEELDEEQSN 1777
Cdd:pfam07888 247 NASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1778 MELLNDRYRKLSMQVETLTTELGAERSFSQ-KTENARQQLERQNKDLRAKLGEmdssvKSKYKMAIATLESKVAQLEEQL 1856
Cdd:pfam07888 327 LQRLEERLQEERMEREKLEVELGREKDCNRvQLSESRRELQELKASLRVAQKE-----KEQLQAEKQELLEYIRQLEQRL 401
|
....*..
gi 1033370542 1857 EQESRER 1863
Cdd:pfam07888 402 ETVADAK 408
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
999-1264 |
3.67e-06 |
|
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: 435008 [Multi-domain] Cd Length: 329 Bit Score: 51.36 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 999 KVSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEERLSEFTSHMAEEEEKVKSLSKL------RNKYEAVMADMEDRLkKE 1072
Cdd:pfam15905 55 KVKSLELKKKSQKDLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLnaavreKTSLSASVASLEKQL-LE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1073 EKGRQELEKLKRKLDGEagdlQEQVAELQQQLEELRQALarkEAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQE- 1151
Cdd:pfam15905 134 LTRVNELLKAKFSEDGT----QKKMSSLSMELMKLRNKL---EAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEk 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1152 --DMESEKLARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVTELKKTIEEEVKVHEAQVLDMRQR--- 1226
Cdd:pfam15905 207 lvSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKckl 286
|
250 260 270
....*....|....*....|....*....|....*....
gi 1033370542 1227 -HTSALEELSEQLEQSRRFKINLEKTKQALEGENAEMQK 1264
Cdd:pfam15905 287 lESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQK 325
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1566-1824 |
3.70e-06 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 51.95 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1566 QVQEMRAQMEELEDELQATEDGKLRLEVNMQALKAQHERELQNRddanddkkkllsKQVRELEAELDAERKQRAQALAGR 1645
Cdd:COG4372 75 QLDDIRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQER------------EAVRQELAAARQNLAKAQQELARL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1646 KKLELDLQEAMAQLDAAnkgRDEAGKQLRKLQAQMKELWREVEEARAAREEIFIQSRESEKKLKNLEAELLQLQ---EDL 1722
Cdd:COG4372 143 TKQAQDLQTRLKTLAEQ---RRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLATRANAAQartEEL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1723 AASERAKRQAQQE---RDDLADELANGNSGKSALLDEKRHLEARIGQLEEELDEEQSNMELLNDRYRKLSMQveTLTTEL 1799
Cdd:COG4372 220 ARRAAAAQQTAQAiqqRDAQISQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQLEAYYQAYVRLRQQ--AAATQR 297
|
250 260
....*....|....*....|....*.
gi 1033370542 1800 GAERSFS-QKTENARQQLERQNKDLR 1824
Cdd:COG4372 298 GQVLAGAaQRVAQAQAQAQAQAQLLS 323
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1442-1983 |
3.79e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.21 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1442 DKLEKGRTRLQQELDDVTVALDQQRQVVSALEKKQKKFDQM---LAEEKLISARYAEERDRAEADAREKETKVLSLSRAL 1518
Cdd:PRK01156 162 NSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIkkqIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSAL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1519 EEALETREEMERQNKQLRAEMDDLVSSKDDVGKNVHELERFKR-----------------ALEQQVQEMRAQMEELEDEL 1581
Cdd:PRK01156 242 NELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKiindpvyknrnyindyfKYKNDIENKKQILSNIDAEI 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1582 QATEDGKLRLEVnMQALKAQHERELQNRDDANDDKKKL----------------LSKQVRELEAELDAERKQRAQALagr 1645
Cdd:PRK01156 322 NKYHAIIKKLSV-LQKDYNDYIKKKSRYDDLNNQILELegyemdynsylksiesLKKKIEEYSKNIERMSAFISEIL--- 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1646 KKLELDLQEAMAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEARAAREEIFIQS------------------RESEKK 1707
Cdd:PRK01156 398 KIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgttlgeeksnhiiNHYNEK 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1708 LKNLEAELLQLQEDLAASERAKRQAQQERDDLADELANGNSGKSALLDEKRHLEARIGQLEEELDEEQSNMELLNDRYRk 1787
Cdd:PRK01156 478 KSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYK- 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1788 lSMQVETLTTE------LGAERSfSQKTENARQQLERQNK---DLRAKLGEMDSS---VKSKYKMAIATLESKVAQLEEQ 1855
Cdd:PRK01156 557 -SLKLEDLDSKrtswlnALAVIS-LIDIETNRSRSNEIKKqlnDLESRLQEIEIGfpdDKSYIDKSIREIENEANNLNNK 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1856 LEQESRERILSGKLvRRAEKKLKEVILQVDEERRNADQYKDQVEKGHLRLKQLKRQLeeaeeeaSRANASRRRMQRELED 1935
Cdd:PRK01156 635 YNEIQENKILIEKL-RGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKAL-------DDAKANRARLESTIEI 706
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1033370542 1936 VTESAESMNREVTSLRNRLskvERRQRKRTPLSFTTRtVRQVFRLDGV 1983
Cdd:PRK01156 707 LRTRINELSDRINDINETL---ESMKKIKKAIGDLKR-LREAFDKSGV 750
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1039-1181 |
4.58e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.75 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1039 SHMAEEEEKVkslsklrnkyEAVMADMEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALarkEAEL 1118
Cdd:PRK00409 509 KLIGEDKEKL----------NELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEA 575
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1033370542 1119 QAALARVEDEAAQknaVLKSLRELQaqlaelqeDMESEKLARAKAEKQRRDLGEELEALKTEL 1181
Cdd:PRK00409 576 QQAIKEAKKEADE---IIKELRQLQ--------KGGYASVKAHELIEARKRLNKANEKKEKKK 627
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
903-1150 |
4.66e-06 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 51.56 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 903 ELENKYQQLSEEKTILAEQLQAETELFAEAEEMRARLAARKQELEDIlHELESRVEEEEERCQQLQgdkKKMQQHVQDLE 982
Cdd:COG4372 75 QLDDIRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAV-RQELAAARQNLAKAQQEL---ARLTKQAQDLQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 983 EQLEEEEAARQKLQLEKVSTEAKLKKMEEDLLVLEDQNSKLHKERKlmeerlseftshMAEEEEKVkslskLRNKYEAVM 1062
Cdd:COG4372 151 TRLKTLAEQRRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLRSA------------QIEQEAQN-----LATRANAAQ 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1063 AdMEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAelqqQLEELRQALARKEAELQAALARVEDEAAQKNAVLKSLREL 1142
Cdd:COG4372 214 A-RTEELARRAAAAQQTAQAIQQRDAQISQKAQQIA----ARAEQIRERERQLQRLETAQARLEQEVAQLEAYYQAYVRL 288
|
....*...
gi 1033370542 1143 QAQLAELQ 1150
Cdd:COG4372 289 RQQAAATQ 296
|
|
| COG1579 |
COG1579 |
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ... |
993-1168 |
5.20e-06 |
|
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function prediction only];
Pssm-ID: 224495 [Multi-domain] Cd Length: 239 Bit Score: 49.67 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 993 QKLQLEKVSTEAK-------LKKMEEDLLVLEDQNSKLHKERKLMEERLSEFTSHMAEEEEKvksLSKLRNKYEAVMAdm 1065
Cdd:COG1579 13 QKLDLEKDRLEPRikeirkaLKKAKAELEALNKALEALEIELEDLENQVSQLESEIQEIRER---IKRAEEKLSAVKD-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1066 EDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQAALARVEDEAAQKNavlKSLRELQAQ 1145
Cdd:COG1579 88 ERELRALNIEIQIAKERINSLEDELAELMEEIEKLEKEIEDLKERLERLEKNLAEAEARLEEEVAEIR---EEGQELSSK 164
|
170 180
....*....|....*....|...
gi 1033370542 1146 LAELQEDMESEKLarAKAEKQRR 1168
Cdd:COG1579 165 REELKEKLDPELL--SEYERIRK 185
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
874-1652 |
5.58e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 51.76 E-value: 5.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 874 TRQDEVMQAKAVELQKVQEKHTKTQMDLKELENKYQQLSEEKTILAEQ----LQAETELFAEAEEMRARLAARKQELEDI 949
Cdd:pfam12128 283 ETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQhgafLDADIETAAADQEQLPSWQSELENLEER 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 950 LHELESRVEEEEERCQQLQgdKKKMQQHVQDLEEQLEEEEAARQKLQLEKVSTEAKLKKMEEDL-LVLEDQNSKLHKERK 1028
Cdd:pfam12128 363 LKALTGKHQDVTAKYNRRR--SKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELrEQLEAGKLEFNEEEY 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1029 LMEERLSE----FTSHMAEEEEK------VKSLSKLRNKYEAVMADMEDRLKKEEKGRQELEKLKRKLdgeaGDLQEQVA 1098
Cdd:pfam12128 441 RLKSRLGElklrLNQATATPELLlqlenfDERIERAREEQEAANAEVERLQSELRQARKRRDQASEAL----RQASRRLE 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1099 ELQQQLEELRQALA----------RKEAEL-QAALARVED-------------------------------EAAQKNAVL 1136
Cdd:pfam12128 517 ERQSALDELELQLFpqagtllhflRKEAPDwEQSIGKVISpellhrtdldpevwdgsvggelnlygvkldlKRIDVPEWA 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1137 KSLRELQAQLAELQEDMESEK-----------LARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVTEL 1205
Cdd:pfam12128 597 ASEEELRERLDKAEEALQSARekqaaaeeqlvQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAER 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1206 KKTIEEEVKVHEAQVLDMRQRHTSALEELSEQLEQSRrfkinlektkqalegenaeMQKevkllQAAKLESEQRRKKLEG 1285
Cdd:pfam12128 677 KDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREAR-------------------TEK-----QAYWQVVEGALDAQLA 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1286 QVQELQLRAGEGerAKAELVERLVKLQNELDGvsgtLGSTESKTIKLAKDLATVESHLQDTQELLQEETRQKLNLSSRVR 1365
Cdd:pfam12128 733 LLKAAIAARRSG--AKAELKALETWYKRDLAS----LGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWL 806
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1366 QLEEEKAAmleqleeeeaAKANFSRQMQSLQQQVmetkKKLEEDAGVAEAIEEARRRAAKDL-----ESLS-VRYEERVQ 1439
Cdd:pfam12128 807 QRRPRLAT----------QLSNIERAISELQQQL----ARLIADTKLRRAKLEMERKASEKQqvrlsENLRgLRCEMSKL 872
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1440 ACDKLEKGRTRLQQELDDVTVALDQQRQV----VSALEKKQKKFDQMLAeeKLISARYAEERDRAEADAREKETKVLSLS 1515
Cdd:pfam12128 873 ATLKEDANSEQAQGSIGERLAQLEDLKLKrdylSESVKKYVEHFKNVIA--DHSGSGLAETWESLREEDHYQNDKGIRLL 950
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1516 RALEEALETREEMERQNKQLRAEMDDLVSSKD-DVGKNVHELERFKRALEQQVQEMRAQMEELEDeLQATEDGKLRLEVN 1594
Cdd:pfam12128 951 DYRKLVPYLEQWFDVRVPQSIMVLREQVSILGvDLTEFYDVLADFDRRIASFSRELQREVGEEAF-FEGVSESAVRIRSK 1029
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 1033370542 1595 MQALkaQHERELQNRDDAnddKKKLLSKQVRELEAELDAERKQRAQALAGRKKLELDL 1652
Cdd:pfam12128 1030 VSEL--EYWPELRVFVKA---FRLWKSDGFGELPDEEYTQAMRRASDILPSAALSGGL 1082
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1006-1408 |
8.67e-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: 429718 [Multi-domain] Cd Length: 488 Bit Score: 50.66 E-value: 8.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1006 LKKMEEDLLVLEDQNSKLHKERKLMEERLSEFTSHMAEEEEkvkSLSKLRNKYEavmaDMEDRLKKEEKGRQELEKLKRK 1085
Cdd:pfam07888 47 LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKE---ELRQSREKVE----ELEEKYKELSRSGEELAEEKDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1086 LDGEAGDLQEQVAELQQQLEELRQALARKEAELQAALARVEDEAAQKnavlkslRELQAQLAELQEDMESeklarakAEK 1165
Cdd:pfam07888 120 LLAQRAESEARIRELEEDIKTLTQRVLERETELERMKERVKKAGAQR-------KEEEAERKQLQAKLQQ-------TEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1166 QRRDLGEELEALKTELEdtldstaaqqelrsKREQEVTELKKTIEEevkvhEAQVLDMRQRHTSALEELSEQLEQSRRFK 1245
Cdd:pfam07888 186 ELRSLSKEFQELRNSLA--------------QRDTQVLQLQDTITT-----LTQKLTTAHRKEAENEALLEELRSLQERL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1246 INLEKTKQALEGENAEMQKEVKLLQA----AKLESEQRRKKL--------EGQVQELQLRAGEGERAKAElVERLVKLQN 1313
Cdd:pfam07888 247 NASERKVEGLGEELSSMAAQRDRTQAelhqARLQAAQLTLQLadaslalrEGRARWAQERETLQQSAEAD-KDRIEKLSA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1314 ELDGVSGTLGSTESKTIKLAKDLAtveshlqdtqellQEETRQKLNLSSRVRQLEEEKAAMLEQLEEEEaakanfsrQMQ 1393
Cdd:pfam07888 326 ELQRLEERLQEERMEREKLEVELG-------------REKDCNRVQLSESRRELQELKASLRVAQKEKE--------QLQ 384
|
410
....*....|....*
gi 1033370542 1394 SLQQQVMETKKKLEE 1408
Cdd:pfam07888 385 AEKQELLEYIRQLEQ 399
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ... |
881-1690 |
9.08e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 225638 [Multi-domain] Cd Length: 1480 Bit Score: 51.04 E-value: 9.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 881 QAKAVELQKVQEKHTKTQmdlKELENKYQQLSEEKTILAEQLQAEtELFAEAEEMRARLAARKQELEDILHELESRVEEE 960
Cdd:COG3096 306 QYRHVDMSRELAELNGAE---GDLEADYQAASDHLNLVQTALRQQ-EKIERYQADLEELTIRLEEQNEVVEEANERQEEN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 961 EERCQQLQGDKKKMQQHVQDLEEQLEeeeaARQKLQLEKVSTEAKLKKMEEdLLVLEDQNSklhkerKLMEERLSEFTSH 1040
Cdd:COG3096 382 EARAEAAELEVDELKSQLADYQQALD----VQQTRAIQYQQAIAALERAKE-LCHLPDLTA------DSAEEWLETFQAK 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1041 MAEEEEKVKSLsklrnkyeavmadmEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAeLQQQLEELRQALARKEAELQA 1120
Cdd:COG3096 451 EEEATEKLLSL--------------EQKMSMAQAAHSQFEQAYQLVVAIAGELARSEA-WDVARELLREGPDQRHLAEQV 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1121 ALARVEdeaaqknavlksLRELQAQLAELQedmESEKLARAKAEKQRRDL-GEELEALKTELEDTLDSTAAQQ----ELR 1195
Cdd:COG3096 516 QPLRMR------------LSELEQRLRQQQ---SAERLLADFCKRQGKNLdAEELEALHQELEALIESLSDSVsnarEQR 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1196 SKREQEVTELKKTIEEEVKVHEAQVldmrqRHTSALEELSEQLEQSrrfkinLEKTKQALEGENAEMQKEvKLLQAAKLE 1275
Cdd:COG3096 581 MALRQEQEQLQSRIQSLMQRAPVWL-----AAQNALEQLSEQSGEE------FTDSQDVTEYMQQLLERE-REATVERDE 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1276 SEQRRKKLEGQVQELQLRAGEGERAKAELVERL--VKLQNELDGV--------SGTLGSteSKTIKLAKDLATVESHLQD 1345
Cdd:COG3096 649 LGARKNALDEEIERLSQPGGSEDQRLNALAERFggVLLSEIYDDVtiedapyfSALYGP--SRHAIVVPDLSQVKEHLEG 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1346 TQE-----LLQEETRQKLNLSSRVRQlEEEKAAMLEQLEEEEAA----------KANFSRQMQSLQQQ---VMETKKKLE 1407
Cdd:COG3096 727 LTDcpedlYLIEGDPQSFDDSVFSVD-ELEKAVVVKIADRQWRYsrfpeiplfgRAAREQRLESLHAErdvLSERHATLS 805
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1408 EDAGVAEAIEEARRRAAKdlESLSVRYE-ERVQACDKLEKGRTRLQQELDD-------VTVALDQQRQVVSALEKKQKKF 1479
Cdd:COG3096 806 FDVQKTQRLHQAFSRFIG--SHLAVAFEaDPEAEIRQLNSRRNELERALSNhendnqqQRIQFDQAKEGVTALNRLIPQL 883
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1480 DqMLAEEKLIsARYAEER---DRAEADAREKETKVLSLSR----------------ALEEALETREEMERQNKQLRAEMD 1540
Cdd:COG3096 884 N-LLADESLA-DRVEEIRerlDEAQEAARFIQQHGNTLSKlepiasvlqsdpeqfeQLKEDYAQAQQMQRQARQQAFALT 961
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1541 DLVSSK-----DDVGKNVHELERFKRALEQQVQEMRAQMEELEDELQatedgklrlevNMQALKAQHERELQNRDDANDD 1615
Cdd:COG3096 962 EVVQRRahfsySDSAEMLSENSDLNEKLRQRLEQAEAERTRAREQLR-----------QHQAQLSQYNQVLASLKSSYDT 1030
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033370542 1616 KKKLLSKQVRELEaELDAERKQRAQALAGRKKLELDlqeamAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEA 1690
Cdd:COG3096 1031 KKELLNELQQELQ-DIGVRADSGAEERARIRRDELH-----AQLSTNRSRRNQLEKQLTFCEAEMDNLTRKLRKL 1099
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
994-1165 |
9.27e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.55 E-value: 9.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 994 KLQLEKVSTEAKLKKMEedlLVLEdQNSKLHKERKLMEERLSEFTSHMAEEEEKVKslsklrnkyeavmaDMEDRLKKEE 1073
Cdd:PRK12704 41 KRILEEAKKEAEAIKKE---ALLE-AKEEIHKLRNEFEKELRERRNELQKLEKRLL--------------QKEENLDRKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1074 kgrQELEKLKRKLDgeagDLQEQVAELQQQLEELRQALARKEAELQAALARV----EDEAaqKNAVLKSLR-ELQAQLAE 1148
Cdd:PRK12704 103 ---ELLEKREEELE----KKEKELEQKQQELEKKEEELEELIEEQLQELERIsgltAEEA--KEILLEKVEeEARHEAAV 173
|
170
....*....|....*..
gi 1033370542 1149 LQEDMESEklARAKAEK 1165
Cdd:PRK12704 174 LIKEIEEE--AKEEADK 188
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
933-1527 |
1.00e-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: 50.59 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 933 EEMRARLAARKQELEdilheLESRVEEEEERCQQLQGDKKKMQQHVQDLEEQLEEEEAARQKLQlekvsteaklkkmeed 1012
Cdd:pfam10174 140 EEMELRIETQKQTLG-----ARDESIKKLLEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLE---------------- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1013 lLVLEDQNSKLHKERKLMEERLSeftshMAEEEEKVKSLSKLRNKYEAVMADMEDRLKKEEkgrQELEKLKRKLDGEAGD 1092
Cdd:pfam10174 199 -VLLDQKEKENIHLREELHRRNQ-----LQPDPAKTKALQTVIEMKDTKISSLERNIRDLE---DEVQMLKTNGLLHTED 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1093 LQEQVAELQ----------QQLEELRQALARKEAELQAALARVE------DEAAQKNAVLK-SLRE-------LQAQLAE 1148
Cdd:pfam10174 270 REEEIKQMEvykshskfmkNKIDQLKQELSKKESELLALQTKLEtltnqnSDCKQHIEVLKeSLTAkeqraaiLQTEVDA 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1149 LQEDMESEKLARAKAEKQRRDLGEELEALKTELEDTLDstaaqqeLRSKREQEVTELKKTIE---EEVKVHEAQVLDMRQ 1225
Cdd:pfam10174 350 LRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKD-------MLDVKERKINVLQKKIEnlqEQLRDKDKQLAGLKE 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1226 RHTS----------ALEELSEQLEQSRRFKINLEKTKQALEGENAEmqkevkllqaaklESEQRRKK---LEGQVQELQL 1292
Cdd:pfam10174 423 RVKSlqtdssntdtALTTLEEALSEKERIIERLKEQREREDRERLE-------------ELESLKKEnkdLKEKVSALQP 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1293 RAGEGERAKAELVERLVKLQNELDGVSGTLGSTESKTIKLAKDLATVESHLQDTQElLQEETRQKLNLSSRVRQLEEEKA 1372
Cdd:pfam10174 490 ELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHN-AEEAVRTNPEINDRIRLLEQEVA 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1373 amlEQLEEEEAAKANFSRQMQSLQQQVMEtkkKLEEDAGVAEaIEEARRRAAKDLESL-----SVRYEERVQACDKLEKG 1447
Cdd:pfam10174 569 ---RYKEESGKAQAEVERLLGILREVENE---KNDKDKKIAE-LESLTLRQMKEQNKKvanikHGQQEMKKKGAQLLEEA 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1448 RTR--------LQQELDDVTVALDQQRQVVSALEKKQKKFDQMLAEEKLISARYAEERdraeadareketkvlslSRALE 1519
Cdd:pfam10174 642 RRRednladnsQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAER-----------------RKQLE 704
|
....*...
gi 1033370542 1520 EALETREE 1527
Cdd:pfam10174 705 EILEMKQE 712
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
910-1284 |
1.05e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 429718 [Multi-domain] Cd Length: 488 Bit Score: 50.27 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 910 QLSEEKTILAEQLQAETELFAEAEEMRARLAARKQELEDILHELESRVEEEEERCQQLQGDKKKMQQHVQDLEEQLEEEE 989
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKVEELEEKYKELSRSGEELA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 990 AARQKLQLEKVSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEERLSEFTSHMAEEEEKVKSLsklrnkyEAVMADMEDRL 1069
Cdd:pfam07888 115 EEKDALLAQRAESEARIRELEEDIKTLTQRVLERETELERMKERVKKAGAQRKEEEAERKQL-------QAKLQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1070 KKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQ--AALARVEDEAAQKNAVLKS-LRELQAQL 1146
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEelRSLQERLNASERKVEGLGEeLSSMAAQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1147 AELQEDMESEKLARAKAEKQRRDLGEELEALKT----ELEDTLDSTAAQQELRSKREQEVTELKKTIEEEVKVHEAQVLD 1222
Cdd:pfam07888 268 DRTQAELHQARLQAAQLTLQLADASLALREGRArwaqERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVE 347
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1033370542 1223 MRQRHTSALEELSEQLEQSRRFKINLEKTkqalegenaemQKEVKLLQAAKLESEQRRKKLE 1284
Cdd:pfam07888 348 LGREKDCNRVQLSESRRELQELKASLRVA-----------QKEKEQLQAEKQELLEYIRQLE 398
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1175-1542 |
1.31e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 429718 [Multi-domain] Cd Length: 488 Bit Score: 49.89 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1175 EALKTELEDTLDSTAAQQELRSKREQEVTELKKTIEEEVKVHEAQVLDMRQRhtsaLEELSEQLEQSRRFKINLEKTKQA 1254
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESR----VAELKEELRQSREKVEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1255 LEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGERAKAELVERLVKLQNELDGVSGTLGSTESKTIKLAK 1334
Cdd:pfam07888 106 LSRSGEELAEEKDALLAQRAESEARIRELEEDIKTLTQRVLERETELERMKERVKKAGAQRKEEEAERKQLQAKLQQTEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1335 DLATVESHLQDTQELLQEETRQKLNLSSRVRQLEEEKAAMLEQLEEEEAAKAnfsrQMQSLQQQVMETKKKLEEDAGVAE 1414
Cdd:pfam07888 186 ELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE----ELRSLQERLNASERKVEGLGEELS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1415 AIEEARRRAAKDLESLSVRYEER----VQACDKLEKGRTRLQQELDDVTVALDQQRQVVSALEKKQKKFDQMLAEEKLis 1490
Cdd:pfam07888 262 SMAAQRDRTQAELHQARLQAAQLtlqlADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERM-- 339
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1033370542 1491 aryaeERDRAEAD-AREKETKVLSLSRALEEALETREEM---ERQNKQLRAEMDDL 1542
Cdd:pfam07888 340 -----EREKLEVElGREKDCNRVQLSESRRELQELKASLrvaQKEKEQLQAEKQEL 390
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteristic of the AAA ... |
1116-1291 |
1.63e-05 |
|
AAA domain; This family of domains contain a P-loop motif that is characteristic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 433006 [Multi-domain] Cd Length: 712 Bit Score: 50.06 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1116 AELQAALARVEDEA--AQKNA-------VLKSLRELQAQLAELQED---MESEKLARAKAEKQRRDLGEELEALKTELED 1183
Cdd:pfam13166 267 AERKAALEAHFDDEftEFQRRlqkliekYESAISSLLAQLPAVSDLaslLSAFELDVEDLKAEAEVLNSQLDGLRQALEA 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1184 TLDSTAAQQELRSKRE--QEVTELKKTIEEEVKVHEAQVLDmrqrHTSALEELSEQLEQSR--RFKINLEKTKQALEGEN 1259
Cdd:pfam13166 347 KRKEPFKSIELDSVDAkiESIKDLVAAINELIAKHNEITDN----LEEEKNKAKKKLWLFLveEFKAEIDEYKDAYAGLE 422
|
170 180 190
....*....|....*....|....*....|..
gi 1033370542 1260 aemqKEVKLLQAAKLESEQRRKKLEGQVQELQ 1291
Cdd:pfam13166 423 ----KAINSLTKEIKNATAEIKKLRAEIRELE 450
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
683-707 |
1.79e-05 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 46.95 E-value: 1.79e-05
10 20
....*....|....*....|....*
gi 1033370542 683 YKESLSKLMSTLRNTNPNFVRCIIP 707
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1016-1836 |
2.05e-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: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1016 LEDQNSKLHKERKLmeerLSEFTSHMAEEEEKVKSLSKLrNKYEAVMADMEDRLkkeEKGRQELEKLKRKLDGEAGDLQE 1095
Cdd:TIGR01612 885 LNDYEKKFNDSKSL----INEINKSIEEEYQNINTLKKV-DEYIKICENTKESI---EKFHNKQNILKEILNKNIDTIKE 956
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1096 QVAELQQQLEELRQALARKEAELQAAL--ARVEDEAAQKNAVLKSLRELQAQLAELQEDMESEKLAraKAEKQRRDLGEE 1173
Cdd:TIGR01612 957 SNLIEKSYKDKFDNTLIDKINELDKAFkdASLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQFD--EKEKATNDIEQK 1034
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1174 LEALKTELEDTldstaaQQELRSKREQEVTELKKTIEEEVKVHEAQVLDMRQRHTSALEELSEQL----------EQSRR 1243
Cdd:TIGR01612 1035 IEDANKNIPNI------EIAIHTSIYNIIDEIEKEIGKNIELLNKEILEEAEINITNFNEIKEKLkhynfddfgkEENIK 1108
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1244 FKINLEKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAG---------EGERAKAELVERLVKLQNE 1314
Cdd:TIGR01612 1109 YADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADkaisnddpeEIEKKIENIVTKIDKKKNI 1188
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1315 LDGVSGTLgsteSKTIKLAKDLATVE-------SHLQDTQELLQEetrqklnlssrvrQLEEEKaamleqleeeeAAKAN 1387
Cdd:TIGR01612 1189 YDEIKKLL----NEIAEIEKDKTSLEevkginlSYGKNLGKLFLE-------------KIDEEK-----------KKSEH 1240
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1388 FSRQMQSLQQQVMETKKKLEEdagvAEAIEEARRRAAKDLESLSVRYeervqacDKLEKGRTRLQQelddvtvaldqQRQ 1467
Cdd:TIGR01612 1241 MIKAMEAYIEDLDEIKEKSPE----IENEMGIEMDIKAEMETFNISH-------DDDKDHHIISKK-----------HDE 1298
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1468 VVSALEKKQKKFDQMLAEEKLIS------ARYAEERDRAEADAREKETKVLSL---------SRALEEALETREEMERQN 1532
Cdd:TIGR01612 1299 NISDIREKSLKIIEDFSEESDINdikkelQKNLLDAQKHNSDINLYLNEIANIynilklnkiKKIIDEVKEYTKEIEENN 1378
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1533 KQLRAEMDDlvsskddvgknvhelerfKRALEQQVQEmRAQMEELEDELQATEDGKLRLEV--NMQALKAQHERELQNRD 1610
Cdd:TIGR01612 1379 KNIKDELDK------------------SEKLIKKIKD-DINLEECKSKIESTLDDKDIDECikKIKELKNHILSEESNID 1439
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1611 ------DANDDKKKLLSKQVREleAELDAERKQRAQALAGRKKLELDLQEAMAQLDAANKGRDEAGKQLRKLQAQmKELW 1684
Cdd:TIGR01612 1440 tyfknaDENNENVLLLFKNIEM--ADNKSQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKN-KELF 1516
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1685 RE-------------------------------VEEARAAREEIFIQSRESEKKLKNLEAELLQLQEDLAASERAKRQA- 1732
Cdd:TIGR01612 1517 EQykkdvtellnkysalaiknkfaktkkdseiiIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAi 1596
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1733 --QQERDDLADEL---ANGNSGKSALLDEKRHLEARIGQLEeeldeeqsnmelLNDRYRKLSMQVETLTTelgaERSFSQ 1807
Cdd:TIGR01612 1597 diQLSLENFENKFlkiSDIKKKINDCLKETESIEKKISSFS------------IDSQDTELKENGDNLNS----LQEFLE 1660
|
890 900
....*....|....*....|....*....
gi 1033370542 1808 KTENARQQLERQNKDlrakLGEMDSSVKS 1836
Cdd:TIGR01612 1661 SLKDQKKNIEDKKKE----LDELDSEIEK 1685
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1026-1242 |
2.12e-05 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 49.93 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1026 ERKLMEERLseftsHMAEEEEKVKSLS-KLRNKYEAVMADMEDR---LKKEEKGRQEL-EKLKRKLDGEAGDLqEQVAEL 1100
Cdd:PLN03188 1046 EKKLEQERL-----RWTEAESKWISLAeELRTELDASRALAEKQkheLDTEKRCAEELkEAMQMAMEGHARML-EQYADL 1119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1101 QqqlEELRQALARKEaELQAALARVEDEAAQ---KNAVLKSLRELQAQLAELqedmeseklaRAKAEKQRRDLGEELEAL 1177
Cdd:PLN03188 1120 E---EKHIQLLARHR-RIQEGIDDVKKAAARagvRGAESKFINALAAEISAL----------KVEREKERRYLRDENKSL 1185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033370542 1178 KTELEDTLDSTAAQQEL--RSKREQE--VTELKKTIEEEVKVHEA--QVLDMRQRHTSALEELSEQLEQSR 1242
Cdd:PLN03188 1186 QAQLRDTAEAVQAAGELlvRLKEAEEalTVAQKRAMDAEQEAAEAykQIDKLKRKHENEISTLNQLVAESR 1256
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1612-1879 |
2.15e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 48.95 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1612 ANDDKKKLLSKQVRELEAELDAERKQRAQALAGRKKLELDLQEAMAQLDAANKGRDEAGKQLRKLQAQMKELwrEVEEaR 1691
Cdd:COG4942 35 ADDKQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARLNAL--EVQE-R 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1692 AAREEIFIQSRESEKKLKNLEAELLQLQEDLAASERAK---RQAQQERDDLADELANgnsGKSALLDEKRHLEARigqle 1768
Cdd:COG4942 112 EQRRRLAEQLAALQRSGRNPPPALLVSPEDAQRSVRLAiyyGALNPARAERIDALKA---TLKQLAAVRAEIAAE----- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1769 eeldeeqsnmellndryrklSMQVETLTTELGAERSFSQKTENARQQLERQ-NKDLRAklgemDSSVKSKYKMAIATLES 1847
Cdd:COG4942 184 --------------------QAELTTLLSEQRAQQAKLAQLLEERKKTLAQlNSELSA-----DQKKLEELRANESRLKN 238
|
250 260 270
....*....|....*....|....*....|..
gi 1033370542 1848 KVAQLEEQLEQESRERILSGKLVRRAEKKLKE 1879
Cdd:COG4942 239 EIASAEAAAAKAREAAAAAEAAAARARAAEAK 270
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1092-1371 |
2.30e-05 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 49.33 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1092 DLQEQVAELQQQLEELRQALARKEAELQAALARV-------EDEAAQKNAVLKSLRE----LQAQLAELQEDME------ 1154
Cdd:pfam03528 5 DLQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFkelylakEEDLKRQNAVLQEAQVeldaLQNQLALARAEMEnikava 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1155 --SEKLARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRSKREQ-EVTELKKTIEEEVKvheaqvlDMRQRHTSAL 1231
Cdd:pfam03528 85 tvSENTKQEAIDEVKSQWQEEVASLQAIMKETVREYEVQFHRRLEQERaQWNQYRESAEREIA-------DLRRRLSEGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1232 EE---------LSEQLEQSRRFKINLEKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQ-ELQLRAGEGERAK 1301
Cdd:pfam03528 158 EEenledemkkAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEASKMKELNHYLEAEKSCRtDLEMYVAVLNTQK 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1033370542 1302 AELVERLVKLQNELDGVSGTLGSTESKTIKLAKDLATVESHLQDTQELL-QEETRQKLNLSS-RVRQLEEEK 1371
Cdd:pfam03528 238 SVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLmRDMQRMESVLTSeQLRQVEEIK 309
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1093-1864 |
2.44e-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: 49.44 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1093 LQEQVAELQQQLEELRQALARKEAELQAALARVED---EAAQKNAVLKslRELQAQLAELQEdmeseklarakaekQRRD 1169
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLGSSMNSIKTfwsPELKKERALR--KEEAARISVLKE--------------QYRV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1170 LGEELEALKTELEDTLDSTAAQQELRSKREQEVTELKKTIEEEVKVHEAQVLDMRQRHtSALEELSEQLEQSRR----FK 1245
Cdd:pfam10174 65 TQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQ-SEHERQAKELFLLRKtleeME 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1246 INLEKTKQALEGENAEMQKEVKLLQAAKLEseqrrKKLEGQVQELQLRAGEGERAKAELVERLVKLQNELDGVSGTLGST 1325
Cdd:pfam10174 144 LRIETQKQTLGARDESIKKLLEMLQSKGLP-----KKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1326 ESKTIKLAKDLATveshlqdtQELLQEETRQKLNLSSRVRQLEEEKAAMLEQLEEEEAAKANFSRQMQSLQQQVMETKKK 1405
Cdd:pfam10174 219 NQLQPDPAKTKAL--------QTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1406 LEEDAGVAEAIEEARRRAAKDLESLSVRYEERVQACDKLEKGRTR-------LQQELDDVTVALDQQRQVvsaLEKKQKK 1478
Cdd:pfam10174 291 IDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAkeqraaiLQTEVDALRLRLEEKESF---LNKKTKQ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1479 FDQMLAEEKLISARYAEERDRAEAdareKETKVLSLSRALEEALETREEMERQNKQLR-----------------AEMDD 1541
Cdd:pfam10174 368 LQDLTEEKSTLAGEIRDLKDMLDV----KERKINVLQKKIENLQEQLRDKDKQLAGLKervkslqtdssntdtalTTLEE 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1542 LVSSKDDVGKNV-HELERFKRALEQQVQEMRAQMEELEDELQATEDGKLRLEVNMQALKaQHERELQNRDDANDDKKKLL 1620
Cdd:pfam10174 444 ALSEKERIIERLkEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLK-EHASSLASSGLKKDSKLKSL 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1621 S----KQVRELEAELDAERKQRAQALAGRKKLELDLQEAMAQLDAANKgRDEAGKQlrklQAqmkelwrEVEEARAAREE 1696
Cdd:pfam10174 523 EiaveQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVARY-KEESGKA----QA-------EVERLLGILRE 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1697 IFIQSRESEKKLKNLEA-ELLQLQEDLAASERAKRQAQQERDDLADELANGNSGKSALLDEKRHLEarigQLEEELDEEQ 1775
Cdd:pfam10174 591 VENEKNDKDKKIAELESlTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQ----LEELMGALEK 666
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1776 SNMELLNDRYRKLSMQV-----ETLTTELGAERsfsqktenaRQQLER-------------QNKDLRAKLGEMDSSVKSK 1837
Cdd:pfam10174 667 TRQELDATKARLSSTQQslaekDGHLTNLRAER---------RKQLEEilemkqeallaaiSEKDANIALLELSSSKKKK 737
|
810 820
....*....|....*....|....*..
gi 1033370542 1838 YKMAIATLESKVAQLEEQLEQESRERI 1864
Cdd:pfam10174 738 TQEEVMALKREKDRLVHQLKQQTQNRM 764
|
|
| GumC |
COG3206 |
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane ... |
997-1291 |
2.53e-05 |
|
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225747 [Multi-domain] Cd Length: 458 Bit Score: 48.98 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 997 LEKVSTEAKLKKM-EEDLLVLEDQNSKLHKERKLMEERLSEFTSHMAEEEEKVKSLSKLRNKYEAVMADMEDRlkkeeKG 1075
Cdd:COG3206 95 LEKVIDKLKLDDDpEFVGKPLIASFLRLLKDLIGPDPTIFEISYRLDDLLESLKVLRAGRSRVIELSYTSNDP-----KL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1076 RQELEK------LKRKLDGEAGDLQEQVAELQQQLEELRQALarKEAELQAALARVE----DEAAQKNAVLKSLRELQAQ 1145
Cdd:COG3206 170 AAKLANalaqayLADQLEAQLEAFRRASDSLDERLEELRARL--QEAEAQVEDFRAQhgltDAARGQLLSEQQLSALNTQ 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1146 LAELQEdMESEKLARAKAEKQRRDLGEELEALKTELEDtldstAAQQELRSKREQEVTELKKTIEEEVKVHEAQVLDMRQ 1225
Cdd:COG3206 248 LQSARA-RLAQAEARLASLLQLLPLGREAAALREVLES-----PTIQDLRQQYAQVRQQIADLSTELGAKHPQLVALEAQ 321
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1033370542 1226 rhtsaLEELSEQLEQ-SRRFKINLEKTKQALEGENAEMQKEVK-----LLQAAKLESEQRRkkLEGQVQELQ 1291
Cdd:COG3206 322 -----LAELRQQIAAeLRQILASLPNELALLEQQEAALEKELAqlkgrLSKLPKLQVQLRE--LEREAEAAR 386
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
1015-1358 |
2.68e-05 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 227608 [Multi-domain] Cd Length: 1213 Bit Score: 49.54 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1015 VLEDQNSKLHKERKLMEERLSEFTSHMAEEEEKVKSLSKLRNKYEAVMADMEDRLKKEEKGRQELEKLKRKLDGEAGDLQ 1094
Cdd:COG5283 26 VLKSSIKDSTQFWKMLEKQQKLTKDGLSASKGKYEGLSEAMEKQKKAYEDLKQEVKEVNRATQASKKAYQEYNAQYTQAE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1095 EQVAELQQQLEELRQALARKEAELQaalarveDEAAQKNAVLKSLRElQAQLAELQEDMESEklARAKAEKQRRDLGEEL 1174
Cdd:COG5283 106 NKLRSLSGQFGVASEQLMLQQKEIQ-------RLQYAISTLNKSMAA-QARLLEQTGNKFGT--ADAKVVGLRESFGRQT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1175 EALKTELEDTLDSTAAQQELRSKREQEVTELKKTIEEEVKVHEAQV----------LDMRQRHTSALEELSEQLEQSR-R 1243
Cdd:COG5283 176 EALNKQLERTKKVADALTYVLDEAQQKLSQALSARLERLQESRTQMsqssgqlgkrLETDKAGAGALGLLGAALAGSFaA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1244 FKINLEKTKQaLEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQEL--QLRAGEGERAKAELVERLVKLqneldGVSGT 1321
Cdd:COG5283 256 IGAAVRRTAQ-MNGELMDKTKQVKGARDNLGKVTSQGEEMSDAIQETaeHIKDSGRELSKAAAIGAAAAM-----GVAAG 329
|
330 340 350
....*....|....*....|....*....|....*..
gi 1033370542 1322 LGSTESKTIKLAKDLATVESHLQDTQELLQEETRQKL 1358
Cdd:COG5283 330 KFPTGQEAKPTLKEMARVAALTATAFNLPADELNDNL 366
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1386-1977 |
2.82e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.45 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1386 ANFSRQMQSLQQQVMETKKKLEEDAGVAEAIEEARRRAAKDLESLSVRYEervqacDKLEKGRTRLQQELDDVTVALDQQ 1465
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLD------DQWKEKRDELNGELSAADAAVAKD 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1466 RQVVSALEKKQKKFDQMLAEeklisaRYAEERDRAEADAREKEtkvlSLSRALEEALETREEMERQNKQLRAEMDDlvSS 1545
Cdd:pfam12128 321 RSELEALEDQHGAFLDADIE------TAAADQEQLPSWQSELE----NLEERLKALTGKHQDVTAKYNRRRSKIKE--QN 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1546 KDDVGKNVHELERFKRALEQQVQEMRAQMEELEDELQATEDGKLRlEVNMQALK-AQHERELQNRDDANDDKKKLLSkQV 1624
Cdd:pfam12128 389 NRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKL-EFNEEEYRlKSRLGELKLRLNQATATPELLL-QL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1625 RELEAELDAERKQRAQALAGRkkleLDLQEAMAQLDAAnkgRDEAGKQLRKLQAQMKELWREVEEARaarEEIFIQSRES 1704
Cdd:pfam12128 467 ENFDERIERAREEQEAANAEV----ERLQSELRQARKR---RDQASEALRQASRRLEERQSALDELE---LQLFPQAGTL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1705 EKKLKNLEAELLQLQEDLAASErakrqaQQERDDLADELaNGNSGKSAL------LDEKR-----------HLEARIGQL 1767
Cdd:pfam12128 537 LHFLRKEAPDWEQSIGKVISPE------LLHRTDLDPEV-WDGSVGGELnlygvkLDLKRidvpewaaseeELRERLDKA 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1768 EEELDEEQSNMELLNDRYRKLSMQVETLTTELGAERSFSQKTENARQQLERQNKDLRAKLGEMDSSVKSKYKMAIATLES 1847
Cdd:pfam12128 610 EEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1848 KVAQLEEQLEQESrERILSGKLVRRAEK--KLKEVILQVDEERRNADQYKDQVEKGH-LRLKQLKRQLEEAEEEASRANA 1924
Cdd:pfam12128 690 QLKQLDKKHQAWL-EEQKEQKREARTEKqaYWQVVEGALDAQLALLKAAIAARRSGAkAELKALETWYKRDLASLGVDPD 768
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1033370542 1925 SRRRMQRELEDVTESAESMNR---EVTSLRNRLSK--VERRQRKRTPLSFTTRTVRQV 1977
Cdd:pfam12128 769 VIAKLKREIRTLERKIERIAVrrqEVLRYFDWYQEtwLQRRPRLATQLSNIERAISEL 826
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
1513-1610 |
3.08e-05 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 431934 [Multi-domain] Cd Length: 151 Bit Score: 46.16 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1513 SLSRALEEALETREEMERQNKQLRAEMDDLVSSKDDVGKNVHELERFKRALEQQVQEMRAQMEELEDELQATEDGKLRLE 1592
Cdd:pfam11559 42 ELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLK 121
|
90
....*....|....*...
gi 1033370542 1593 VNMQALKAQHERELQNRD 1610
Cdd:pfam11559 122 NALQQIKTQFAHEVKKRD 139
|
|
| HlyD |
pfam00529 |
HlyD membrane-fusion protein of T1SS; HlyD is a component of the prototypical alpha-haemolysin ... |
1092-1235 |
3.60e-05 |
|
HlyD membrane-fusion protein of T1SS; HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD and HlyB are inner-membrane proteins and specific components of the transport apparatus of alpha-haemolysin. 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: 48.19 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1092 DLQEQVAELQQQLEELRQALARKEAELQAA----------LARVEDEAAQKNAVLKSLRELQAQLAELQEDMESEKLARA 1161
Cdd:pfam00529 55 DYQAALDSAEAQLAKAQAQVARLQAELDRLqaleselaisRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAP 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033370542 1162 KAEKQRRDLgEELEALKTELEDTLDSTAAQQE-LRSKREQEVTELKKTIEEEVKVHEAQVLDMRQRHTSALEELS 1235
Cdd:pfam00529 135 IGGISRESL-VTAGALVAQAQANLLATVAQLDqIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumor ... |
1006-1237 |
4.58e-05 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumor 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: 434432 Cd Length: 528 Bit Score: 48.30 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1006 LKKMEEDLLVLEDQNSKLHKERKlMEERLSEFTSHMAEEEEKVKSLSKLRNKYEaVMADMEDRLKK------EEKGRQEL 1079
Cdd:pfam15066 307 LQPLEEDMALNEVLQKLKHTNRK-QQMQIQDLQCSNLYLEKKVKELQMKITKQQ-VFVDIINKLKEnveeliEDKYNVIL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1080 EK--LKRKLDgeagDLQEQVAELQQQLEElrqalARKEAE-LQAALARVedeaaQKNAVL---KSLRELQAQLAELQEDM 1153
Cdd:pfam15066 385 EKndINKTLQ----NLQEILANTQKHLQE-----SRKEKEtLQLELKKI-----KVNYVHlqeRYITEMQQKNKSVSQCL 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1154 ESEKLARAKAEKQRRdlgeeLEALKTELEDTldSTAAQQELrsKREQEVTELK-KTIEEEVKVHEAQVLDMRQRHTSALE 1232
Cdd:pfam15066 451 EMDKTLSKKEEEVER-----LQQLKGELEKA--TTSALDLL--KREKETREQEfLSLQEEFQKHEKENLEERQKLKSRLE 521
|
....*
gi 1033370542 1233 ELSEQ 1237
Cdd:pfam15066 522 KLVAQ 526
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1042-1282 |
4.61e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 48.41 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1042 AEEEEKVKS-LSKLRnkYEAVMAdmedRLKKEEKGRQEleKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQA 1120
Cdd:PRK05035 440 AIEQEKKKAeEAKAR--FEARQA----RLEREKAAREA--RHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAG 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1121 ALARVEDEAAQKNAVLKSLRELQAQLAELQEDMESEK-----LARAKAEKQrrdlgeELEALKTELEDTLDSTAAQQELR 1195
Cdd:PRK05035 512 ARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAavaaaIARAKAKKA------AQQAANAEAEEEVDPKKAAVAAA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1196 SKREQEVTELKKTIEEEVKVHEAQVLDMRQRHTSALE-----ELSEQLEQSRRFKINLEKTKQALEGENAEMQKEVKLLQ 1270
Cdd:PRK05035 586 IARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIArakakKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQA 665
|
250
....*....|..
gi 1033370542 1271 AAKLESEQRRKK 1282
Cdd:PRK05035 666 NAEPEEAEDPKK 677
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1076-1242 |
4.98e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 47.65 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1076 RQELEKLKRKLDgeagDLQEQVAELQQQL-------EELRQALARKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAE 1148
Cdd:PRK09039 45 SREISGKDSALD----RLNSQIAELADLLslerqgnQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1149 LQEDMESEKLARAKAEKQRRDLGEELEALKTEL---EDTLDSTaaqqelrskreqevtelkktiEEEVKVHEAQVLDMRQ 1225
Cdd:PRK09039 121 LAQELDSEKQVSARALAQVELLNQQIAALRRQLaalEAALDAS---------------------EKRDRESQAKIADLGR 179
|
170
....*....|....*..
gi 1033370542 1226 RHTSALEELSEQLEQSR 1242
Cdd:PRK09039 180 RLNVALAQRVQELNRYR 196
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1481-1827 |
5.18e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteristic 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: 47.75 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1481 QMLAEEKLISARYAEERDRAEADAREKETKVLSLSRALEEALETREEMERQNKQLRAEMDDLVSSKDDVGKNVHELERFK 1560
Cdd:pfam19220 55 ALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1561 RALEQQVQEMRAQMEELEDELQATEdGKLRLEVNMQALKAQHERELQNRDDANDDKKKLLSKQVRELEAELDAERK---- 1636
Cdd:pfam19220 135 RALEEENKALREEAQAAEKALQRAE-GELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRArlra 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1637 ---QRAQALAGRKKLELDLQEAMAQ-----------LDAANKGRDEAGKQLRKLQAQMKELWREVEEARAAREEIFIQSR 1702
Cdd:pfam19220 214 legQLAAEQAERERAEAQLEEAVEAhraeraslrmkLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERD 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1703 ESEKKLKNLEAELLQLQEDLAASERAkRQAQQERddlADELANGNSGKSALLDEKrhlearigqleeeldeeqsnmellN 1782
Cdd:pfam19220 294 TLERRLAGLEADLERRTQQFQEMQRA-RAELEER---AEMLTKALAAKDAALERA------------------------E 345
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1033370542 1783 DRYRKLSMQVETLTtelgaersfsQKTENARQQLERQNKDLRAKL 1827
Cdd:pfam19220 346 ERIASLSDRIAELT----------KRFEVERAALEQANRRLKEEL 380
|
|
| HOOK |
pfam05622 |
HOOK protein; This family consists of several HOOK1, 2 and 3 proteins from different ... |
1092-1530 |
5.76e-05 |
|
HOOK protein; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organisms. 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 the 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.
Pssm-ID: 428548 [Multi-domain] Cd Length: 526 Bit Score: 48.13 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1092 DLQEQVAELQQQ---LEELRQALARKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQEDMESEKLA----RAKAE 1164
Cdd:pfam05622 11 ELAQRCHELDQQvslLQEEKNSLQAENKKLQERLNQLESFDESGTPTSKKYSLLQKQLEQLQEENFRLETArddyRIKCE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1165 KQRRDLGE------ELEALKTE---LEDTLDSTAAQQELRSKREQEVTELKKTIEE------EVKVHEAQVLDMRQRHTs 1229
Cdd:pfam05622 91 ELEKEVLElqhrneELTSLAEEaqaLKDEIDILRESSDKVSKLEATVETYKKKLEDlgdlrrQVKLLEERNAVYMQNTV- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1230 aleELSEQLEQSRRFKINLEKTKQALEGENAEMQKEVKllQAAKLESEQrrKKLEGQVQELQlraGEGERAKAE---LVE 1306
Cdd:pfam05622 170 ---SLEEELKKANALRGQLELYKRQVQELHGKLSEESK--KADKLEFEY--KKLEEKLEALQ---KEKERLIIErdtLRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1307 -----RLVKLQNELDGVSGTLGSTESKTIKLAKDLATVEshLQDTQELLQEEtrQKLNLSSRVRQLEEEKAAMLEQLEEE 1381
Cdd:pfam05622 240 tneelRCAQLQQDELSQADALGSPSSSVDNLAAEILPAE--IREKLIRLQHE--NKMLRLQQEGSEREKLTELQALLEDA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1382 EAAKANFSRQMQSLQQQVMETKKKLEEdagVAEAIEEARRRAaKDLESLSVRYEERVQACDKLEKGRTRLQQELDDVTVA 1461
Cdd:pfam05622 316 NRRKNELETQNRLANQRILELQQQVEE---LQKALQEQGSKA-EDSSLLKQKLEEHLEKLHEAQEELQKKKEQLEELEPK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1462 LDQQRQVVSALEKK-QKKFDQMLAEE-------------------KLISARYAEERDRaEADAREKETKVLSLSRALEEA 1521
Cdd:pfam05622 392 VDSNLQKIDELQEAlRKKDEDMKAMEerykkyvekaksviktldpKQNPASPPEIQAL-RNQLLEKDKKIEHLERDYEKS 470
|
....*....
gi 1033370542 1522 LETREEMER 1530
Cdd:pfam05622 471 KLQREQEEK 479
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
872-1257 |
5.84e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 428520 [Multi-domain] Cd Length: 660 Bit Score: 48.19 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 872 QVTRQDEVMQAKAVELQKVQEKHTKTQMDLKELENKYQQLSEEKTILAEQLQAETEL----------FAEAEEMRARLaA 941
Cdd:pfam05557 119 QIQRQELELSSTNSELEELQERLDLQKAKAQEAEQLRQNLEAQQSSLAEAEQRIKELefeiqsqeqdSEIVKNSKSEL-A 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 942 RKQELEDILheleSRVEEEEERCQQLQGDKKKMQQHVQDLEEQLEEEEAARQK---LQLEKVSTEAKLKKMEE------- 1011
Cdd:pfam05557 198 RIPELEREL----ERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEGYREElatLELEKEKLEQELKSWEKlaqdtgl 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1012 DLLVLEDQNSK---LHKERKLMEERLSEFTSHMAEEEekvKSLSKLRNKYEAVMADMEDrlkkEEKGRQELEKLKRKldg 1088
Cdd:pfam05557 274 NLRSPEDLSRRieqLQQREITLKEENSSLTSSARQLE---KAQRELEQELAQYLKNIED----LNKKLKRHKALVRR--- 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1089 eagdLQEQVAELQQQLEELRQALARKEAELQAA------LARVEDEAAQKNAVLKSLRELQAQLAELQE----------- 1151
Cdd:pfam05557 344 ----LQRRVLLLTKERDGMRAILESYDKELTPSnyspqlLERIEEAEDMTQDMQAHNEEMEAQLSVAEEelggykqqatt 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1152 -DMESEKLARAKAEKQRRDLGEELEALKTELEDTLdstAAQQELR-SKREQEVTELKKTIEEEVKVHEAQVLDMRQRHTS 1229
Cdd:pfam05557 420 lERELQALRQQESLADPSYSKEEVDSLRRKLETLE---AERQRLReQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAA 496
|
410 420 430
....*....|....*....|....*....|...
gi 1033370542 1230 ALEELS-EQLEQSR----RFKINLEKTKQALEG 1257
Cdd:pfam05557 497 EAYQQRaNDLEKLQaeieRLKRRLKKLEDDLEQ 529
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1564-1703 |
6.04e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 47.27 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1564 EQQVQEMRAQMEELEDELQATEDGKLRLEVNMQALKA-----QHERE-LQNRDDANDDKKKLLSKQVRELEAELDAERKQ 1637
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRAslsaaEAERSrLQALLAELAGAGAAAEGRAGELAQELDSEKQV 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033370542 1638 RAQALAgrkKLEL----------DLQEAMAQLDAANKGRDEAGKQLRKLQAQMK-ELWREVEEARAAREEIFIQSRE 1703
Cdd:PRK09039 132 SARALA---QVELlnqqiaalrrQLAALEAALDASEKRDRESQAKIADLGRRLNvALAQRVQELNRYRSEFFGRLRE 205
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1106-1283 |
6.25e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 6.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1106 ELRQALARKEAELQAALARVEDEAAQKNAVLkslrELQAQLAELQEDMESEKLAR----AKAEKQRRDLGEELEALKTEL 1181
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALL----EAKEEIHKLRNEFEKELRERrnelQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1182 EDTLDSTAAQQELRSKREQEVTELKKTIEEevkvheaqvldMRQRHTSALEELSE-QLEQSRrfKINLEKTKQALEGENA 1260
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQELEKKEEELEE-----------LIEEQLQELERISGlTAEEAK--EILLEKVEEEARHEAA 172
|
170 180
....*....|....*....|...
gi 1033370542 1261 EMQKEVKllQAAKLESEQRRKKL 1283
Cdd:PRK12704 173 VLIKEIE--EEAKEEADKKAKEI 193
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1071-1335 |
8.04e-05 |
|
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: 435008 [Multi-domain] Cd Length: 329 Bit Score: 47.12 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1071 KEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEelrqalaRKEAELQAALarvedeaAQKNAVLKSLRELQAQLAELQ 1150
Cdd:pfam15905 70 KESKDQKELEKEIRALVQERGEQDKRLQALEEELE-------KVEAKLNAAV-------REKTSLSASVASLEKQLLELT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1151 EDME--SEKLARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVTELKKTIEEEVKVHEAQVLDMRQRH- 1227
Cdd:pfam15905 136 RVNEllKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKi 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1228 ---------TSALEELSEQLEQSRRFKINLEKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGE 1298
Cdd:pfam15905 216 eekseteklLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELL 295
|
250 260 270
....*....|....*....|....*....|....*..
gi 1033370542 1299 RAKAELVERLVKlqnELDGVSGTLGSTESKTIKLAKD 1335
Cdd:pfam15905 296 REYEEKEQTLNA---ELEELKEKLTLEEQEHQKLQQK 329
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1346-1964 |
9.57e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.73 E-value: 9.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1346 TQELLQEETRQKLNLSSRVRQLEEEKAAMLEQLEEEEAAKANFSRQMQSLQQQVMETKKKLEEDAGVAEAIEEARRRAAK 1425
Cdd:TIGR00606 204 EHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEK 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1426 DLESLSVRYEERVQACDK----LEKGRTRLQQELDDVTValDQQRQVvSALEKKQKKFDQMLAEEKLISARYAEERDRAE 1501
Cdd:TIGR00606 284 DNSELELKMEKVFQGTDEqlndLYHNHQRTVREKERELV--DCQREL-EKLNKERRLLNQEKTELLVEQGRLQLQADRHQ 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1502 ADAREKETKVLSLSRALE-EALETREEMERQNKQLRAEMDDLVSSKDD-VGKNVHELERFKRALEQQVQEMRAQMEELED 1579
Cdd:TIGR00606 361 EHIRARDSLIQSLATRLElDGFERGPFSERQIKNFHTLVIERQEDEAKtAAQLCADLQSKERLKQEQADEIRDEKKGLGR 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1580 ELQateDGKLRLEVNMQALKAQhERELQNRDDANDDkkkLLSKQVRELEAELDAERKQRAQALAGRKKLELDLQEAMAQL 1659
Cdd:TIGR00606 441 TIE---LKKEILEKKQEELKFV-IKELQQLEGSSDR---ILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADL 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1660 DAANKGRDEAGKQLRKLQAQMKELWREVEEARAAREEIFIQSRESEKKLKNLEAEL---LQLQEDLAASERAKRQAQQER 1736
Cdd:TIGR00606 514 DRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFpnkKQLEDWLHSKSKEINQTRDRL 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1737 DDLADELANGNSGKSALLDEKRHLEARIGQLEEE------LDEEQSNMELLNDRYRKLSMQVETLTTELGAERSFSQKTE 1810
Cdd:TIGR00606 594 AKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvcgSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLT 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1811 NARQQ---LERQNKDLRAKLGEMDSSVKSKYKMA---IATLESKVAQLEEQLEQESRERILSGKLVRRAEKKLKEVILQV 1884
Cdd:TIGR00606 674 DENQSccpVCQRVFQTEAELQEFISDLQSKLRLApdkLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKL 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1885 DEERRNADQYKDQVEKGHLRLKQLKRQLEEAEEEASRANASRRrMQRELEDVTESAESMNREVTSLRNRLSKVERRQRKR 1964
Cdd:TIGR00606 754 QKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMER-FQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQ 832
|
|
| COG1579 |
COG1579 |
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ... |
1022-1238 |
9.81e-05 |
|
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function prediction only];
Pssm-ID: 224495 [Multi-domain] Cd Length: 239 Bit Score: 45.82 E-value: 9.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1022 KLHKERKLMEERLSEFTSHMAEEEEKVKSLSKLRNKYEAVMADMEDRLKKEEkgrqeleklkrkldgeagDLQEQVAELQ 1101
Cdd:COG1579 4 NNLKSLLAIQKLDLEKDRLEPRIKEIRKALKKAKAELEALNKALEALEIELE------------------DLENQVSQLE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1102 QQLEELRQALARKEAELQAAlarvedeaaqknavlKSLRELQAqlaeLQEDMESEKLARAKAEKQRRDLGEELEALKTEL 1181
Cdd:COG1579 66 SEIQEIRERIKRAEEKLSAV---------------KDERELRA----LNIEIQIAKERINSLEDELAELMEEIEKLEKEI 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1033370542 1182 EDTLDSTAAQqelrskrEQEVTELKKTIEEEVKVHEAQVLDMRQRHTSALEELSEQL 1238
Cdd:COG1579 127 EDLKERLERL-------EKNLAEAEARLEEEVAEIREEGQELSSKREELKEKLDPEL 176
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
997-1208 |
1.19e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 47.23 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 997 LEKVSTEAKLKKMEEDLLVLEDQNSKLhkerklmEERLSEFTSHMAEEEEKVKSLSKLRNkyeavmADMEDRLKKEEKGr 1076
Cdd:PRK05771 79 VSVKSLEELIKDVEEELEKIEKEIKEL-------EEEISELENEIKELEQEIERLEPWGN------FDLDLSLLLGFKY- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1077 qeleklkrkLDGEAGDLQEQVAELQQQLEELRQALARKEAELQAALARV-EDEAAQKnaVLKSLRELQAQLAELQEDMES 1155
Cdd:PRK05771 145 ---------VSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYVVVVvLKELSDE--VEEELKKLGFERLELEEEGTP 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1033370542 1156 EKLARAKAE------KQRRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVTELKKT 1208
Cdd:PRK05771 214 SELIREIKEeleeieKERESLLEELKELAKKYLEELLALYEYLEIELERAEALSKFLKT 272
|
|
| HEC1 |
COG5185 |
Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, ... |
1200-1634 |
1.34e-04 |
|
Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227512 [Multi-domain] Cd Length: 622 Bit Score: 46.90 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1200 QEVTELKKTIEEEVKVHEAQVLDMRQRHTSALEELSEQLEQSRRFKINLEKTKQALEGENAEMQKEVKLLQaaklESEQR 1279
Cdd:COG5185 214 QPLKTLDQQDRYELMVEKLLFDYFTESYKSFLKLEDNYEPSEQELKLGFEKFVHIINTDIANLKTQNDNLY----EKIQE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1280 RKKLEGQVQELqlragegERAKAELVERLVKLQNELDGVSGTLGSTESKTIKLAKDLATVESHLQDTQELLQEETRQKLN 1359
Cdd:COG5185 290 AMKISQKIKTL-------REKWRALKSDSNKYENYVNAMKQKSQEWPGKLEKLKSEIELKEEEIKALQSNIDELHKQLRK 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1360 LSSRVRQLEEEKAamleqleeeeaAKANFSRQMQSLQQQVMETKKKLEEDAGVAEAIEEARRRAAKDLESLSVRYEERVQ 1439
Cdd:COG5185 363 QGISTEQFELMNQ-----------EREKLTRELDKINIQSDKLTKSVKSRKLEAQGIFKSLEKTLRQYDSLIQNITRSRS 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1440 ACDKLEKGRTRLQQELDDVTVALDQQRQVVSALEKKQKKFDQMLAEEKLISARYAEERDRAEADAREKETKV----LSLS 1515
Cdd:COG5185 432 QIGHNVNDSSLKINIEQLFPKGSGINESIKKSILELNDEIQERIKTEENKSITLEEDIKNLKHDINELTQILekleLELS 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1516 RALEEALETREEMERQNKQLRAEMDDLvsskddvgknvhelerfKRALEQQVQEMRAQMEELEDELQATEDGKLRLEVNM 1595
Cdd:COG5185 512 EANSKFELSKEENERELVAQRIEIEKL-----------------EKELNDLNLLSKTSILDAEQLVQSTEIKLDELKVDL 574
|
410 420 430
....*....|....*....|....*....|....*....
gi 1033370542 1596 QALKAQHERELQNRDDANDDKKKLLSKQVRELEAELDAE 1634
Cdd:COG5185 575 NRKRYKIHKQVIHVIDITSKFKINIQSSLEDLENELGKV 613
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1013-1296 |
1.34e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 47.10 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1013 LLVLEDQNSKLHKERKLMEERLSEFTSHMAEEEEKVKSLSK----LRNKYEAVMA----------DMEDRLKKEEKGRQE 1078
Cdd:PRK10246 532 LDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQeeqaLTQQWQAVCAslnitlqpqdDIQPWLDAQEEHERQ 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1079 LEKLKRK--LDGEAGDLQEQVAELQQQLEELRQALARK----------EAELQAALARVEDEAA---QKNAVLKSLRELQ 1143
Cdd:PRK10246 612 LRLLSQRheLQGQIAAHNQQIIQYQQQIEQRQQQLLTAlagyaltlpqEDEEASWLATRQQEAQswqQRQNELTALQNRI 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1144 AQLAELQEDMESEKLARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRSKREQEV-----TELKKTIEEEVKVHEA 1218
Cdd:PRK10246 692 QQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAqaqfdTALQASVFDDQQAFLA 771
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1033370542 1219 QVLDMRQRHTsaLEELSEQLEQSRRFKINL-EKTKQALEgENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGE 1296
Cdd:PRK10246 772 ALLDEETLTQ--LEQLKQNLENQRQQAQTLvTQTAQALA-QHQQHRPDGLDLTVTVEQIQQELAQLAQQLRENTTRQGE 847
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1483-1646 |
1.36e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1483 LAEEKLISARYAEERDRAEADAREKETKVLSLSRALEEALETREEMERQNKQLRAEMDD----LVSSKDDVGKNVHELER 1558
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKlekrLLQKEENLDRKLELLEK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1559 FKRALEQQVQEMRAQMEELEdelqatedgklRLEVNMQALKAQHERELQN-----RDDAnddkKKLLSKQVRElEAELDA 1633
Cdd:PRK12704 108 REEELEKKEKELEQKQQELE-----------KKEEELEELIEEQLQELERisgltAEEA----KEILLEKVEE-EARHEA 171
|
170
....*....|....*...
gi 1033370542 1634 -----ERKQRAQALAGRK 1646
Cdd:PRK12704 172 avlikEIEEEAKEEADKK 189
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1081-1370 |
1.50e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 46.77 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1081 KLKRKLDGEAGDLQEQVAELQQQLEELRQALAR-KEAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQEDmesekLA 1159
Cdd:PLN03229 422 KKREAVKTPVRELEGEVEKLKEQILKAKESSSKpSELALNEMIEKLKKEIDLEYTEAVIAMGLQERLENLREE-----FS 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1160 RAKAEKQ--RRDLGEELEALKTELEDTLDSTAAQQELRSK---------------REQEVTELKKTIEEEVKvheaQVLD 1222
Cdd:PLN03229 497 KANSQDQlmHPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKldmlnefsrakalseKKSKAEKLKAEINKKFK----EVMD 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1223 mRQRHTSALEELSEQLEQSRRFKINL--EKTKQALEGENAEMQKEV-KLLQAAKLESEQRRKKlegQVQELQLRAGEGER 1299
Cdd:PLN03229 573 -RPEIKEKMEALKAEVASSGASSGDEldDDLKEKVEKMKKEIELELaGVLKSMGLEVIGVTKK---NKDTAEQTPPPNLQ 648
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1033370542 1300 AKAE-LVERLVKLQNELDGVSGTLGSTESKTIKLAKDLATVESHLQDTQELLQEETRQKLNLSSRVRQLEEE 1370
Cdd:PLN03229 649 EKIEsLNEEINKKIERVIRSSDLKSKIELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEALNSSELKEK 720
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1003-1239 |
1.51e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 46.67 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1003 EAKLKKMEEDLLVLEDQNSKLHKERKLMEErLSEFTShmAEEEEKVKSLSKLRNKYEAVMADMEDRLKKEEKGRqeLEKL 1082
Cdd:pfam09731 218 PETPPKLPEHLDNVEEKVEKAQSLAKLVDQ-YKELVA--SERIVFQQELVSIFPDIIPVLKEDNLLSNDDLNSL--IAHA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1083 KRKLDGEAGDLQEQVAELQQQLEE-LRQALARKEAELQAALARVEDEAAQKNAVLKslRELQAQLAELQEDMESEklara 1161
Cdd:pfam09731 293 HREIDQLSKKLAELKKREEKHIERaLEKQKEELDKLAEELSARLEEVRAADEAQLR--LEFEREREEIRESYEEK----- 365
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1033370542 1162 kaekqrrdLGEELEALKTELEDTLDSTAAQQELRSKREQEvTELKKTIEEEVKVHEAQVLDMrqrhTSALEELSEQLE 1239
Cdd:pfam09731 366 --------LRTELERQAEAHEEHLKDVLVEQEIELQREFL-QDIKEKVEEERAGRLLKLNEL----LANLKGLEKATS 430
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
1089-1692 |
1.84e-04 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 227606 [Multi-domain] Cd Length: 833 Bit Score: 46.56 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1089 EAGDLQEQVAELQQQLEeLRQALARKEAELQAALARVEDEAAQKNAvlkslrelqaqlAELQEDMESEKLArakAEKQRR 1168
Cdd:COG5281 28 EAIDVIKQASRFLAQGV-RRGEEFNSVNESGDRAVRALAAGVGKAA------------ADLRQMADAQALA---ADKAVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1169 DLGEELEALKTELEDTLDSTAAQQELRSkreqevtelkktieeevkvheAQVLDMRQRHTSALEELSEQLEQSRRFKINL 1248
Cdd:COG5281 92 SLISLKEQLRDEYPEPVQFTDIATQLAG---------------------GQWPWLINLQQGGQATLSFGLIGPAARIANV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1249 EKTKQALEGENAE-----MQKEVKLLQAAKLESEQRRKKLEG-------QVQELQLRAGEGERAK------AELVERLVK 1310
Cdd:COG5281 151 LTAAGALVAVGAAgyaaaLGAGAMAWYAGAQETEAFNKVLILtgeyagtTAAQLRAGAAAGITQHqaaevlAQLVAAGVA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1311 LQNELDGVSGT-------LGSTESKTIKLAKDLAtveshlQDTQELLQEETRQKLNLSSRVRQLEE--EKAAMLEQLEEE 1381
Cdd:COG5281 231 TAEQLGDVAQAaarfasaSGESIDKTIKAFSKLT------DDPVNGAKALNRQFHYLTAAQLEQIAalQRAGDTAAAAAA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1382 EAAKANFSRQMQSLQQQVMETKKKLEEDAGVAEA------IEEARRRAAKDLESLSVRYEERVQACDKLEKGrTRLQQEL 1455
Cdd:COG5281 305 AAEAAAAMDDRTARVKENMGTLETAWDALADAAKkmwdavLGIGREDKQAALLAAKLAAEKLARVTAQGALN-ARLKLAQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1456 DDVTVALDQQRQVVSALEKKQkkfDQMLAEEKLISARYAEERDRAEAdareketkvlSLSRALEEALETREEMERQNKQL 1535
Cdd:COG5281 384 DDLTQAELNYAAADQAANQEG---ALNAREDEAEVLSTQEERRDILK----------NLLADAEKRTARQEELNKALAKA 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1536 RAEMDDLVSSKD--DVGKNVHELERFKRALEQQVQEMRAQMEELEDELQATEDGKLR--------------LEVNMQALK 1599
Cdd:COG5281 451 KILQADKAAKAYqeDILQREAQSRGKTAAAERSQEQMTAALKALLAFQQQIADLSGAkekasdqksllwkaEEQYALLKE 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1600 AQHERELQNRDDANDDKKKLLskqvrELEAELDAERKQRAQalagrkKLELDLQEAMAQLDAANKGRDEAGKQLRK-LQA 1678
Cdd:COG5281 531 EAKQRQLQEQKALLEHKKETL-----EYTSQLAELLDQQAD------RFELSAQAAGSQKERGSDLYREALAQNAAaLNK 599
|
650
....*....|....*..
gi 1033370542 1679 QMKEL---WREVEEARA 1692
Cdd:COG5281 600 ALNELaayWSALDLLQG 616
|
|
| COG1579 |
COG1579 |
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ... |
1096-1240 |
1.85e-04 |
|
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function prediction only];
Pssm-ID: 224495 [Multi-domain] Cd Length: 239 Bit Score: 45.05 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1096 QVAELQQQLEELRQALARKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQEDMES--EKLARAKAEKQRRDLGEE 1173
Cdd:COG1579 18 EKDRLEPRIKEIRKALKKAKAELEALNKALEALEIELEDLENQVSQLESEIQEIRERIKRaeEKLSAVKDERELRALNIE 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033370542 1174 LEALKTELEDTLDSTAAQQELRSKREQEVTELKKTIEEEvkvhEAQVLDMRQRHTSALEELSEQLEQ 1240
Cdd:COG1579 98 IQIAKERINSLEDELAELMEEIEKLEKEIEDLKERLERL----EKNLAEAEARLEEEVAEIREEGQE 160
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1172-1894 |
1.93e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.72 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1172 EELEALKTELEDTLDSTAAQQELRSKREQEVTELKKTIEEEvkvhEAQVLDMRQRHTSALEELSEQLEQSRRfkinLEKT 1251
Cdd:PRK10246 191 EQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDE----EKQLLTAQQQQQQSLNWLTRLDELQQE----ASRR 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1252 KQALEGENAEMQKEVKllQAAKLESEQRRKKLEGQVQELQlragegerakaELVERLVKLQNELDGVSGTLGSTesktik 1331
Cdd:PRK10246 263 QQALQQALAAEEKAQP--QLAALSLAQPARQLRPHWERIQ-----------EQSAALAHTRQQIEEVNTRLQST------ 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1332 LAKDLATVESHLQDTQELLQEETRQK--LNLSSRVRQLEEEKAAMLEQLEEEEAAKAnfsrQMQSLQQQVMETKKKLE-- 1407
Cdd:PRK10246 324 MALRARIRHHAAKQSAELQAQQQSLNtwLAEHDRFRQWNNELAGWRAQFSQQTSDRE----QLRQWQQQLTHAEQKLNal 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1408 ---------EDAGVAEAIEEARRRAAKDLESLSVRYEERVQACDKLEKGRTRLQQELDDVTVALDQQRQvvsalekKQKK 1478
Cdd:PRK10246 400 paitltltaDEVAAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQ-------RYKE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1479 FDQMLAEEKLISARYAEERDRAEADAREKETKVLSLSRALE-------EALET------REEMERQNKQLRAEMDDLVSS 1545
Cdd:PRK10246 473 KTQQLADVKTICEQEARIKDLEAQRAQLQAGQPCPLCGSTShpaveayQALEPgvnqsrLDALEKEVKKLGEEGAALRGQ 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1546 KDDVGKNVHELERFKRALEQQVQEMRAQMEELEDELQATEDGKLRLEVNMQAlKAQHERELQNRDDANDDKKKLLS--KQ 1623
Cdd:PRK10246 553 LDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDA-QEEHERQLRLLSQRHELQGQIAAhnQQ 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1624 VRELEAELDAERKQRAQALAGrkkLELDLQEAMAQLDAANKGRDEAGK------QLRKLQAQMKEL------WREVEEAR 1691
Cdd:PRK10246 632 IIQYQQQIEQRQQQLLTALAG---YALTLPQEDEEASWLATRQQEAQSwqqrqnELTALQNRIQQLtplletLPQSDDLP 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1692 AAREEIFIQS-RESEKKLKNLEAEL--LQLQEDLAASERAKRQAQQERDDLADELANGNSGKSALLDEkrhlearigqle 1768
Cdd:PRK10246 709 HSEETVALDNwRQVHEQCLSLHSQLqtLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFLAALLDE------------ 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1769 eeldeeqsnmellnDRYRKLSMQVETLTTELGAERSFSqktENARQQLERQnkdLRAKLGEMDSSVKSKykmaiaTLESK 1848
Cdd:PRK10246 777 --------------ETLTQLEQLKQNLENQRQQAQTLV---TQTAQALAQH---QQHRPDGLDLTVTVE------QIQQE 830
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1033370542 1849 VAQLEEQL-EQESRERILSGKLVRRAE--KKLKEVILQVDEERRNADQY 1894
Cdd:PRK10246 831 LAQLAQQLrENTTRQGEIRQQLKQDADnrQQQQALMQQIAQATQQVEDW 879
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1252-1669 |
2.31e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.20 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1252 KQALEGENAEMQKEVKLLQAAkLESEQRRKKLEGQVQELQLRAGEGERAKAELVERLVKLQNELDGVSGTLGSTEsktik 1331
Cdd:PRK10929 33 EQAKAAKTPAQAEIVEALQSA-LNWLEERKGSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTDA----- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1332 LAKDLATVESHLQDTQELLQEETRQKLNLSSRVRQLEEEKAAMLEQLeeeeaakANFSRQMQSLQQqvmeTKKKLEEDAG 1411
Cdd:PRK10929 107 LEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQL-------NEIERRLQTLGT----PNTPLAQAQL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1412 VAEAIEEARRRAAKD---LESLSVRYEE---RVQAcDKLEKGRTRLQQELDDVTVALDQQRQVV--SALEKKQkkfdqML 1483
Cdd:PRK10929 176 TALQAESAALKALVDeleLAQLSANNRQelaRLRS-ELAKKRSQQLDAYLQALRNQLNSQRQREaeRALESTE-----LL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1484 AEEklisaryaeerdraEADAREKETKVLSLSRALEEALetreemerqNKQLRaEMDDLVSSKDDVGKNVHELERFKRAL 1563
Cdd:PRK10929 250 AEQ--------------SGDLPKSIVAQFKINRELSQAL---------NQQAQ-RMDLIASQQRQAASQTLQVRQALNTL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1564 EQQVQ----------EMRAQMEELED--ELQatedgklRLEVNMQALKAQH-------ERELQNRDDANDDKKKLLSKQV 1624
Cdd:PRK10929 306 REQSQwlgvsnalgeALRAQVARLPEmpKPQ-------QLDTEMAQLRVQRlryedllNKQPQLRQIRQADGQPLTAEQN 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1033370542 1625 RELEAELDAERKQRAQALAGRKKLELDLQE---AMAQLDAANKGRDEA 1669
Cdd:PRK10929 379 RILDAQLRTQRELLNSLLSGGDTLILELTKlkvANSQLEDALKEVNEA 426
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1620-1889 |
2.34e-04 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 45.79 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1620 LSKQVRELEAELDAERKQRAQALAGRKKLELDLQ-------EAMAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEARA 1692
Cdd:COG4372 79 IRPQLRALRTELGTAQGEKRAAETEREAARSELQkarqereAVRQELAAARQNLAKAQQELARLTKQAQDLQTRLKTLAE 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1693 AREEIFIQSRESEKKLKNLEAELLQLQ-EDLAASERAKRQAQQERD---------DLADELANGNSGKSALLDEKRHLEA 1762
Cdd:COG4372 159 QRRQLEAQAQSLQASQKQLQASATQLKsQVLDLKLRSAQIEQEAQNlatranaaqARTEELARRAAAAQQTAQAIQQRDA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1763 RIGQLEEELDEEQSNMELLNDRYRKLSMQVETLTTELG-AERSFSQKTENARQQLERQNKDLRAKLGEMDSSVKSKYKMA 1841
Cdd:COG4372 239 QISQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAqLEAYYQAYVRLRQQAAATQRGQVLAGAAQRVAQAQAQAQAQ 318
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1033370542 1842 IATLESKVAQLEEQLEQESRERILSGKLVRRAEKKLKEVILQVDEERR 1889
Cdd:COG4372 319 AQLLSSANRPAALRLRRSPRRGRRQRPVTRHTTRRRRPATRQSPSGRE 366
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1216-1467 |
2.34e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 223571 [Multi-domain] Cd Length: 557 Bit Score: 46.05 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1216 HEAQVLDMRQRHTSALEELSEQLEQSRRfkiNLEKTKQALEgenaEMQKEVKLLQAAKLESEQRRKKLEGQVQELQ---L 1292
Cdd:COG0497 130 HEHQSLLKPELQRQLLDAFAGLEELAQE---AYQEAYQAWK----QARRELEDLQEKERERAQRADLLQFQLEELEelnL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1293 RAGEGErakaELVERLVKLQNeldgvsgtlgstesktiklAKDLATVeshLQDTQELLQEEtRQKLNLSSRVRQLEEEKA 1372
Cdd:COG0497 203 QPGEDE----ELEEERKRLSN-------------------SEKLAEA---IQNALELLSGE-DDTVSALSLLGRALEALE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1373 AMLEQLEEEEAAKANFSRQMQSLQQQVMETKKKLEE---DAGVAEAIEE-------ARRRAAKDLESLsVRYEERVQA-- 1440
Cdd:COG0497 256 DLSEYDGKLSELAELLEEALYELEEASEELRAYLDElefDPNRLEEVEErlfalksLARKYGVTIEDL-LEYLDKIKEel 334
|
250 260 270
....*....|....*....|....*....|....*.
gi 1033370542 1441 ---------CDKLEKGRTRLQQELDDVTVALDQQRQ 1467
Cdd:COG0497 335 aqldnseesLEALEKEVKKLKAELLEAAEALSAIRK 370
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
900-1151 |
2.45e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 223571 [Multi-domain] Cd Length: 557 Bit Score: 46.05 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 900 DLKELENKYQQLSEEKTILAEQLQAETELFAEAEemraRLAARKQELEDIlhelesrvEEEEERCQQLQGDKKKMQQHVQ 979
Cdd:COG0497 155 AQEAYQEAYQAWKQARRELEDLQEKERERAQRAD----LLQFQLEELEEL--------NLQPGEDEELEEERKRLSNSEK 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 980 DLEEQLEeeeaARQKLQLE--KVSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEERLSEFTSHMAEEEEKVKSLSKLRNK 1057
Cdd:COG0497 223 LAEAIQN----ALELLSGEddTVSALSLLGRALEALEDLSEYDGKLSELAELLEEALYELEEASEELRAYLDELEFDPNR 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1058 YEAVmadmEDRLkkeekgrQELEKLKRKLDGEAGDLQEQVAELQQQLEELrQALARKEAELQAALARVEDEAAQKNAVLK 1137
Cdd:COG0497 299 LEEV----EERL-------FALKSLARKYGVTIEDLLEYLDKIKEELAQL-DNSEESLEALEKEVKKLKAELLEAAEALS 366
|
250 260
....*....|....*....|
gi 1033370542 1138 SLR-----ELQAQL-AELQE 1151
Cdd:COG0497 367 AIRkkaakELEKEVtAELKA 386
|
|
| Atg14 |
pfam10186 |
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ... |
1103-1246 |
2.83e-04 |
|
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N-terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.
Pssm-ID: 431120 [Multi-domain] Cd Length: 347 Bit Score: 45.14 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1103 QLEELRQALARKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQEdmesEKLARAKAEKQRRDLGEELEALKTELE 1182
Cdd:pfam10186 20 RLYELRVRLARLLSENDSLKKKVEEALEGKEEGNQLEDNIGNKKLKLRL----LKSEIAISNERLNEIKDKLDQLRREIA 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033370542 1183 DTLDSTAAQQELRSKREQEVTELKKTIEEEVKVHEAQVLDMRQRHTSALEELSEQLEQSRRFKI 1246
Cdd:pfam10186 96 EKKKKIEKLRSKLKQRRSDLESAQYQLEERRASQLAKLQNSIKRIKQKWTALHSLTAESRSFLC 159
|
|
| Cortex-I_coil |
pfam09304 |
Cortexillin I, coiled coil; Members of this family are predominantly found in the ... |
1083-1186 |
2.86e-04 |
|
Cortexillin I, coiled coil; Members of this family are predominantly found in the actin-bundling protein Cortexillin I from Dictyostelium discoideum. They adopt a structure consisting of an 18-heptad-repeat alpha-helical coiled-coil, and are a prerequisite for the assembly of Cortexillin I.
Pssm-ID: 312712 [Multi-domain] Cd Length: 107 Bit Score: 42.30 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1083 KRKLDGEAGDLQEQVAELQQQLEE---LRQALARKEAELQAALARVEDEAAQKNavlKSLRELQAQLAELQEDMESEKLA 1159
Cdd:pfam09304 4 KERLEASKNSLANKLAGLENSLESektSREQLIKQKDELESLLASLEQENAERE---KRLRELEAKLDEALKNLELEKLA 80
|
90 100
....*....|....*....|....*..
gi 1033370542 1160 RAKAEKQRRDLGEELEALKTELEDTLD 1186
Cdd:pfam09304 81 RMELESRLSKTEKDKAILELKLAEALD 107
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1603-1825 |
2.92e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1603 ERELQNRDDANDdKKKLLSKQVRELEAELdaerkQRAQA-LAGRKKLELDLQEAMAQLDAANKGRDEAGKQLRKLQAQmk 1681
Cdd:PRK11281 38 EADVQAQLDALN-KQKLLEAEDKLVQQDL-----EQTLAlLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDD-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1682 elwreveEARAAREEIFIQS-RESEKKLKNLEAELLQLQEDLA-----------ASERAKRQ---AQQERDDLADELANG 1746
Cdd:PRK11281 110 -------NDEETRETLSTLSlRQLESRLAQTLDQLQNAQNDLAeynsqlvslqtQPERAQAAlyaNSQRLQQIRNLLKGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1747 NSGKSALLDEKRH-LEARIgqleeeldeeqSNMELLNDrYRKLSMQVETLTTELGAERsFSQKTENArQQLERQNKDLRA 1825
Cdd:PRK11281 183 KVGGKALRPSQRVlLQAEQ-----------ALLNAQND-LQRKSLEGNTQLQDLLQKQ-RDYLTARI-QRLEHQLQLLQE 248
|
|
| TolA |
COG3064 |
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1044-1223 |
3.05e-04 |
|
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225606 [Multi-domain] Cd Length: 387 Bit Score: 45.32 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1044 EEEKVKSLSKLRNKYEAVMADMEDRLKKEEKGRQELEKlKRKLDGEAGDLQEQvaELQQQLEELRQALARKEAELQAALA 1123
Cdd:COG3064 78 EQQRKKKEEQVAEELKPKQAAEQERLKQLEKERLKAQE-QQKQAEEAEKQAQL--EQKQQEEQARKAAAEQKKKAEAAKA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1124 RVEDEAAQKNA----------VLKSLRELQAQLAELQEDMESEKLARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQE 1193
Cdd:COG3064 155 KAAAEAAKLKAaaeakkkaeeAAKAAEEAKAKAEAAAAKKKAEAEAKAAAEKAKAEAEAKAKAEKKAEAAAEEKAAAEKK 234
|
170 180 190
....*....|....*....|....*....|
gi 1033370542 1194 LRSKREQEVTELKKTIEEEVKVHEAQVLDM 1223
Cdd:COG3064 235 KAAAKAKADKAAAAAKAAERKAAAAALDDI 264
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1115-1315 |
3.18e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1115 EAELQA---ALARVEDEAAQKNAVLKSLRELQAQLAELQ---EDMESEKLARAKAEKQRRDLGEELEALKTELEDTLDST 1188
Cdd:PRK11281 38 EADVQAqldALNKQKLLEAEDKLVQQDLEQTLALLDKIDrqkEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1189 AAQQELR--SKREQEVTELKKTIEEEVKVHEAQVLDMR---QRHTSALEELSEQLEQSRRFKINLEKTKQALEGEN-AEM 1262
Cdd:PRK11281 118 LSTLSLRqlESRLAQTLDQLQNAQNDLAEYNSQLVSLQtqpERAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQrVLL 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1033370542 1263 QKEVKLLQAaklESEQRRKKLEG--QVQELqlrageGERAKAELVERLVKLQNEL 1315
Cdd:PRK11281 198 QAEQALLNA---QNDLQRKSLEGntQLQDL------LQKQRDYLTARIQRLEHQL 243
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
828-1132 |
3.24e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.88 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 828 ARKAFMKKQQQMSALK---VMQRNcaaylklRHWQWWRLFTKVKPLLQVTRQDEVMQ-AKAVELQKVQ-EKHTKTQMDLK 902
Cdd:pfam17380 324 ARQAEMDRQAAIYAEQermAMERE-------RELERIRQEERKRELERIRQEEIAMEiSRMRELERLQmERQQKNERVRQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 903 ELE--NKYQQLSEEKTILAEQLQAETELF------AEAEEMRARLAARKQELEDIlhelesrVEEEEERCQQLQgdkkKM 974
Cdd:pfam17380 397 ELEaaRKVKILEEERQRKIQQQKVEMEQIraeqeeARQREVRRLEEERAREMERV-------RLEEQERQQQVE----RL 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 975 QQHVQDLEeqleeeeaaRQKLQLEKVSTEAKLkkmeedllvLEDQNsklhkeRKLMEERLSEFTSHMAEEEEKVKSLSKL 1054
Cdd:pfam17380 466 RQQEEERK---------RKKLELEKEKRDRKR---------AEEQR------RKILEKELEERKQAMIEEERKRKLLEKE 521
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1033370542 1055 RNKYEAVMADMEDRLKKEEKGRQELEKLKRKldgeagdlqeQVAELQQQLEELRQALARKEAELQAALARVEDEAAQK 1132
Cdd:pfam17380 522 MEERQKAIYEEERRREAEEERRKQQEMEERR----------RIQEQMRKATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1423-1692 |
3.43e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 45.10 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1423 AAKDLESLSVRYEERVQACDKLEKGRTRLQQELDDVTVALDQQRQVVSALEKKQKKFDqmlAEEKLISARYAEERDRAEA 1502
Cdd:COG4942 29 AAFSAAADDKQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETA---DDLKKLRKQIADLNARLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1503 DAREKETKVLSLSRALEEALETREEMERQNKQLRAEMDDLVSSKDDVGKNVHELERFKRALEQQVQEMRAQMEELEDElq 1582
Cdd:COG4942 106 LEVQEREQRRRLAEQLAALQRSGRNPPPALLVSPEDAQRSVRLAIYYGALNPARAERIDALKATLKQLAAVRAEIAAE-- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1583 atedgKLRLEVNMQALKAQHERELQNRddanDDKKKLLskqvRELEAELDAERKQRAQALAGRKKLELDLQEAMAQLDAA 1662
Cdd:COG4942 184 -----QAELTTLLSEQRAQQAKLAQLL----EERKKTL----AQLNSELSADQKKLEELRANESRLKNEIASAEAAAAKA 250
|
250 260 270
....*....|....*....|....*....|
gi 1033370542 1663 NKGRDEAGKQLRKLQAQMKELWREVEEARA 1692
Cdd:COG4942 251 REAAAAAEAAAARARAAEAKRTGETYKPTA 280
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1243-1597 |
3.44e-04 |
|
Intermediate filament protein;
Pssm-ID: 425436 [Multi-domain] Cd Length: 313 Bit Score: 44.91 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1243 RFKINLEKTkQALEGENAEMQKEVKLLQAAKLESEQRRKKL-EGQVQEL--QLRAGEGERAKAELverlvklqnELDGVS 1319
Cdd:pfam00038 12 RLASYIDKV-RFLEQQNKDLETKISELRQKKGAEPSRLYSLyEREIRELrrQLDTLTVERARLQL---------ELDNLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1320 GTLGSTESKTIKLAKDLATVESHLQDTQELLQEETRQKLNLSSRVRQLEEEKAAMleqleeeeaaKANFSRQMQSLQQQV 1399
Cdd:pfam00038 82 LAAEDFRQKYEDELNLRQSAEADIVGLRKDLDEATLARVDLEMKIESLKEELAFL----------KKNHEEEVRELQSQV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1400 METKKKLEEDAG----VAEAIEEARRraakDLESLSVRYEERVQAcdklekgrtRLQQELDDVTVALDQQRQVVSAlekk 1475
Cdd:pfam00038 152 SDTQVNVEMDAArkldLTSALAEIRA----QYEEIAEKNREEAEE---------WYQSKLEELQQAAARNGDALRS---- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1476 qkkfdqmlAEEKLISARYAEERDRAEADAreketkVLSLSRALEEAL-ETREEMERQNKQLRAEMDDLvsskddvgknvh 1554
Cdd:pfam00038 215 --------AKEEITELRRQIQSLEIELQS------LKKQKASLERQLaETEERYELQLADYQELISEL------------ 268
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1033370542 1555 elerfkralEQQVQEMRAQMEELEDELQATEDGKLRLEVNMQA 1597
Cdd:pfam00038 269 ---------EAELQQIRQEMARQLREYQELLNVKLALDIEIAT 302
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1129-1373 |
3.70e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1129 AAQKNAVLKSLRELQAQLAELQEdmeseklarakaekqRRDLGEELEALKTELEDTLDSTAAQQelrsKREQEVTELKKT 1208
Cdd:PRK11281 28 RAASNGDLPTEADVQAQLDALNK---------------QKLLEAEDKLVQQDLEQTLALLDKID----RQKEETEQLKQQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1209 I-----------EEEVKVHEAQVLDMRQRHTSA-LEELSEQLEQSRrfkINLEKTKQALEGENAEM---QKEVKLLQAAK 1273
Cdd:PRK11281 89 LaqapaklrqaqAELEALKDDNDEETRETLSTLsLRQLESRLAQTL---DQLQNAQNDLAEYNSQLvslQTQPERAQAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1274 LESEQR----RKKL-EGQVQELQLRAGEGERAKAELVerLVKLQNELDGVSGTLGSTESKTIKLAKDLATVES-HLQDTQ 1347
Cdd:PRK11281 166 YANSQRlqqiRNLLkGGKVGGKALRPSQRVLLQAEQA--LLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIqRLEHQL 243
|
250 260
....*....|....*....|....*...
gi 1033370542 1348 ELLQEETRQK-LNLSSR-VRQLEEEKAA 1373
Cdd:PRK11281 244 QLLQEAINSKrLTLSEKtVQEAQSQDEA 271
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
886-1351 |
3.78e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.66 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 886 ELQKVQEKHTKTQMDLKELENKYQQLSEEKTILAEQLQAETELFAEAEEMRARLAARKQELEDILhELESRVEEEEERCQ 965
Cdd:PRK01156 205 QIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMEL-EKNNYYKELEERHM 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 966 QLQGDKK-KMQQHVQDLEEQLEEEEAARQKLQ---LEKVSTEAKLKKMEE------DLLVLEDQNSKLHKERKLMEERLS 1035
Cdd:PRK01156 284 KIINDPVyKNRNYINDYFKYKNDIENKKQILSnidAEINKYHAIIKKLSVlqkdynDYIKKKSRYDDLNNQILELEGYEM 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1036 EFTSHMAEEEEKVKSLSKLRNKYEAVMADMEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKE 1115
Cdd:PRK01156 364 DYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELS 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1116 AELQAALAR------------------VEDEAAQKNAVLKSLRELQAQLAELQEDMESEK--LARAKAEKQRRDLGE--E 1173
Cdd:PRK01156 444 RNMEMLNGQsvcpvcgttlgeeksnhiINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKkrKEYLESEEINKSINEynK 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1174 LEALKTELEDTLDSTAAQQELRSKREQEVTELKKTIEEEVKVHEAQVLD-MRQRHT-------SALEELSEQL----EQS 1241
Cdd:PRK01156 524 IESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNaLAVISLidietnrSRSNEIKKQLndleSRL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1242 RRFKINLEKTKQALEGENAEMQKEVKLLQAAKLESEQR---RKKLEGQVQELQLRAGEG---ERAKAELVERLVKLQNEL 1315
Cdd:PRK01156 604 QEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENkilIEKLRGKIDNYKKQIAEIdsiIPDLKEITSRINDIEDNL 683
|
490 500 510
....*....|....*....|....*....|....*.
gi 1033370542 1316 DGVSGTLGSTESktiKLAKDLATVESHLQDTQELLQ 1351
Cdd:PRK01156 684 KKSRKALDDAKA---NRARLESTIEILRTRINELSD 716
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
886-1194 |
3.80e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 429718 [Multi-domain] Cd Length: 488 Bit Score: 45.26 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 886 ELQKVQEKHTKTQMDLKELENKYQQLSEEKTILAEQLQAETELFAEAEEMRARLAARKQELEDILhelesrveeeeercq 965
Cdd:pfam07888 88 ELRQSREKVEELEEKYKELSRSGEELAEEKDALLAQRAESEARIRELEEDIKTLTQRVLERETEL--------------- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 966 qlqgdkKKMQQHVQDLEEQLEEEEAARQKLQLEKVSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEERLSEFTSHMAEEE 1045
Cdd:pfam07888 153 ------ERMKERVKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1046 EKVKSLSKLRNKYEAVMADMEDRLKKEEKGRQELEKLKRKLDGEAGDLQE---QVAELQQQLEELRQAL----ARKEAEL 1118
Cdd:pfam07888 227 RKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQarlQAAQLTLQLADASLALregrARWAQER 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1119 QAALARVEdeaAQKNAVLKSLRELQAQLAELQED-MESEKL----------ARAKAEKQRRDLGEELEALKTELEDTLDS 1187
Cdd:pfam07888 307 ETLQQSAE---ADKDRIEKLSAELQRLEERLQEErMEREKLevelgrekdcNRVQLSESRRELQELKASLRVAQKEKEQL 383
|
....*..
gi 1033370542 1188 TAAQQEL 1194
Cdd:pfam07888 384 QAEKQEL 390
|
|
| YhaN |
COG4717 |
Uncharacterized protein YhaN, contains AAA domain [Function unknown]; |
1228-1966 |
3.83e-04 |
|
Uncharacterized protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 227061 [Multi-domain] Cd Length: 984 Bit Score: 45.60 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1228 TSALEELSEQLEQSRRFKINLEKtKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGERAKAELVER 1307
Cdd:COG4717 153 TSGSPASTKLLEVLNKEADSLYK-PSGRNPQINQLLEKLKQERNEIDEAEKEYATYHKLLESRRAEHARLAELRSELRAD 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1308 LVKLQNELDGVSGTLGSTESKTIKLAKDLATVESHLQDTQELLQEETRQKlNLSSRVRQLE---EEKAAMLEQLEEEEAA 1384
Cdd:COG4717 232 RDHIRALRDAVELWPRLQEWKQLEQELTRRREELATFPRDGVLRLEKREA-HLQKTEAEIDallVRLAELKDLASQLIPA 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1385 KANFSRQMQSLQQQVMETKKKLEEDAGVAEAIEEARRRaaKDLESLSVRYEERVQACDKLEKGRT------RLQQELDDV 1458
Cdd:COG4717 311 KEAVLQALVRLHQQLSEIKASAFELTETLAGIEADLRD--KEEAAGNGFEAERVHDLRSLECMLRyqssqrELKQTEAAY 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1459 TVALDQQRQvvsalekkqkkFDQMLAEEKLISARYAEERDRAEADAREKETKVLSLSRALEEALETREEMERQNKQLRAE 1538
Cdd:COG4717 389 CKRLDEKRL-----------FEDEAEEEARQRLADDEEEVRAGDEAREEKIAANSQVIDKEEVCNLYDRRDTAWQKQRFL 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1539 MDdlvsskddvgknvhELERFKRALEQQ---VQEMRAQME--ELEDELQATEDGKLRLEVNMQALKAQherelqnrddan 1613
Cdd:COG4717 458 RE--------------KQTAFERQKTEHtkiIALRLAGMLlvALSRLLTSLIFQIIFAVAQIVFLSAE------------ 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1614 ddkKKLLSKQVRELEAELDAERKQRAQALAgrkklELDLQEAMAQLDAANKGRDEAGKQLRKL---QAQMKELWREVEEA 1690
Cdd:COG4717 512 ---IKSSSRAVREEKAAVTDIPEELARLLI-----TDELPELAVDLLVQSRIRQHWQQLRKALdqlEAAYEALEGRFAAA 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1691 RAAREEIFIQSRE-------SEKKLKNLEAELLQLQEDLAASERAKRQAQQERDDLADELANGNSGKSALLDEkrhLEAR 1763
Cdd:COG4717 584 EAAMAEWQSEWEEaldelglSRELSPEQQLDILSTMKDLKKLMQKKAELTHQVARLREEQAAFEERVEGLLAV---LEAQ 660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1764 IGQLEEE--LDEEQSNMELLNDRYRKLSMQVETLTTELGAErsfsqkTENARQQLERQNKDL--RAKLGEMDSSVKSKYK 1839
Cdd:COG4717 661 FIDLSTLfcVQRLRVAAELQKEEARLALEGNIERTKELNDE------LRAELELHRKEILDLfdCGTADTEDAFREAARE 734
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1840 MAIAT-LESKVAQLEEQLEQESRERIlsGKLVRRAEKKLKEVILQVDEERRnaDQYKDQVEKGHLRLKQLKRQLEEAEEE 1918
Cdd:COG4717 735 EQQLTqRESRLESLEAQLEGVAAEAY--ELSASLDQRELKEEELALLEEAI--DALDEEVEELHAQVAALSRQIAQLEGG 810
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1033370542 1919 ASRANAsRRRMQRELEDVTESAESMNREVTSLRNRLSKVERRQRKRTP 1966
Cdd:COG4717 811 GTVAEL-RQRRESLKEDLEEKARKWASLRLAVQVLEEALRLFKERRLP 857
|
|
| YhaN |
COG4717 |
Uncharacterized protein YhaN, contains AAA domain [Function unknown]; |
1057-1826 |
3.83e-04 |
|
Uncharacterized protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 227061 [Multi-domain] Cd Length: 984 Bit Score: 45.60 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1057 KYEAVMADMEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQvaelQQQLEELRQALARKEAElQAALARVEDEAAQKNAVL 1136
Cdd:COG4717 161 KLLEVLNKEADSLYKPSGRNPQINQLLEKLKQERNEIDEA----EKEYATYHKLLESRRAE-HARLAELRSELRADRDHI 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1137 KSLRELQAQLAELQEDME-SEKLARAKAEKQR--RDLGEELEALKTELEdtldSTAAQQELRSKREQEVTELKKtieeev 1213
Cdd:COG4717 236 RALRDAVELWPRLQEWKQlEQELTRRREELATfpRDGVLRLEKREAHLQ----KTEAEIDALLVRLAELKDLAS------ 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1214 kvheaQVLDMRQRHTSALEELSEQLeqSRRFKINLEKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEgQVQELQLR 1293
Cdd:COG4717 306 -----QLIPAKEAVLQALVRLHQQL--SEIKASAFELTETLAGIEADLRDKEEAAGNGFEAERVHDLRSLE-CMLRYQSS 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1294 AGEGERAKAELVERLVKLQNELDgvsgtlgSTESKTIKlakDLATVESHLQDTQELLQEetrqKLNLSSRVRQLEEEKAA 1373
Cdd:COG4717 378 QRELKQTEAAYCKRLDEKRLFED-------EAEEEARQ---RLADDEEEVRAGDEAREE----KIAANSQVIDKEEVCNL 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1374 MLEQLEEEEaakanfsRQMQSLQQQVMETKKKLEEDAGVAeaieeaRRRAAKDLESLSVRYEERVQACDKLEKGRTRLQQ 1453
Cdd:COG4717 444 YDRRDTAWQ-------KQRFLREKQTAFERQKTEHTKIIA------LRLAGMLLVALSRLLTSLIFQIIFAVAQIVFLSA 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1454 ELDDVTVALDQQRQVVSALEKKQKKFDQMLAEEKLISARYAEERDRAEADAREKETKVLSlsraleealETREEMERQNK 1533
Cdd:COG4717 511 EIKSSSRAVREEKAAVTDIPEELARLLITDELPELAVDLLVQSRIRQHWQQLRKALDQLE---------AAYEALEGRFA 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1534 QLRAEMDDLVSskddvgknvhELERFKRALEQQVQEMRAQMEELEDELQA-TEDGKLRLEVNMQALK-AQHERELQNRDD 1611
Cdd:COG4717 582 AAEAAMAEWQS----------EWEEALDELGLSRELSPEQQLDILSTMKDlKKLMQKKAELTHQVARlREEQAAFEERVE 651
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1612 ANDdkkKLLSKQVRELEAELDAERKQRAQALA---GRKKLELDLQEAMAQLDAANKGRDEAGKQLRKLqaqmkelwreVE 1688
Cdd:COG4717 652 GLL---AVLEAQFIDLSTLFCVQRLRVAAELQkeeARLALEGNIERTKELNDELRAELELHRKEILDL----------FD 718
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1689 EARAAREEIFIQSRESEKKLKNLEAELlqlQEDLAASERAkrqaqqerDDLADELANGNSGKSALLDEKRHLEARIgqle 1768
Cdd:COG4717 719 CGTADTEDAFREAAREEQQLTQRESRL---ESLEAQLEGV--------AAEAYELSASLDQRELKEEELALLEEAI---- 783
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 1033370542 1769 eelDEEQSNMELLNDRYRKLSMQVETLttELGAERSfsqkteNARQQLERQNKDLRAK 1826
Cdd:COG4717 784 ---DALDEEVEELHAQVAALSRQIAQL--EGGGTVA------ELRQRRESLKEDLEEK 830
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1540-1894 |
4.18e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.81 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1540 DDLVSSKDDVGKNVHELERFKRALEQQVQEMRAQMEELEDelqatedgklrleVNMQALKAQHERELQNRDD---ANDDK 1616
Cdd:TIGR01612 1118 DDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLED-------------VADKAISNDDPEEIEKKIEnivTKIDK 1184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1617 KKLLSKQVRELEAELdAERKQRAQALAGRKKLELDLQEAMAQ--LDAANKGRDEAGKQLRKLQAQMKELwreveearaar 1694
Cdd:TIGR01612 1185 KKNIYDEIKKLLNEI-AEIEKDKTSLEEVKGINLSYGKNLGKlfLEKIDEEKKKSEHMIKAMEAYIEDL----------- 1252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1695 EEIFIQSRESEKKLK-----NLEAELLQLQEDlaASERAKRQAQQERDDLAD------ELANGNSGKSALLDEKRHLEAR 1763
Cdd:TIGR01612 1253 DEIKEKSPEIENEMGiemdiKAEMETFNISHD--DDKDHHIISKKHDENISDirekslKIIEDFSEESDINDIKKELQKN 1330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1764 IGQLEEELDEEQSNMELLNDRYRKLsmqvetlttELGAERSFSQKTENARQQLERQNKDLRAKLGEMDSSVKS-KYKMAI 1842
Cdd:TIGR01612 1331 LLDAQKHNSDINLYLNEIANIYNIL---------KLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKiKDDINL 1401
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1033370542 1843 ATLESKVaqleeqleqesrERILSGKLVRRAEKKLKEVILQVDEERRNADQY 1894
Cdd:TIGR01612 1402 EECKSKI------------ESTLDDKDIDECIKKIKELKNHILSEESNIDTY 1441
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1007-1238 |
4.88e-04 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 45.02 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1007 KKMEEDLLVLEDQNSKLHKERKLMEERLSEFTSHMAEEEEKVKSLSKLRNKYEAVMADMEDRLKKEEKGRQELeklkRKL 1086
Cdd:COG4372 67 RNLRSGVFQLDDIRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQQEL----ARL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1087 DGEAGDLQEQVAEL---QQQLEELRQALARKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQEDMESEKLARAKA 1163
Cdd:COG4372 143 TKQAQDLQTRLKTLaeqRRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLATRANAAQARTEELARR 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1033370542 1164 EKQRRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVTELKKT---IEEEVKVHEAQVLDMRQRHTSALEELSEQL 1238
Cdd:COG4372 223 AAAAQQTAQAIQQRDAQISQKAQQIAARAEQIRERERQLQRLETAqarLEQEVAQLEAYYQAYVRLRQQAAATQRGQV 300
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
1073-1553 |
5.38e-04 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 227606 [Multi-domain] Cd Length: 833 Bit Score: 45.02 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1073 EKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQAALARVEDeAAQKNAVLKSLRELQAQLAElqed 1152
Cdd:COG5281 177 YAGAQETEAFNKVLILTGEYAGTTAAQLRAGAAAGITQHQAAEVLAQLVAAGVAT-AEQLGDVAQAAARFASASGE---- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1153 mESEKLARAkAEKQRRDLGEELEALKTELEDTldsTAAQQELRSKREQEVTELKKTIEEEVKVHEAQVLDMR-QRHTSAL 1231
Cdd:COG5281 252 -SIDKTIKA-FSKLTDDPVNGAKALNRQFHYL---TAAQLEQIAALQRAGDTAAAAAAAAEAAAAMDDRTARvKENMGTL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1232 EelSEQLEQSRRFKinleKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGERAKAELVERLVKL 1311
Cdd:COG5281 327 E--TAWDALADAAK----KMWDAVLGIGREDKQAALLAAKLAAEKLARVTAQGALNARLKLAQDDLTQAELNYAAADQAA 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1312 -----QNELDGVSGTLGSTESKTIKLAKDLATVESHLQDTQELLQEETRQKLNLS-SRVRQLEEEKAAMLEQLEEEEAAK 1385
Cdd:COG5281 401 nqegaLNAREDEAEVLSTQEERRDILKNLLADAEKRTARQEELNKALAKAKILQAdKAAKAYQEDILQREAQSRGKTAAA 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1386 ANFSRQMQSLQQQVMETKKKLEEDAGVAEAIEEARRRAAKDLESLSVRYEERVQACDKLEKGRTRLQQELDDVTVALdqq 1465
Cdd:COG5281 481 ERSQEQMTAALKALLAFQQQIADLSGAKEKASDQKSLLWKAEEQYALLKEEAKQRQLQEQKALLEHKKETLEYTSQL--- 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1466 rqvvsALEKKQKKFDQMLAEEKLISARYAEERDRAEADAReketKVLSLSRALEEALETREEMERQNKQLRAEMDDLVSS 1545
Cdd:COG5281 558 -----AELLDQQADRFELSAQAAGSQKERGSDLYREALAQ----NAAALNKALNELAAYWSALDLLQGDWKAGALSALAN 628
|
....*...
gi 1033370542 1546 KDDVGKNV 1553
Cdd:COG5281 629 YRDSATDV 636
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
880-1141 |
5.79e-04 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 44.63 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 880 MQAKAVELQKVQEKHTKTQMDLKELENKYQQLSEEKTILAEQLQAETELFAEAEEMRARLAARKQELEDILHELESRVEE 959
Cdd:COG4372 83 LRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQQELARLTKQAQDLQTRLKTLAEQRRQ 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 960 EEERCQQLQGDKKKMQqhvqdleeqleeeeAARQKLQLEKVSTEAKLKKMEEdllvlEDQNskLHKERKLMEERLSEFTS 1039
Cdd:COG4372 163 LEAQAQSLQASQKQLQ--------------ASATQLKSQVLDLKLRSAQIEQ-----EAQN--LATRANAAQARTEELAR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1040 HMAEEEEKVKSLS----KLRNKYEAVMADMEDRLKKEEKGrQELEKlkrkldgEAGDLQEQVAELQ---QQLEELR-QAL 1111
Cdd:COG4372 222 RAAAAQQTAQAIQqrdaQISQKAQQIAARAEQIRERERQL-QRLET-------AQARLEQEVAQLEayyQAYVRLRqQAA 293
|
250 260 270
....*....|....*....|....*....|.
gi 1033370542 1112 ARKEAELQA-ALARVEDEAAQKNAVLKSLRE 1141
Cdd:COG4372 294 ATQRGQVLAgAAQRVAQAQAQAQAQAQLLSS 324
|
|
| NtpI |
COG1269 |
Archaeal/vacuolar-type H+-ATPase subunit I/STV1 [Energy production and conversion]; |
998-1152 |
5.95e-04 |
|
Archaeal/vacuolar-type H+-ATPase subunit I/STV1 [Energy production and conversion];
Pssm-ID: 224188 [Multi-domain] Cd Length: 660 Bit Score: 44.66 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 998 EKVSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEERLSEFTSHMA------EEEEKVKSLS-KLRN----KYEAVMADME 1066
Cdd:COG1269 86 EVEKLEAELKSLEEVIKPAEKFSSEVEELTRKLEERLSELDEELEdledllEELEPLAYLDfDLSLlrglKFLLVRLGLV 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1067 DRLKKEEK-------------------------GRQELEKLKRKLDGEAGDLQE----------QVAELQQQLEELRQAL 1111
Cdd:COG1269 166 RREKLEALvgviedevalygenveasvvivvahGAEDLDKVSKILNELGFELYEvpefdggpseLISELEEVIAEIQDEL 245
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1033370542 1112 ARKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQED 1152
Cdd:COG1269 246 ESLRSELEALAEKIAEELLAVREILEIEKALGDVLSKLART 286
|
|
| EVC2_like |
pfam12297 |
Ellis van Creveld protein 2 like protein; This family of proteins is found in eukaryotes. ... |
1020-1193 |
5.96e-04 |
|
Ellis van Creveld protein 2 like protein; This family of proteins is found in eukaryotes. Proteins in this family are typically between 571 and 1310 amino acids in length. There are two conserved sequence motifs: LPA and ELH. EVC2 is implicated in Ellis van Creveld chondrodysplastic dwarfism in humans. Mutations in this protein can give rise to this congenital condition. LIMBIN is a protein which shares around 80% sequence homology with EVC2 and it is implicated in a similar condition in bovine chondrodysplastic dwarfism.
Pssm-ID: 432462 [Multi-domain] Cd Length: 429 Bit Score: 44.66 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1020 NSKLHKERKLMEERLSE--------FTSHMA-EEEEKVKSLSKlrnKYEAVMADMEDRLKK-EEKGRQELEKLKRKLDG- 1088
Cdd:pfam12297 198 SSVFNKQFLAMEGRLQEeygrkmaaLAAECNlETREKMEAQHQ---KEMAEKEEAEELLQHaSEQEALECSSLLDKLHKl 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1089 EAGDLQ--------EQVAELQQQLEELRqalaRKE------AELQAALARVEDEAAQKNAVLKSLRELQAQLAEL-QEDM 1153
Cdd:pfam12297 275 EQEHLQrslllkqeEEFAKARRQLAVKR----RVElhkiffEQLKEATRKGELKEEAAKRLLHDYSKIQDTIEELmDFFQ 350
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1033370542 1154 ESEKLARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQE 1193
Cdd:pfam12297 351 ANQRYHLEERFAQREYLVKSLQSLETHISALLNTAATQLT 390
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1066-1312 |
6.44e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 224259 [Multi-domain] Cd Length: 294 Bit Score: 43.90 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1066 EDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQAALARVEDEAAQKNAVLKSLRELQAQ 1145
Cdd:COG1340 12 ELKRKQLKEEIEELKEKRDELRKEASELAEKRDELNAKVRELREKAQELREERDEINEEVQELKEKRDEINAKLQELRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1146 LAELQEDMESEKLARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRSKREQ-EVTELKKTIEEEVKVHEAQVLDMR 1224
Cdd:COG1340 92 YRELKEKRNEFNLGGRSIKSLEREIERLEKKQQTSVLTPEEERELVQKIKELRKElEDAKKALEENEKLKELKAEIDELK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1225 QRHTSALEELSEQLEQSRRFKINLEKTKQALEgenaEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGERAKAEL 1304
Cdd:COG1340 172 KKAREIHEKIQELANEAQEYHEEMIKLFEEAD----ELRKEADELHEEFVELSKKIDELHEEFRNLQNELRELEKKIKAL 247
|
....*...
gi 1033370542 1305 VERLVKLQ 1312
Cdd:COG1340 248 RAKEKAAK 255
|
|
| HOOK |
pfam05622 |
HOOK protein; This family consists of several HOOK1, 2 and 3 proteins from different ... |
886-1267 |
6.47e-04 |
|
HOOK protein; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organisms. 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 the 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.
Pssm-ID: 428548 [Multi-domain] Cd Length: 526 Bit Score: 44.66 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 886 ELQKVQEKHTKTQMDLKELENKYQQLSEEKTILAEQLQAETELFAEAEEM--------RARLAARKQ--ELEDILHELES 955
Cdd:pfam05622 1 ELSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQAENKKLQERLNQLESFdesgtptsKKYSLLQKQleQLQEENFRLET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 956 RVEEEEERCQQLQGDKKKMQQHVQDLEEQLEEEEAARQKLQLEKVSTEaKLKKMEEDLLV----LEDQNSkLHKERKLME 1031
Cdd:pfam05622 81 ARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEIDILRESSD-KVSKLEATVETykkkLEDLGD-LRRQVKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1032 ERLSEFTSHMAEEEEKVKSLSKLRNKYEA-------VMADMEDRLKKEEKGRQELEKLKRKLDG----------EAGDLQ 1094
Cdd:pfam05622 159 ERNAVYMQNTVSLEEELKKANALRGQLELykrqvqeLHGKLSEESKKADKLEFEYKKLEEKLEAlqkekerliiERDTLR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1095 EQVAEL---QQQLEELRQALARKE--------------AELQAALARVEDEaaqkNAVLKSLRELQAQ--LAELQEDMES 1155
Cdd:pfam05622 239 ETNEELrcaQLQQDELSQADALGSpsssvdnlaaeilpAEIREKLIRLQHE----NKMLRLQQEGSERekLTELQALLED 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1156 EKLARAKAEKQRRDLGEELEALKTELEDTldsTAAQQELRSKREQEVTELKKTIEEEVKVHEAQvlDMRQRHTSALEELS 1235
Cdd:pfam05622 315 ANRRKNELETQNRLANQRILELQQQVEEL---QKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQ--EELQKKKEQLEELE 389
|
410 420 430
....*....|....*....|....*....|..
gi 1033370542 1236 EQLEQSRRFKINLEKTKQALEGENAEMQKEVK 1267
Cdd:pfam05622 390 PKVDSNLQKIDELQEALRKKDEDMKAMEERYK 421
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
997-1210 |
6.66e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 44.85 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 997 LEKVSTEAKLKKMEEDLLVLEDQNSKLH-----KERKLMEE---RLSEFTSH--------MAEEEEKVKSLSKLRNKYEA 1060
Cdd:PLN03229 479 VIAMGLQERLENLREEFSKANSQDQLMHpvlmeKIEKLKDEfnkRLSRAPNYlslkykldMLNEFSRAKALSEKKSKAEK 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1061 VMADMEDRLkKEEKGRQElekLKRKLDGEAGDLQEQVAELQQQL-EELRQALARKEAELQAALARV------EDEAAQKN 1133
Cdd:PLN03229 559 LKAEINKKF-KEVMDRPE---IKEKMEALKAEVASSGASSGDELdDDLKEKVEKMKKEIELELAGVlksmglEVIGVTKK 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1134 AVLKSLR----ELQAQLAELQEDMESE-----------------KLARAKAEKQRR-DLGEELEALKTELEDTLDSTAAQ 1191
Cdd:PLN03229 635 NKDTAEQtpppNLQEKIESLNEEINKKiervirssdlkskiellKLEVAKASKTPDvTEKEKIEALEQQIKQKIAEALNS 714
|
250
....*....|....*....
gi 1033370542 1192 QELRSKREQEVTELKKTIE 1210
Cdd:PLN03229 715 SELKEKFEELEAELAAARE 733
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1563-1752 |
6.85e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.41 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1563 LEQQVQEMRAQMEELEDE-LQATEDGKLRLEVNMQALKAQHERELQNRDDANDDKKKLLSKQVRELEAELDAERKQRAQA 1641
Cdd:PRK09510 92 LQQKQAAEQERLKQLEKErLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1642 LAGRKKLELDLQEAMAQLDAANKGRDEAGKqlrKLQAQMKELWREVEEARAAREEIFIQSRESEKKLKNLEAEllqlqed 1721
Cdd:PRK09510 172 EAEAAKKAAAEAKKKAEAEAAAKAAAEAKK---KAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKA------- 241
|
170 180 190
....*....|....*....|....*....|.
gi 1033370542 1722 LAASERAKRQAQQERDDLADELANGNSGKSA 1752
Cdd:PRK09510 242 AAAKAAEKAAAAKAAAEVDDLFGGLDSGKNA 272
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1022-1233 |
7.91e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 42.82 E-value: 7.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1022 KLHKERKLMEERLSEFTSHMAEEE--EKVKSLSKLRNKYEAVMADMEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAE 1099
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDygDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1100 LQQQLEELRQALARKEAELQAALARVEdEAAQKNAVLKSLRELQAQLAELQEDMESEKLARAKaeKQRRDLGEELEALKT 1179
Cdd:cd00176 84 LNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASEDLGKDLESVEELL--KKHKELEEELEAHEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1033370542 1180 ELEDTLDstaAQQELRSKREQEVTELKKTIEEEVKVHEAQVLDMRQRHTSALEE 1233
Cdd:cd00176 161 RLKSLNE---LAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1252-1551 |
8.26e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 43.94 E-value: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1252 KQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGERAKAELVERLVKLQNELDGVSGTLGSTESKTIK 1331
Cdd:COG4942 33 AAADDKQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARLNALEVQERE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1332 LAKDLAtveshlqdtqELLQEETRQKLNLSSRVRQLEEEKAAmleqleeEEAAKANFSRQMQSLQQQVMETKKKLEEDAG 1411
Cdd:COG4942 113 QRRRLA----------EQLAALQRSGRNPPPALLVSPEDAQR-------SVRLAIYYGALNPARAERIDALKATLKQLAA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1412 VAEAIEEARRraakdleslsvryeervqacdKLEKGRTRLQQELDDVTVALDQQRQVVSALEKKQKKFDQMLAEEKLISA 1491
Cdd:COG4942 176 VRAEIAAEQA---------------------ELTTLLSEQRAQQAKLAQLLEERKKTLAQLNSELSADQKKLEELRANES 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1492 RYAEERDRAEADAREKETKVLSLSRALEEALETREEMERQNKQLRAEMDDLVSSKDDVGK 1551
Cdd:COG4942 235 RLKNEIASAEAAAAKAREAAAAAEAAAARARAAEAKRTGETYKPTAPEKMLISSTGGFGA 294
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1096-1303 |
8.39e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.91 E-value: 8.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1096 QVAELQQQLEELRQALARKEAELQ-------AALARVEDEAAQKNAVLKSLRELQAQLAELQEDMES-----EKLARAKA 1163
Cdd:PRK11637 41 HASDNRDQLKSIQQDIAAKEKSVRqqqqqraSLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDElnasiAKLEQQQA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1164 EkQRRDLGEELEAL-----KTELEDTLDSTAAQQE---------LRSKREQEVTELKKTiEEEVKVHEAQVLDMRQRHTS 1229
Cdd:PRK11637 121 A-QERLLAAQLDAAfrqgeHTGLQLILSGEESQRGerilayfgyLNQARQETIAELKQT-REELAAQKAELEEKQSQQKT 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033370542 1230 AleeLSEQLEQsrrfkinlektKQALEGENAEMQKEVKLLQAAkLESEQRRKKlEGQVQELQLRageGERAKAE 1303
Cdd:PRK11637 199 L---LYEQQAQ-----------QQKLEQARNERKKTLTGLESS-LQKDQQQLS-ELRANESRLR---DSIARAE 253
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1657-1900 |
8.63e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 43.94 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1657 AQLDAANKGRDEAGKQLRKLQAQMKELWREVEEARAAReeifiqsRESEKKLKNLEAELLQLQEDLAASERAKRqaqQER 1736
Cdd:COG4942 45 KEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQL-------IETADDLKKLRKQIADLNARLNALEVQER---EQR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1737 DDLADELANGN-SGKSALLDEKRHLEarigqleeeldeEQSNMELLNDRYRKLSMQVETLTTELGAERsfsQKTENARQQ 1815
Cdd:COG4942 115 RRLAEQLAALQrSGRNPPPALLVSPE------------DAQRSVRLAIYYGALNPARAERIDALKATL---KQLAAVRAE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1816 LERQNKDLRAKLGEMDSSvKSKYKMAIATLESKVAQLEEQLEQESRERILSGKLVRRAEKKLKEVILQVDEERRNADQYK 1895
Cdd:COG4942 180 IAAEQAELTTLLSEQRAQ-QAKLAQLLEERKKTLAQLNSELSADQKKLEELRANESRLKNEIASAEAAAAKAREAAAAAE 258
|
....*
gi 1033370542 1896 DQVEK 1900
Cdd:COG4942 259 AAAAR 263
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1634-1962 |
9.77e-04 |
|
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: 44.29 E-value: 9.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1634 ERKQRAQALAGRKKLELDLQEAMAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEA---RAAREE-IFIQSRESEKKLK 1709
Cdd:TIGR02169 154 ERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAeryQALLKEkREYEGYELLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1710 NLEAELLQLQEDLAASERAKRQAQQERDDLADELAngnsgksALLDEKRHLEARIgqleeeldeeqsnMELLNDRYRKLS 1789
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLE-------EIEQLLEELNKKI-------------KDLGEEEQLRVK 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1790 MQVETLTTELgaersfsQKTENARQQLERQNKDLRAKLgemdssvkSKYKMAIATLESKVAQLEEQLEQESRERilsgkl 1869
Cdd:TIGR02169 294 EKIGELEAEI-------ASLERSIAEKERELEDAEERL--------AKLEAEIDKLLAEIEELEREIEEERKRR------ 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1870 vrraekklkevilqvdeerrnaDQYKDQVEKGHLRLKQLKRQLEEAEEEASRANASRRRMQRELEDVTESAESMNREVTS 1949
Cdd:TIGR02169 353 ----------------------DKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
|
330
....*....|...
gi 1033370542 1950 LRNRLSKVERRQR 1962
Cdd:TIGR02169 411 LQEELQRLSEELA 423
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1003-1582 |
1.02e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 44.13 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1003 EAKLKKMEEDLLVLEDQ-------NSKLHKERKLM--EERLSEFT----------SHMAEEEEKVKSLSKLRNKYEAVMA 1063
Cdd:pfam15964 127 EAEVKFCKEELSEMKQRvqvvvleNEKLQQELKSQtqEETLREQTlldssgnmqnSWCTPEDSRVHQTSKRPASHNLAER 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1064 DMEDRLKKEEKGRQELEKLK-------RKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQAALARVEDEAAQKNAvl 1136
Cdd:pfam15964 207 LKSATTGEDEKWRLELEKLKllyeaktEVLESQVKSLRKDLAESQKTCEDLKERLKHKESLVAASTSSRVGGLCLKCA-- 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1137 kslrELQAQLAELQEDMESEKLARAKaeKQRRDLGEELEALKTELEDtldstaAQQELRSKREQEVTELKKTieEEVKVH 1216
Cdd:pfam15964 285 ----QHEAVLAQTHTNVHMQTIERLT--KERDDLMSALVSVRSSLAE------AQQRESSAYEQVKQAVQMT--EEANFE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1217 EAQVLDMRQRHTSALEELSEQLEqsRRFKINLEKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQelqlragE 1296
Cdd:pfam15964 351 KTKALIQCEQLKSELERQKERLE--KELASQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVE-------K 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1297 GERAKAELVERLVKLQNELdgvsgtlgstESKTIKLAKDLATVESHLQDTQELLQEETRQKLNLSSRV-RQLEeekaaml 1375
Cdd:pfam15964 422 VTREKNSLVSQLEEAQKQL----------ASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTKTgRQLE------- 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1376 EQLEEEEAAKANFSRQMQSLQQQVMETKKKLEEDAGVAEAIEEARR-----RAAKDLESLSVRYEERVQACDKLEKGRtR 1450
Cdd:pfam15964 485 IKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESEHqlhltRLEKESIQQSFSNEAKAQALQAQQREQ-E 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1451 LQQELDDVTVALDQQRQVVSALEKKQKKFDQMLAEEKLISARYAEERdraeadAREKETKVLSLSRALEEALETREEMER 1530
Cdd:pfam15964 564 LTQKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEI------TQKSRSEVEQLSQEKEYLQDRLEKLQK 637
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1033370542 1531 QNKQLRAEMDDLVSSKDDVGKNVHELERFKRALEQQVQEMRAQMEELEDELQ 1582
Cdd:pfam15964 638 RNEELEEQCVQHGRMHERMKQRLRQLDKHCQATAQQLVQLLSKQNQLFKERQ 689
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1451-1958 |
1.06e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.04 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1451 LQQELDDVTVALDQQRQVVSALEKKQKKFDQMLAEEKLISARYAEERDR----AEADAREKETKVLsLSRALEEALETRE 1526
Cdd:pfam10174 135 LRKTLEEMELRIETQKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWERtrriAEAEMQLGHLEVL-LDQKEKENIHLRE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1527 EMERQNK--QLRAEMDDLVSSKDDVGKNVHELERFKRALEQQVQE----------------------------MRAQMEE 1576
Cdd:pfam10174 214 ELHRRNQlqPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMlktngllhtedreeeikqmevykshskfMKNKIDQ 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1577 LEDELQATEDGKLRLEVNMQALKAQHERELQNRDDAnddKKKLLSKQVRE--LEAELDAER---KQRAQALAGRKKLELD 1651
Cdd:pfam10174 294 LKQELSKKESELLALQTKLETLTNQNSDCKQHIEVL---KESLTAKEQRAaiLQTEVDALRlrlEEKESFLNKKTKQLQD 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1652 LQEAMA-----------QLDAANKGRDEAGKQLRKLQAQMKELWREVEEARAAREEIFIQSRESEKKLKNLEAELLQ--- 1717
Cdd:pfam10174 371 LTEEKStlageirdlkdMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEker 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1718 ----LQEDlaaSERAKRQAQQERDDLADELANGNSGKSALLDEKRHLEARIGQLEEELDEEQSNMELLNDRYRKLSMQVE 1793
Cdd:pfam10174 451 iierLKEQ---REREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVE 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1794 TLTTELGAERSFSQKTENARQQlERQNKDLRAKLGEMDSSVKSkYKMAIATLESKVAQLEEQLEQESRERILSgklvrra 1873
Cdd:pfam10174 528 QKKEECSKLENQLKKAHNAEEA-VRTNPEINDRIRLLEQEVAR-YKEESGKAQAEVERLLGILREVENEKNDK------- 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1874 EKKLKEviLQVDEERRNADQYKDQVEKGHLRLKQLKRQLEEAEEEASRA-NASRRRMQRELEDVTESAESMNREVTSLRN 1952
Cdd:pfam10174 599 DKKIAE--LESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREdNLADNSQQLQLEELMGALEKTRQELDATKA 676
|
....*.
gi 1033370542 1953 RLSKVE 1958
Cdd:pfam10174 677 RLSSTQ 682
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1071-1720 |
1.15e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.02 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1071 KEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEEL----RQALARKEAELQAA--LARVEDEAAQKNAVLKSLRELQA 1144
Cdd:PRK10246 192 QHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLtdeeKQLLTAQQQQQQSLnwLTRLDELQQEASRRQQALQQALA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1145 QLAELQEDMesEKLARAKAEKQRRDLGEELEalktELEDTLDSTAAQQELRSKREQEVTELKKTIEEEVKVHEAQVLDMR 1224
Cdd:PRK10246 272 AEEKAQPQL--AALSLAQPARQLRPHWERIQ----EQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQ 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1225 QRHTSALEE--------------------LSEQLEQSRRFKINLEKTKQALEGE-------NAEMQKEVKLLQAAKLESE 1277
Cdd:PRK10246 346 QSLNTWLAEhdrfrqwnnelagwraqfsqQTSDREQLRQWQQQLTHAEQKLNALpaitltlTADEVAAALAQHAEQRPLR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1278 QRRKKLEGQVQELQLRagegeraKAELVERLVKLQNELDGVSGTLGS------------TESKTI----KLAKDLATVES 1341
Cdd:PRK10246 426 QRLVALHGQIVPQQKR-------LAQLQVAIQNVTQEQTQRNAALNEmrqrykektqqlADVKTIceqeARIKDLEAQRA 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1342 HLQDTQ--------ELLQEETRQKLNLS---SRVRQLEEEKAAMleqleeeEAAKANFSRQMQSLQQQvmetkkkLEEDa 1410
Cdd:PRK10246 499 QLQAGQpcplcgstSHPAVEAYQALEPGvnqSRLDALEKEVKKL-------GEEGAALRGQLDALTKQ-------LQRD- 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1411 gvaeaiEEARRRAAKDLESLSVRYEErvqACDKLEKGRTrLQQELDDVTVALDQQRQVVSALEKKQKKFDQMLAEEKLIS 1490
Cdd:PRK10246 564 ------ESEAQSLRQEEQALTQQWQA---VCASLNITLQ-PQDDIQPWLDAQEEHERQLRLLSQRHELQGQIAAHNQQII 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1491 ARYAEERDRAEADAREKETKVLSLSRALEEA--LETREEMERQNKQLRAEMDDLVSskddvgknvhELERFKRALEQ--Q 1566
Cdd:PRK10246 634 QYQQQIEQRQQQLLTALAGYALTLPQEDEEAswLATRQQEAQSWQQRQNELTALQN----------RIQQLTPLLETlpQ 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1567 VQEMRAQMEELE-DELQATEDGKLRLEVNMQALKAQHERELQNRDDANDD-----KKKLLSKQVRELEAELDAERKQRAQ 1640
Cdd:PRK10246 704 SDDLPHSEETVAlDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQfdtalQASVFDDQQAFLAALLDEETLTQLE 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1641 ALagRKKLELDLQEAMAQLDAANKGRDEAGKQ----------LRKLQAQMKELWREVEEARAAREEIFIQSRESEKKLKN 1710
Cdd:PRK10246 784 QL--KQNLENQRQQAQTLVTQTAQALAQHQQHrpdgldltvtVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQ 861
|
730
....*....|
gi 1033370542 1711 LEAELLQLQE 1720
Cdd:PRK10246 862 QQALMQQIAQ 871
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1611-1726 |
1.16e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 224755 [Multi-domain] Cd Length: 225 Bit Score: 42.69 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1611 DANDDKKKLLSKQVRELEAELDAERKQRAQALAGRKKLELDLQEAMAQ--------LDAANKGRDEAGKQL----RKLQA 1678
Cdd:COG1842 20 DKAEDPEKMLEQAIRDMESELAKARQALAQAIARQKQLERKLEEAQARaekleekaELALQAGNEDLAREAleekQSLED 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1033370542 1679 QMKELWREVEEARAAREEIFIQSRESEKKLKNLEAELLQLQEDLAASE 1726
Cdd:COG1842 100 LAKALEAELQQAEEQVEKLKKQLAALEQKIAELRAKKEALKARKAAAK 147
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1390-1647 |
1.18e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 43.56 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1390 RQMQSLQQQVMETKKKLEedagvaeAIEEARRRAAKDLESLSVRYEERVQACDKLEKGRTRLQQELDDVTVALDQQRQVV 1469
Cdd:COG4942 59 DQRAKLEKQLKSLETEIA-------SLEAQLIETADDLKKLRKQIADLNARLNALEVQEREQRRRLAEQLAALQRSGRNP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1470 SALEKkqkkfdqMLAEEKLISARYAE-ERDRAEADAREKEtkvlSLSRALEEALETREEMERQNKQLRAEMDDLVSSKDD 1548
Cdd:COG4942 132 PPALL-------VSPEDAQRSVRLAIyYGALNPARAERID----ALKATLKQLAAVRAEIAAEQAELTTLLSEQRAQQAK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1549 VGKNVHELERFKRALEQQVQEMRAQMEELedELQATEDGKLRLEVNMQALKAQHERELQNRDDANDDKKKLLSKQVRELE 1628
Cdd:COG4942 201 LAQLLEERKKTLAQLNSELSADQKKLEEL--RANESRLKNEIASAEAAAAKAREAAAAAEAAAARARAAEAKRTGETYKP 278
|
250
....*....|....*....
gi 1033370542 1629 AELDAERKQRAQALAGRKK 1647
Cdd:COG4942 279 TAPEKMLISSTGGFGALRG 297
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1222-1472 |
1.26e-03 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 43.47 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1222 DMRQRHTSaLEELSEQLEQSRRFKINLEKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGERAK 1301
Cdd:COG4372 82 QLRALRTE-LGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQQELARLTKQAQDLQTRLKTLAEQR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1302 AELVERLVKLQNELDGVSGTLGSTESKTIKLAKDLATVEshlQDTQELlqeETRQKlnlssRVRQLEEEKAAMLEQLEEE 1381
Cdd:COG4372 161 RQLEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQIE---QEAQNL---ATRAN-----AAQARTEELARRAAAAQQT 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1382 EAAKANFSRQMQSLQQQVMETKKKLEEDAGVAEAIEEARRRAAKDLESLSVRYEERV-QACDKLEKGRTRLQQELDDVTV 1460
Cdd:COG4372 230 AQAIQQRDAQISQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQLEAYYQAYVrLRQQAAATQRGQVLAGAAQRVA 309
|
250
....*....|..
gi 1033370542 1461 ALDQQRQVVSAL 1472
Cdd:COG4372 310 QAQAQAQAQAQL 321
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1363-1642 |
1.27e-03 |
|
Intermediate filament protein;
Pssm-ID: 425436 [Multi-domain] Cd Length: 313 Bit Score: 42.98 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1363 RVRQLEEEKAAMLEQLEEEEAAKANFSRQMQSLQQQVMETKKKLEEDAGVAEA-IEEARRRAAKDLESLSVRYEERVQAC 1441
Cdd:pfam00038 19 KVRFLEQQNKDLETKISELRQKKGAEPSRLYSLYEREIRELRRQLDTLTVERArLQLELDNLRLAAEDFRQKYEDELNLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1442 DKLEKGRTRLQQELDDVTVA-LDQQRQVVSALEkkQKKFDQMLAEEKL--ISARYAEERDRAEADAREKetkvLSLSRAL 1518
Cdd:pfam00038 99 QSAEADIVGLRKDLDEATLArVDLEMKIESLKE--ELAFLKKNHEEEVreLQSQVSDTQVNVEMDAARK----LDLTSAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1519 EEaleTREEMERQNKQLRAEMDDLVSSK-----DDVGKNVHELerfkRALEQQVQEMRAQMEELEDELQATEDGKLRLEV 1593
Cdd:pfam00038 173 AE---IRAQYEEIAEKNREEAEEWYQSKleelqQAAARNGDAL----RSAKEEITELRRQIQSLEIELQSLKKQKASLER 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1033370542 1594 NMQALKAQHERELQNrddanddkkklLSKQVRELEAELDAERKQRAQAL 1642
Cdd:pfam00038 246 QLAETEERYELQLAD-----------YQELISELEAELQQIRQEMARQL 283
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1545-1965 |
1.30e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1545 SKDDVGKNVHELERFKRA---LEQQVQEMRAQMEELEDELQATEDGKLRLEvNMQALKAQHERELqnrddanddkkKLLS 1621
Cdd:PRK03918 146 SREKVVRQILGLDDYENAyknLGEVIKEIKRRIERLEKFIKRTENIEELIK-EKEKELEEVLREI-----------NEIS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1622 KQVRELEAELDAERKQRaqalagrkkleLDLQEAMAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEaraareeifiqS 1701
Cdd:PRK03918 214 SELPELREELEKLEKEV-----------KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE-----------L 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1702 RESEKKLKNLEAELLQLQEDLAASERAKRqaqqERDDLADELANGNSGKSALLDEKRHLEARIgqleeeldeeqSNMELL 1781
Cdd:PRK03918 272 KKEIEELEEKVKELKELKEKAEEYIKLSE----FYEEYLDELREIEKRLSRLEEEINGIEERI-----------KELEEK 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1782 NDRYRKLSMQVETLTTELGAERSFSQKTENARQQLERQNKdLRAKLGEMdssvkskykmaiaTLESKVAQLEEqleqesr 1861
Cdd:PRK03918 337 EERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELER-LKKRLTGL-------------TPEKLEKELEE------- 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1862 erilsgklVRRAEKKLKEVILQVDEERRNADQYKDQVEKGHLRLKQLK-------RQLEEAEEEA--SRANASRRRMQRE 1932
Cdd:PRK03918 396 --------LEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgRELTEEHRKEllEEYTAELKRIEKE 467
|
410 420 430
....*....|....*....|....*....|...
gi 1033370542 1933 LEDVTESAESMNREVTSLRNRLSKVERRQRKRT 1965
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLKKESELIKLKE 500
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1083-1604 |
1.38e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 428594 [Multi-domain] Cd Length: 562 Bit Score: 43.48 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1083 KRKL-DGEAGDLQEQVAELQQQLEELRQALARKEAELQAAL------------ARVEDEAAQKNAVLKSLRelqaqLAEL 1149
Cdd:pfam05701 36 RRKLvELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKrlieelklnlerAQTEEAQAKQDSELAKLR-----VEEM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1150 QEDMESEKLARAKAE----KQRRDLG-EELEALKTELEDT---LDSTAAQQELRSKREQEVTELKKTIEEEVKVHEAQVL 1221
Cdd:pfam05701 111 EQGIADEASVAAKAQlevaKARHAAAvAELKSVKEELESLrkeYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1222 DMRQRHTSALEELSEQLEQSRRFKINLEKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQlragegeRAK 1301
Cdd:pfam05701 191 ATKESLESAHAAHLEAEEHRIGAALAREQDKLNWEKELKQAEEELQRLNQQLLSAKDLKSKLETASALLL-------DLK 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1302 AELVERLV-KLQNELDGVSGTLGSTESKTIKLAKDLATVESHLQDTQELLQEETRQKLNLSSRVRQLEEEKAAMLEQLEE 1380
Cdd:pfam05701 264 AELAAYMEsKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAAASLRSELEKEKAELASLRQR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1381 EEAAKANFSrqmqSLQQQVMETKKKLEEdagVAEAIEEARRRAAKDLESLSVRYEERVQACDKLEKGRTRLQQELDDVTV 1460
Cdd:pfam05701 344 EGMASIAVS----SLEAELNRTKSEIAL---VQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQ 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1461 ALDQQRQVVSALEKKQKKFDQMLAEEKL-ISARYAEERDRAEADAREKETKVLSLSRALEEALE----TREEMERQNKQL 1535
Cdd:pfam05701 417 AKAAASTVESRLEAVLKEIEAAKASEKLaLAAIKALQESESSAESTNQEDSPRGVTLSLEEYYElskrAHEAEELANKRV 496
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1033370542 1536 RAEMDDLVSSKDDVGKNVHELERFKRALEQQVQEMRAQMEELEDelqaTEDGKLRLEVNMQALKAQHER 1604
Cdd:pfam05701 497 AEAVSQIEEAKESELRSLEKLEEVNREMEERKEALKIALEKAEK----AKEGKLAAEQELRKWRAEHEQ 561
|
|
| YhaN |
COG4717 |
Uncharacterized protein YhaN, contains AAA domain [Function unknown]; |
1319-1961 |
1.45e-03 |
|
Uncharacterized protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 227061 [Multi-domain] Cd Length: 984 Bit Score: 43.68 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1319 SGTLGSTESktIKLAKDLATVESHL---QDTQELLQEETRQKLNLSSRVRQLEEEKAAMLEQLEEEEAAkanfSRQMQSL 1395
Cdd:COG4717 151 SGTSGSPAS--TKLLEVLNKEADSLykpSGRNPQINQLLEKLKQERNEIDEAEKEYATYHKLLESRRAE----HARLAEL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1396 QQQVMETKKKLEEDAGVAEaiEEARRRAAKDLES-LSVRYEERVQ----ACDKLEKGRTRLQQ---ELDDVTVAL----D 1463
Cdd:COG4717 225 RSELRADRDHIRALRDAVE--LWPRLQEWKQLEQeLTRRREELATfprdGVLRLEKREAHLQKteaEIDALLVRLaelkD 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1464 QQRQVVSALEKKQKKFDQMLAEEKLISARYAEERDRAEADAREKETKVLSLSRALEEaleTREEMERQNKQLRAEMDDLV 1543
Cdd:COG4717 303 LASQLIPAKEAVLQALVRLHQQLSEIKASAFELTETLAGIEADLRDKEEAAGNGFEA---ERVHDLRSLECMLRYQSSQR 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1544 SSKDDVGKNVHELERFKRALEQQVQEMRAQMEELEDELQATEDGKLRLEVNMQAL--KAQHERELQNRDDANDDKKKLLS 1621
Cdd:COG4717 380 ELKQTEAAYCKRLDEKRLFEDEAEEEARQRLADDEEEVRAGDEAREEKIAANSQVidKEEVCNLYDRRDTAWQKQRFLRE 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1622 KQ---------------VRELEAELDAERKQRAQALAGRKKLELDLQEAMAQLDAANKGRDE---AGKQLRKLQAQMK-- 1681
Cdd:COG4717 460 KQtaferqktehtkiiaLRLAGMLLVALSRLLTSLIFQIIFAVAQIVFLSAEIKSSSRAVREekaAVTDIPEELARLLit 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1682 ELWREVEEARAAREEIFIQSRESEKKLKNLEAELLQLQEDLAASERAKRQAQQERDDLADELangnsGKSALLDEKRHLE 1761
Cdd:COG4717 540 DELPELAVDLLVQSRIRQHWQQLRKALDQLEAAYEALEGRFAAAEAAMAEWQSEWEEALDEL-----GLSRELSPEQQLD 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1762 ArigqleeelDEEQSNMELLNDRYRKLSMQVETLTTELgaeRSFSQKTENARQQLERQNKDL-----RAKLGEMDSSVKS 1836
Cdd:COG4717 615 I---------LSTMKDLKKLMQKKAELTHQVARLREEQ---AAFEERVEGLLAVLEAQFIDLstlfcVQRLRVAAELQKE 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1837 KYKMAIATLESKVAQLEEQLEQESRerilsgkLVRRAEKKLKEVILQVDEER-----RNADQYKDQVEKGHLRLKQLKRq 1911
Cdd:COG4717 683 EARLALEGNIERTKELNDELRAELE-------LHRKEILDLFDCGTADTEDAfreaaREEQQLTQRESRLESLEAQLEG- 754
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1912 LEEAEEEASRANASRRRMQRELEDVTESAESMNREVTSLRNRLSKVERRQ 1961
Cdd:COG4717 755 VAAEAYELSASLDQRELKEEELALLEEAIDALDEEVEELHAQVAALSRQI 804
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1092-1240 |
1.50e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 426264 [Multi-domain] Cd Length: 170 Bit Score: 41.49 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1092 DLQEQVAELQQQLEELRQALARKEAELQAALArvedeaaqknavlKSLRELQAQLAELQEDMesEKLARAKAEKQRRDLG 1171
Cdd:pfam01442 29 ETEALRERLQKDLEEVRAKLEPYLEELQAKLQ-------------QNVEELRQRLEPYTEEL--RKRLNADAEELQEKLA 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033370542 1172 EELEALKTELEDTLDSTAAQ-----QELRSKREQEVTELKKTIEEEVKVHEAQVldmrqrhTSALEELSEQLEQ 1240
Cdd:pfam01442 94 PYGEELRERLEQNVDALRARlapyaEELRQKLAERLEELKESLAPYAEEVQAQL-------SQRLQELREKLEP 160
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
966-1166 |
1.73e-03 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 43.09 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 966 QLQGDKKKMQQHVQDLEEQLEEEEAARQKLQL---EKVSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEERLSEFTSHMA 1042
Cdd:COG4372 82 QLRALRTELGTAQGEKRAAETEREAARSELQKarqEREAVRQELAAARQNLAKAQQELARLTKQAQDLQTRLKTLAEQRR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1043 EEEEKVKSLSKLRNKYEAVMADMEDRlkkeekgRQELEKLKRKLDGEAGDLQEQVAELQQQLEEL------RQALARKEA 1116
Cdd:COG4372 162 QLEAQAQSLQASQKQLQASATQLKSQ-------VLDLKLRSAQIEQEAQNLATRANAAQARTEELarraaaAQQTAQAIQ 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1117 ELQAALARVEDEAAQKNAVLKSlRELQAQLAELQEDMESEKLARAKAEKQ 1166
Cdd:COG4372 235 QRDAQISQKAQQIAARAEQIRE-RERQLQRLETAQARLEQEVAQLEAYYQ 283
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1077-1303 |
1.78e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.91 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1077 QELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQAALARVEDEAAQKNAvlkslrELQAQLAELQEDMESE 1156
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQA------EQAAKQAEEKQKQAEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1157 KLARAKAEKQRRdlgEELEALKTELEDtldstAAQQELRSKREQEVTELKKTIEEEVKVHEAQvldmrqrhTSALEELSE 1236
Cdd:TIGR02794 124 AKAKQAAEAKAK---AEAEAERKAKEE-----AAKQAEEEAKAKAAAEAKKKAEEAKKKAEAE--------AKAKAEAEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033370542 1237 QLEQsrrfKINLEKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGERAKAE 1303
Cdd:TIGR02794 188 KAKA----EEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQG 250
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ... |
884-1471 |
1.83e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 225638 [Multi-domain] Cd Length: 1480 Bit Score: 43.34 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 884 AVELQKVQEKHTKTQMDLKELENKYQQLSEEKTILAEQLQAETELFaEAEEmrarLAARKQELEDILHELESRVEEEEER 963
Cdd:COG3096 505 GPDQRHLAEQVQPLRMRLSELEQRLRQQQSAERLLADFCKRQGKNL-DAEE----LEALHQELEALIESLSDSVSNAREQ 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 964 CQQLQGDKKKMQQHVQDLEEQLEEEEAARQKL-QLEKVSTEAklkkMEEDLLVLEDQNSKLHKERKLMEER--LSEFTSH 1040
Cdd:COG3096 580 RMALRQEQEQLQSRIQSLMQRAPVWLAAQNALeQLSEQSGEE----FTDSQDVTEYMQQLLEREREATVERdeLGARKNA 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1041 MAEEEEKVKS--------LSKLRNKYEAVM-ADMEDRLKKEEK-------GRQELEKLKRKLDGeagdlqeqVAELQQQL 1104
Cdd:COG3096 656 LDEEIERLSQpggsedqrLNALAERFGGVLlSEIYDDVTIEDApyfsalyGPSRHAIVVPDLSQ--------VKEHLEGL 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1105 EELRQALARKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQEdmeSEKLARAKAEKQrrdlgeeLEALKTELEDT 1184
Cdd:COG3096 728 TDCPEDLYLIEGDPQSFDDSVFSVDELEKAVVVKIADRQWRYSRFPE---IPLFGRAAREQR-------LESLHAERDVL 797
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1185 ldstAAQQELRSKREQEVTELKKTIEEEVKVH---------EAQVLDMRQRHTSALEELSEQLEQSRRFKINLEKTKQAL 1255
Cdd:COG3096 798 ----SERHATLSFDVQKTQRLHQAFSRFIGSHlavafeadpEAEIRQLNSRRNELERALSNHENDNQQQRIQFDQAKEGV 873
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1256 EGENaemqkevKLLQAAKLESEQrrkKLEGQVQELQLRAGEGERAKAELVERLVKLqNELDGVSGTLGSTESKTIKLAKD 1335
Cdd:COG3096 874 TALN-------RLIPQLNLLADE---SLADRVEEIRERLDEAQEAARFIQQHGNTL-SKLEPIASVLQSDPEQFEQLKED 942
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1336 LATVESHLQDTQ----------------------ELLQEETRQKLNLSSRVRQLEEEKAAMLEQLEEEEAAKANFSRQMQ 1393
Cdd:COG3096 943 YAQAQQMQRQARqqafaltevvqrrahfsysdsaEMLSENSDLNEKLRQRLEQAEAERTRAREQLRQHQAQLSQYNQVLA 1022
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1394 SLQQQVMETKKKLEE------DAGV---AEAIEEARRRAAKDLESLSVRYEERVQacdkLEKGRTRLQQELDDVTVAL-- 1462
Cdd:COG3096 1023 SLKSSYDTKKELLNElqqelqDIGVradSGAEERARIRRDELHAQLSTNRSRRNQ----LEKQLTFCEAEMDNLTRKLrk 1098
|
650
....*....|....*
gi 1033370542 1463 ------DQQRQVVSA 1471
Cdd:COG3096 1099 lerdyfEMREQVVTA 1113
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
990-1242 |
1.92e-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: 435008 [Multi-domain] Cd Length: 329 Bit Score: 42.50 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 990 AARQKLQLEKVSTEAKLKKMEeDLLVLEDQNSKLHKERKLMEERLSEFTSHMAEEEEKVKSLSKLRNKYEAVMADMEDRL 1069
Cdd:pfam15905 53 ARKVKSLELKKKSQKDLKESK-DQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1070 ------------KKEEKGRQ--------ELEKLKRKLDG---EAGDLQEQVAELQQQLEELRQALARKEAELQAALARVE 1126
Cdd:pfam15905 132 leltrvnellkaKFSEDGTQkkmsslsmELMKLRNKLEAkmkEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1127 DEAAQKNAVLKSLRELQAQLAELQEDMESEKLARAKAEKQRRDLGEELEALKTELEdtldstaAQQELRSKREQEVTELK 1206
Cdd:pfam15905 212 KEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLE-------EKEQELSKQIKDLNEKC 284
|
250 260 270
....*....|....*....|....*....|....*.
gi 1033370542 1207 KTIEEEVKVHEAQVLDMRQRHTSALEELSEQLEQSR 1242
Cdd:pfam15905 285 KLLESEKEELLREYEEKEQTLNAELEELKEKLTLEE 320
|
|
| ERM |
pfam00769 |
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ... |
1555-1693 |
2.33e-03 |
|
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.
Pssm-ID: 425860 [Multi-domain] Cd Length: 247 Bit Score: 41.85 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1555 ELERFKRALEQQVQEMRAQMEELEDELQATEDGKLRLEvnMQALKAQHERElqnrddanddkkkLLSKQVRELEAELDAE 1634
Cdd:pfam00769 3 EAEREKQELEERLKQYEEETRKAQEELEESEETAELLE--EKLRVAEEEAE-------------LLEQKAQEAEEEKERL 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1033370542 1635 RKQRAQALAGRKKLELDLQEAMAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEARAA 1693
Cdd:pfam00769 68 EESAEMEAEEKEQLERELREAQEEVARLEEESERKEEEAERLQEELEEAREEEEEAKEK 126
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1270-1484 |
2.35e-03 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 42.70 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1270 QAAKLESEQRRKKLEGQVQELQLRAGEGERAKAElvERLVKLQNELDGVSGTLGSTESKTIKLAKDLATVESHLQDTQEL 1349
Cdd:COG4372 75 QLDDIRPQLRALRTELGTAQGEKRAAETEREAAR--SELQKARQEREAVRQELAAARQNLAKAQQELARLTKQAQDLQTR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1350 LQeetrqklNLSSRVRQLEEEKAAMLeqleeeeaakaNFSRQMQSLQQQVMETKKKLEEDAGVAEAIEEARRRAAKDLES 1429
Cdd:COG4372 153 LK-------TLAEQRRQLEAQAQSLQ-----------ASQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLATRANAAQA 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1033370542 1430 LSVRYEERVQACDKLEKGRTRLQQELDDVTVALDQQRQVVSALEKKQKKFDQMLA 1484
Cdd:COG4372 215 RTEELARRAAAAQQTAQAIQQRDAQISQKAQQIAARAEQIRERERQLQRLETAQA 269
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
993-1187 |
2.40e-03 |
|
Caldesmon;
Pssm-ID: 426572 [Multi-domain] Cd Length: 490 Bit Score: 42.55 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 993 QKLQLEKVSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEERLSEFTSHMAEEEEKVKSLSKLRNKYEAVMADMEDRLKKE 1072
Cdd:pfam02029 140 EKDDKKAVPKEEEEEEDAKTEEEEEEEEEEKKVSKKKKEKLKDEYTSKVFLDQKKGHPEQKSQNGALEEVTSMTVKLKRT 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1073 EK-GRQELEKLKRKLDGEAgdlqeqVAELQQQLEELRQALARKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQE 1151
Cdd:pfam02029 220 ERtFSQKSLVAEDEEEGAA------FLEAEQKLEELRRRRQEKESQEFEKLRQKQQEAELELEELKKKREERRKILEEEE 293
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1033370542 1152 DM--ESEKLARAKAEKQRRDLGEELEALKTE-------LEDTLDS 1187
Cdd:pfam02029 294 QRrkQEEAERKAREEEEKRRMKEEIERRRAEaaekrqkMEDTSSA 338
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
901-1670 |
2.60e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.87 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 901 LKELENKYQQLS-EEKTILAEQLQAE---------TELFAEAEEMRARLAARKQELEDilhelesrveeeeercqqlqgd 970
Cdd:PRK10246 218 VQSLTASLQVLTdEEKQLLTAQQQQQqslnwltrlDELQQEASRRQQALQQALAAEEK---------------------- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 971 kkkmqqhvqdleeqleeeeAARQKLQLEKVSTEAKLKKMEEDllvLEDQNSKLHKERKLMEERLSEFTSHMAEEEEKVKS 1050
Cdd:PRK10246 276 -------------------AQPQLAALSLAQPARQLRPHWER---IQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHH 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1051 LSKLRNKYEAVMADMEDRLKKEEKGR---QELEKLKRKLDGEAGDlQEQVAELQQQLEELRQALArkeAELQAALARVED 1127
Cdd:PRK10246 334 AAKQSAELQAQQQSLNTWLAEHDRFRqwnNELAGWRAQFSQQTSD-REQLRQWQQQLTHAEQKLN---ALPAITLTLTAD 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1128 EAAQKNAVLKSLRELQAQLAELQEDMeseklarAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVTELKK 1207
Cdd:PRK10246 410 EVAAALAQHAEQRPLRQRLVALHGQI-------VPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKT 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1208 TIEEEVKVHEaqvldmrqrhtsaLEELSEQLEQSRRFKINLEKTKQALEGENAeMQKEVKLLQAAKLESEQRRKKLE--- 1284
Cdd:PRK10246 483 ICEQEARIKD-------------LEAQRAQLQAGQPCPLCGSTSHPAVEAYQA-LEPGVNQSRLDALEKEVKKLGEEgaa 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1285 --GQVQELQLRAGEGERAKAELVERLVKLQNELDGVSGTLGSTESKTIKLAKDLATVESHLQDTQELlqeetRQKLNLSS 1362
Cdd:PRK10246 549 lrGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLRLL-----SQRHELQG 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1363 rvrQLEEEKAAMLEQLEEEEAAKANFSRQMQSLQQQVMETKkklEEDAGVAEAIEEARRRAAKDLESLSVRyeERVQACD 1442
Cdd:PRK10246 624 ---QIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQED---EEASWLATRQQEAQSWQQRQNELTALQ--NRIQQLT 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1443 K-LEKGRTRLQQELDDVTVALDQQRQVVS---ALEKKQKKFDQMLAEEKlisARYAEerdraeadAREKETKVLSLSRal 1518
Cdd:PRK10246 696 PlLETLPQSDDLPHSEETVALDNWRQVHEqclSLHSQLQTLQQQDVLEA---QRLQK--------AQAQFDTALQASV-- 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1519 eealetreeMERQNKQLRAEMDDlvsskddvgKNVHELERFKRALEQQVQEMRAQMEE----LEDELQATEDGkLRLEVN 1594
Cdd:PRK10246 763 ---------FDDQQAFLAALLDE---------ETLTQLEQLKQNLENQRQQAQTLVTQtaqaLAQHQQHRPDG-LDLTVT 823
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033370542 1595 MQALKAQ-HERELQNRDdaNDDKKKLLSKQVREleaelDAERKQRAQALagrkkleldlqeaMAQLDAANKGRDEAG 1670
Cdd:PRK10246 824 VEQIQQElAQLAQQLRE--NTTRQGEIRQQLKQ-----DADNRQQQQAL-------------MQQIAQATQQVEDWG 880
|
|
| COG1579 |
COG1579 |
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ... |
1483-1640 |
2.74e-03 |
|
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function prediction only];
Pssm-ID: 224495 [Multi-domain] Cd Length: 239 Bit Score: 41.58 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1483 LAEEKLISARYAEERDRAEADAREKETKVLSLSRALEEALETREEMERQNKQLRAEMDDLVSSKDDVGKNVHEL--ERFK 1560
Cdd:COG1579 12 IQKLDLEKDRLEPRIKEIRKALKKAKAELEALNKALEALEIELEDLENQVSQLESEIQEIRERIKRAEEKLSAVkdEREL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1561 RALEQQVQEMRAQMEELEDELQATEDGKLRLEVNMQALKAQHERELQNRDDAnddkKKLLSKQVRELEAELDAERKQRAQ 1640
Cdd:COG1579 92 RALNIEIQIAKERINSLEDELAELMEEIEKLEKEIEDLKERLERLEKNLAEA----EARLEEEVAEIREEGQELSSKREE 167
|
|
| YloA |
COG1293 |
Predicted component of the ribosome quality control (RQC) complex, YloA/Tae2 family, contains ... |
1003-1165 |
2.78e-03 |
|
Predicted component of the ribosome quality control (RQC) complex, YloA/Tae2 family, contains fibronectin-binding (FbpA) and DUF814 domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 224212 [Multi-domain] Cd Length: 564 Bit Score: 42.38 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1003 EAKLKKMEEDLLVLEDQNSKLHKERKLMEERLSEFTSHMAEEEEKVKSLSKLRNKYEAVMADMEDRLKKEEKGRQELEKL 1082
Cdd:COG1293 292 EKELKKLENKLEKQEDELEELEKAAEELRQKGELLYANLQLIEEGLKSVRLADFYGNEEIKIELDKSKTPSENAQRYFKK 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1083 KRKLDGEAGDLQEQVAELQQQLEELRQALarkeaelqaalarvedEAAQKNAVLKSLRELQAQLAELQEdMESEKLARAK 1162
Cdd:COG1293 372 YKKLKGAKVNLDRQLSELKEAIAYYESAK----------------TALEKAEGKKAIEEIREELIEEGL-LKSKKKKRKK 434
|
...
gi 1033370542 1163 AEK 1165
Cdd:COG1293 435 KEW 437
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1057-1226 |
2.83e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1057 KYEAVMADMEDRL----KKEEKGRQELEKLKRKLDGEAG---------DLQEQVAELQQQLEELRQALA----------- 1112
Cdd:PRK11281 77 RQKEETEQLKQQLaqapAKLRQAQAELEALKDDNDEETRetlstlslrQLESRLAQTLDQLQNAQNDLAeynsqlvslqt 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1113 ---RKEAELQAALARVEdeaaQKNAVLKSLRELQAQL-AELQEDMESE-KLARAKAEKQRRDLgeeleALKTELEDTLDS 1187
Cdd:PRK11281 157 qpeRAQAALYANSQRLQ----QIRNLLKGGKVGGKALrPSQRVLLQAEqALLNAQNDLQRKSL-----EGNTQLQDLLQK 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1033370542 1188 -----TAAQQELRSKRE--QEVTELKKTIEEEVKVHEAQVLDMRQR 1226
Cdd:PRK11281 228 qrdylTARIQRLEHQLQllQEAINSKRLTLSEKTVQEAQSQDEAAR 273
|
|
| RmuC |
COG1322 |
DNA anti-recombination protein (rearrangement mutator) RmuC [Replication, recombination and ... |
1116-1294 |
2.84e-03 |
|
DNA anti-recombination protein (rearrangement mutator) RmuC [Replication, recombination and repair];
Pssm-ID: 224241 [Multi-domain] Cd Length: 448 Bit Score: 42.38 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1116 AELQAALARVEDEAAQKNAVLKSLRELQAQLAELQEDMESEKLARAKAEKQRRdLGEELEALKTELEDTLDSTAAQQEL- 1194
Cdd:COG1322 18 AFIRQLLLRLGRLEQMLGELAAVLEQLLLLLAFRAEAEQLRTFARSLQALNLE-LIQELNELKARLQQQLLQSREQLQLl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1195 ---RSKREQEVTELKKTIEEEV--KVHE------AQVLDMRQRHTSALEELSEQL--EQSRRFKINLEKTKQALeGENAE 1261
Cdd:COG1322 97 iesLAQLSSEFQELANEIFEELnrRLAElnqqnlKQLLKPLREVLEKFREQLEQRihESAEERSTLLEEIDRLL-GEIQQ 175
|
170 180 190
....*....|....*....|....*....|...
gi 1033370542 1262 MQKEVKLLQAAkleseQRRKKLEGQVQELQLRA 1294
Cdd:COG1322 176 LAQEAGNLTAA-----LKGNKTRGNWGEVQLER 203
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1077-1173 |
2.89e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 430106 [Multi-domain] Cd Length: 176 Bit Score: 40.68 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1077 QELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAEL---QAALARVEDEAAQKNAVLKS----LRELQAQLAEL 1149
Cdd:pfam08614 53 QSLEQLLAQLREELAELYRSRGELAQQLVDLNEELQELEKKLredERRLAELEAERAQLEEKLRDreeeLREKRKLNQDL 132
|
90 100
....*....|....*....|....
gi 1033370542 1150 QEDMESEKLARAKAEKQRRDLGEE 1173
Cdd:pfam08614 133 QDELVALQLQLNMAEEKLRKLEKE 156
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1167-1308 |
2.93e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1167 RRDLGEELEALKTELEDTLDstAAQQELRSKREQEVTELKKTIEEEVKVHEAQVLDMRqrhtsalEELSEQLEQSRRFKI 1246
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERR-------NELQKLEKRLLQKEE 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033370542 1247 NLEKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLEG----QVQELQLRAG-EGERAKAELVERL 1308
Cdd:PRK12704 97 NLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEElieeQLQELERISGlTAEEAKEILLEKV 163
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
1067-1319 |
2.94e-03 |
|
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.
Pssm-ID: 434726 [Multi-domain] Cd Length: 520 Bit Score: 42.53 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1067 DRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQAALARVEDEAAQK----NAVLKSLreL 1142
Cdd:pfam15450 115 ERKGAEQEANLRLTKLTGMLKQEEQGREAACSALQKSQEEASQKVDHEVARMQAQVTKLGEEMSLRflkrEAKLCSF--L 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1143 QAQLAELQEDMESEKLARAKAEKQRRdlgEELEALKTELEDTLDSTAaqQELRSKREQEVTELKktiEEEVKVHEAQVld 1222
Cdd:pfam15450 193 QKSFLALEKRMKASESTRLKAESSLR---EELEGKWQKLQELTEERL--RALTGQLEQEEGHLL---EQCRGLDEAVV-- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1223 mrqRHTSALEELSEQLEQSRRFKINLEKTKQALEGENAE-----MQKEvklLQAAKLESEQRRKKLEGQVQELQLRAGEG 1297
Cdd:pfam15450 263 ---QLTKFVRQNQVSLNRVLLAEQKARDAKGQLEESRAGelasyMQES---LEAMQLAGDLARRETQAALELLQEKSQVL 336
|
250 260
....*....|....*....|..
gi 1033370542 1298 ERAKAELVERLVKLQNELDGVS 1319
Cdd:pfam15450 337 EHSVAELVTQLKDLSDHFLALS 358
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1553-1941 |
3.04e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 428594 [Multi-domain] Cd Length: 562 Bit Score: 42.32 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1553 VHELERfKRALEQQVQEMRAQMEELEDELQATEDGKlrlevnMQALKaqherELQNRDDANDDKKKLLSK-QVRELEAEL 1631
Cdd:pfam05701 31 IQTVER-RKLVELELEKVQEEIPEYKKQSEAAEAAK------AQVLE-----ELESTKRLIEELKLNLERaQTEEAQAKQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1632 DAERKQ-RAQALAGRKKLELDLqEAMAQLDAANKGRDEAGKQLRKLQAQMKELWRE----VEEARAAR---EEIFIQSRE 1703
Cdd:pfam05701 99 DSELAKlRVEEMEQGIADEASV-AAKAQLEVAKARHAAAVAELKSVKEELESLRKEyaslVSERDIAIkraEEAVSASKE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1704 SEKKLKNLEAELLQLQEDLAASERAKRQAQQERDDLA-----DELANGNSGKSAlLDEKRHLEARIGQLEEELDEEQSNM 1778
Cdd:pfam05701 178 IEKTVEELTIELIATKESLESAHAAHLEAEEHRIGAAlareqDKLNWEKELKQA-EEELQRLNQQLLSAKDLKSKLETAS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1779 ELLNDRYRKLSMQVETLTTELGAERSFSQKTEN--------ARQQLERQNKDL-RAK-----LGEMDSSVKS---KYKMA 1841
Cdd:pfam05701 257 ALLLDLKAELAAYMESKLKEEADGEGNEKKTSTsiqaalasAKKELEEVKANIeKAKdevncLRVAAASLRSeleKEKAE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1842 IATLESK-------VAQLEEQLEQESRERILSGKLVRRAEKKLKEVILQVDEERRNADQYKDQVEKGHLRLKQLKRQLEE 1914
Cdd:pfam05701 337 LASLRQRegmasiaVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQ 416
|
410 420
....*....|....*....|....*..
gi 1033370542 1915 AEEEASRANASRRRMQRELEDVTESAE 1941
Cdd:pfam05701 417 AKAAASTVESRLEAVLKEIEAAKASEK 443
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1600-1938 |
3.06e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1600 AQHERELQNRDDANDDKKKLLSKQVRELEAE---LDAERKQRAQALAGRKKLELDLQEAMAQLDAANKGRDEAGKqLRKL 1676
Cdd:PRK04863 275 MRHANERRVHLEEALELRRELYTSRRQLAAEqyrLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEK-IERY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1677 QAQMKELWREVEEARAAREEIFIQSRESEKKLKNLEAELLQLQEDLAASERA----------KRQAQQerddlADELANG 1746
Cdd:PRK04863 354 QADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQAldvqqtraiqYQQAVQ-----ALERAKQ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1747 NSGKSALLDEKrhlearigqleeeldeeqsnmelLNDRYRKLSMQVETLTTELgaeRSFSQK---TENARQQLERQNKDL 1823
Cdd:PRK04863 429 LCGLPDLTADN-----------------------AEDWLEEFQAKEQEATEEL---LSLEQKlsvAQAAHSQFEQAYQLV 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1824 RAKLGEMDSSV-KSKYKMAIATLESKVAQLE--EQLEQESRERILSGKLVRRAEKKLKEVILQVDEERRNADQYKDQVEk 1900
Cdd:PRK04863 483 RKIAGEVSRSEaWDVARELLRRLREQRHLAEqlQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQE- 561
|
330 340 350
....*....|....*....|....*....|....*...
gi 1033370542 1901 ghlrlkQLKRQLEEAEEEASRANASRRRMQRELEDVTE 1938
Cdd:PRK04863 562 ------ELEARLESLSESVSEARERRMALRQQLEQLQA 593
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1807-1963 |
3.08e-03 |
|
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: 42.75 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1807 QKTENARQQLERQnKDLRAKLGEMDSSVKSKYKMA----IATLESKVAQLEEQLEQESRERILSGKLVRRAEKKLKEVIL 1882
Cdd:TIGR02169 201 ERLRREREKAERY-QALLKEKREYEGYELLKEKEAlerqKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1883 QVDEERRN-ADQYKDQVEKGHLRLKQLKR-------QLEEAEEEASRANASRRRMQRELEDVTESAESMNREVTSLRNRL 1954
Cdd:TIGR02169 280 KIKDLGEEeQLRVKEKIGELEAEIASLERsiaekerELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY 359
|
....*....
gi 1033370542 1955 SKVERRQRK 1963
Cdd:TIGR02169 360 AELKEELED 368
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1628-2014 |
3.09e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.42 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1628 EAELDAERKQRAQALAGRKKLEldlqeamaqldAANKGRDEAGKQLRKLQAQMKELWREVEearaaREEIFIQSRESEKK 1707
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLE-----------EAEKARQAEMDRQAAIYAEQERMAMERE-----RELERIRQEERKRE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1708 LKNLEAELLQLQ-EDLAASERAKRQAQQERDDLADELANGNsgKSALLDEKRhlEARIGQLEEELDEEQSNMEllNDRYR 1786
Cdd:pfam17380 362 LERIRQEEIAMEiSRMRELERLQMERQQKNERVRQELEAAR--KVKILEEER--QRKIQQQKVEMEQIRAEQE--EARQR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1787 KLSMQVETLTTELGAERSFSQKTENARQQLERQNKDLRAKLGEMDSSvkskykmaiatleskvaQLEEQLEQESRERILs 1866
Cdd:pfam17380 436 EVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKE-----------------KRDRKRAEEQRRKIL- 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1867 gklvrraEKKLKEVILQVDEERRNADQYKDQVEKghlrlkqlkRQLEEAEEEASRANASRRRMQRELEDVTESAESMnRE 1946
Cdd:pfam17380 498 -------EKELEERKQAMIEEERKRKLLEKEMEE---------RQKAIYEEERRREAEEERRKQQEMEERRRIQEQM-RK 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1947 VTSLRNRLSKVER------------RQRKRTPLSFTTRTVRQVFRLDgvsDEETEDPESDSPSTNHKPLTPSQGPPQPAT 2014
Cdd:pfam17380 561 ATEERSRLEAMEReremmrqiveseKARAEYEATTPITTIKPIYRPR---ISEYQPPDVESHMIRFTTQSPEWATPSPAT 637
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1085-1308 |
3.35e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.13 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1085 KLDGEAGDLQEQVAELQQQLEELRqaLARKEAELQAALARVED-------EAAQKNAVLKSLRELQAQLAELQEDME--S 1155
Cdd:PRK04778 253 DIEKEIQDLKEQIDENLALLEELD--LDEAEEKNEEIQERIDQlydilerEVKARKYVEKNSDTLPDFLEHAKEQNKelK 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1156 EKLAR--------AKAEKQRRDLGEELEALKTELEDTLDSTAAQQ----ELRSKREQEVTELKKTIEEEVKVHEAqVLDM 1223
Cdd:PRK04778 331 EEIDRvkqsytlnESELESVRQLEKQLESLEKQYDEITERIAEQEiaysELQEELEEILKQLEEIEKEQEKLSEM-LQGL 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1224 RQRHTSA---LEELSEQLEQSRRF--KINL----EKTKQALEGENAEMQKEVKLLQAAKLESEQRRKKLE---GQVQELQ 1291
Cdd:PRK04778 410 RKDELEArekLERYRNKLHEIKRYleKSNLpglpEDYLEMFFEVSDEIEALAEELEEKPINMEAVNRLLEeatEDVETLE 489
|
250
....*....|....*..
gi 1033370542 1292 LRAGEgERAKAELVERL 1308
Cdd:PRK04778 490 EETEE-LVENATLTEQL 505
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1026-1178 |
3.66e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1026 ERKLMEERLSEFTSHMAEEEEKVKSLSKLRNKYEavmadMEDRLKKEEKGRqELEKLKRK---LDGEAGDLqeqvAELQQ 1102
Cdd:PRK12705 36 ERILQEAQKEAEEKLEAALLEAKELLLRERNQQR-----QEARREREELQR-EEERLVQKeeqLDARAEKL----DNLEN 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1033370542 1103 QLEELRQALARKEAELQAALARVEDEAAQKnAVLKSLRELQAQLAELQEDMESEKLARAKAEKQRRDLGEELEALK 1178
Cdd:PRK12705 106 QLEEREKALSARELELEELEKQLDNELYRV-AGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQN 180
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1561-1760 |
3.67e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1561 RALEQQVQEMRAQMEELEDELQATEDgklrLEVNMQALKAQHERELQNRDDANDDKKKLLSKQVRELEAEL---DAERKQ 1637
Cdd:PHA02562 177 RELNQQIQTLDMKIDHIQQQIKTYNK----NIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELlnlVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1638 RAQALAGRKKLELDLQEAMAQLDAANK-------------GRDEAGKQLRKLQAQMKELWREVEEARAAREE---IFIQS 1701
Cdd:PHA02562 253 PSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDEleeIMDEF 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1033370542 1702 RESEKKLKNLEAELLQLQEDLAASERAKRQAQQERDDLADELANGNSGKSALLDEKRHL 1760
Cdd:PHA02562 333 NEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1475-1638 |
3.69e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1475 KQKKFDQMLAEEKLISARYAEERDRAEADAREKETKVLSLSRALEEALETREEMERQNKQLRAEMDDLVSSKDDVGKNVH 1554
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1555 ELERFKRALEQQVQEMRAQMEELEDELQatEDGKLRLEVNMQALKAQHERELqnrddaNDDKKKLLSKQvrELEAELDAE 1634
Cdd:PRK12705 106 QLEEREKALSARELELEELEKQLDNELY--RVAGLTPEQARKLLLKLLDAEL------EEEKAQRVKKI--EEEADLEAE 175
|
....
gi 1033370542 1635 RKQR 1638
Cdd:PRK12705 176 RKAQ 179
|
|
| MscK |
COG3264 |
Small-conductance mechanosensitive channel [Cell wall/membrane/envelope biogenesis]; |
1107-1280 |
3.73e-03 |
|
Small-conductance mechanosensitive channel [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225803 [Multi-domain] Cd Length: 835 Bit Score: 42.37 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1107 LRQALARKEAELqaalarVEDEAAQKNAVLKSLRELQAQL-AELQEDMESEKLARAKAEKQRRDLGEELEALKTELEDTL 1185
Cdd:COG3264 8 VLQELLQSRREL------LTAESAQLEAALQLLQEAVNSKrQEEAEPAAEEAELQAELIQQELAINDQLSQALNQQTERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1186 DSTAAQQELRSKREQEVTELKKTIEEEVKVHEAQVLDMRQRHTsALEELSEQLEQSRRFKINLEktKQALEGENAEMQKE 1265
Cdd:COG3264 82 NALASDDRQLANLLLQLLQSSRTIREQIAVLRGSLLLSRILLQ-QLGPLPEAGQPQEQFEVTQE--RDALQAEKAYINAL 158
|
170
....*....|....*
gi 1033370542 1266 VKllQAAKLESEQRR 1280
Cdd:COG3264 159 EG--QAEQLTAEVRD 171
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
1122-1647 |
3.88e-03 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227596 [Multi-domain] Cd Length: 4600 Bit Score: 42.68 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1122 LARVEDEAAQKNAVLKSLRELQAQLAELQEDMESEKLARAKAEKQRRDLGEELEALKTELEDTLDstaaQQELRSKREQE 1201
Cdd:COG5271 3840 LANEEDTANQSDLDESEARELESDMNGVTKDSVVSENENSDSEEENQDLDEEVNDIPEDLSNSLN----EKLWDEPNEED 3915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1202 VTELKKTIEEEVKVHEAQVLDMRQRHTSALEELSEQLEQsrrfkinlektkqalegENAEMQKEVkllqaakleseqrrk 1281
Cdd:COG5271 3916 LLETEQKSNEQSAANNESDLVSKEDDNKALEDKDRQEKE-----------------DEEEMSDDV--------------- 3963
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1282 kleGQVQELQLRAGEGERAKAelverlvklqneldgvsgtlgsTESKTIKLAKDLATVESHlqdtqellqEETRQKLNLS 1361
Cdd:COG5271 3964 ---GIDDEIQPDIQENNSQPP----------------------PENEDLDLPEDLKLDEKE---------GDVSKDSDLE 4009
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1362 SrvrqleeekaaMLEQLEEEEAAKANFSRQMQSLQQQVMETKKKLEEDAGVAEAIEEARRRAAKDLESlsvrYEERVQAC 1441
Cdd:COG5271 4010 D-----------MDMEAADENKEEADAEKDEPMQDEDPLEENNTLDEDIQQDDFSDLAEDDEKMNEDG----FEENVQEN 4074
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1442 DKLEKGRTRLQQELDDVTVALDQqrqvvsALEKKQKkfdqMLAEEKLISARYAEERDRAEADAREKETKVLSLSRALEEA 1521
Cdd:COG5271 4075 EESTEDGVKSDEELEQGEVPEDQ------AIDNHPK----MDAKSTFASAEADEENTDKGIVGENEELGEEDGVRGNGTA 4144
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1522 LETREEMER---QNKQLRAEMDDLVSSKDDVGKNVHELERFKRAleQQVQEMRAQMEELEDELQATEDGklrlEVNMQAL 1598
Cdd:COG5271 4145 DGEFEQVQEdtsTPKEAMSEADRQYQSLGDHLREWQQANRIHEW--EDLTESQSQAFDDSEFMHVKEDE----EEDLQAL 4218
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1033370542 1599 KAQHERELQNRDD---ANDDKKKLLSKQVRELEA-ELDAERKQRAQALAGRKK 1647
Cdd:COG5271 4219 GNAEKDQIKSIDRdesANQNPDSMNSTNIAEDEAdEVGDKQLQDGQDISDIKQ 4271
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
898-1168 |
3.92e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 224259 [Multi-domain] Cd Length: 294 Bit Score: 41.59 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 898 QMDLKELENKYQQLSEEktiLAEQLQAETELFAEAEEMRAR---LAARKQELEDILHELESRVEEEEERCQQLQGDKKKM 974
Cdd:COG1340 5 LDKLDELELKRKQLKEE---IEELKEKRDELRKEASELAEKrdeLNAKVRELREKAQELREERDEINEEVQELKEKRDEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 975 QQHVQDLEEQLEEEEAARQKLQLEKVSTEAKLKKMEEdlLVLEDQNSKLHKERklmEERLSEFTSHMAEEEEKVKSLSKL 1054
Cdd:COG1340 82 NAKLQELRKEYRELKEKRNEFNLGGRSIKSLEREIER--LEKKQQTSVLTPEE---ERELVQKIKELRKELEDAKKALEE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1055 RNKYEAVMADMEDRLKKEEKGRQELEKLKRkldgEAGDLQEQVAELQQQLEELRQALARKEAELQAALARVEDEAAQKNA 1134
Cdd:COG1340 157 NEKLKELKAEIDELKKKAREIHEKIQELAN----EAQEYHEEMIKLFEEADELRKEADELHEEFVELSKKIDELHEEFRN 232
|
250 260 270
....*....|....*....|....*....|....
gi 1033370542 1135 VLKSLRELQAQLAELQEDMESEKLARAKAEKQRR 1168
Cdd:COG1340 233 LQNELRELEKKIKALRAKEKAAKRREKREELKER 266
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1068-1163 |
3.99e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.31 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1068 RLKKEEKGRQELEKLKRKLDGEAG-----DLQEQVAELQQQLEELRQALARKEA-------ELQAALARVEDEAAQKNAV 1135
Cdd:PTZ00491 674 LLEQEARGRLERQKMHDKAKAEEQrtkllELQAESAAVESSGQSRAEALAEAEArlieaeaEVEQAELRAKALRIEAEAE 753
|
90 100
....*....|....*....|....*...
gi 1033370542 1136 LKSLRELQAQLAELQEDMESEKLARAKA 1163
Cdd:PTZ00491 754 LEKLRKRQELELEYEQAQNELEIAKAKE 781
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
1544-1699 |
4.01e-03 |
|
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.
Pssm-ID: 434695 [Multi-domain] Cd Length: 258 Bit Score: 41.09 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1544 SSKDDVGKNVHELERFKRALEQQVQEMRAQMEELEDELQATEDgklrlEVN-----------MQALK-AQHERELQNRDD 1611
Cdd:pfam15397 60 SNKKQLQQAKAELQEWEEKEESKLNKLEQQLEQLNAKIQKTQE-----ELNflstykdkeypVKAVQiANLVRQLQQLKD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1612 AN----DDKKKLLSKQVRELEAELDAERKQRAQALA---------GRKKLELDLQEAMAQLDAANKGRDEAGKQLRKLQA 1678
Cdd:pfam15397 135 SQqdelDELEEMRREVLESLSRKIQKKKEKILSSLAektqspyqeSLLQKTRDNQVMLKEIEQFREFIDELEEEIPKLKA 214
|
170 180
....*....|....*....|.
gi 1033370542 1679 QMKELWREVEEaraAREEIFI 1699
Cdd:pfam15397 215 EVQQLQAQRQE---PREIIFA 232
|
|
| PRK10920 |
PRK10920 |
putative uroporphyrinogen III C-methyltransferase; Provisional |
1093-1161 |
4.14e-03 |
|
putative uroporphyrinogen III C-methyltransferase; Provisional
Pssm-ID: 236795 Cd Length: 390 Bit Score: 41.62 E-value: 4.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033370542 1093 LQEQVAELQQQLEELRQALARKEAELQAALarveDEAAQKNAVL-KSLRELQAQLAELQ-EDMESEKLARA 1161
Cdd:PRK10920 72 LANQLTALQKAQESQKQELEGILKQQAKAL----DQANRQQAALaKQLDELQQKVATISgSDAKTWLLAQA 138
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
1042-1156 |
4.20e-03 |
|
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.
Pssm-ID: 428166 [Multi-domain] Cd Length: 124 Bit Score: 39.32 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1042 AEEEEKVKSLSKLRNKYEAVMADMEDRLKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQAA 1121
Cdd:pfam04871 4 SELESEAASLKDENTELKAELQALSDQYQSLEQKKKAAESQAKELEAENKKLEEELKKLRAELSEEKQKEKEKQSELEDL 83
|
90 100 110
....*....|....*....|....*....|....*
gi 1033370542 1122 LARVEDEAAQKNAVLKSLRELQAQLAELQEDMESE 1156
Cdd:pfam04871 84 LLLLGDLEEKVEKYKARLKELGEEVSDDEDDDEDD 118
|
|
| F-BAR_CIP4-like |
cd07653 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 ... |
1185-1314 |
4.30e-03 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Cdc42-Interacting Protein 4 (CIP4), Formin Binding Protein 17 (FBP17), FormiN Binding Protein 1-Like (FNBP1L), and similar proteins. CIP4 and FNBP1L are Cdc42 effectors that bind Wiskott-Aldrich syndrome protein (WASP) and function in endocytosis. CIP4 and FBP17 bind to the Fas ligand and may be implicated in the inflammatory response. CIP4 may also play a role in phagocytosis. Members of this subfamily typically contain an N-terminal F-BAR domain and a C-terminal SH3 domain. In addition, some members such as FNBP1L contain a central Cdc42-binding HR1 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153337 [Multi-domain] Cd Length: 251 Bit Score: 41.08 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1185 LDSTAAQQELRSK--REQEVTELKKTIEEevkvHEAQvldmRQRHTSALEELSEQLEQSRRfkiNLEKTKQALEGENAEM 1262
Cdd:cd07653 74 VNDIAGQHELIAEnlNSNVCKELKTLISE----LRQE----RKKHLSEGSKLQQKLESSIK---QLEKSKKAYEKAFKEA 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1033370542 1263 QKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGERAKAELVERLVKLQNE 1314
Cdd:cd07653 143 EKAKQKYEKADADMNLTKADVEKAKANANLKTQAAEEAKNEYAAQLQKFNKE 194
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1063-1214 |
4.64e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1063 ADMEDRLKKEEK---GRQELEKLKRKLDGEagdLQEQVAELQQQLEELRQalarKEAELQAALARVEDEAAQKNAVLKSL 1139
Cdd:PRK12704 47 AKKEAEAIKKEAlleAKEEIHKLRNEFEKE---LRERRNELQKLEKRLLQ----KEENLDRKLELLEKREEELEKKEKEL 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1033370542 1140 RELQAQLAELQEDMESeklaraKAEKQRRDLgEELEALKTEledtldsTAAQQ---ELRSKREQEVTELKKTIEEEVK 1214
Cdd:PRK12704 120 EQKQQELEKKEEELEE------LIEEQLQEL-ERISGLTAE-------EAKEIlleKVEEEARHEAAVLIKEIEEEAK 183
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
996-1256 |
4.72e-03 |
|
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 226883 [Multi-domain] Cd Length: 570 Bit Score: 41.98 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 996 QLEKVSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEERLSEFTSHMAEEEEKVKSL----SKLRNKYeavmadmedRLKK 1071
Cdd:COG4477 273 QLELDEAEEELGLIQEKIESLYDLLEREVEAKNVVEENLPILPDYLEKAKENNEHLkeeiERVKESY---------RLAE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1072 EEKGRQEleKLKRKLDgEAGDLQEQVAELQQQLEELRQALARKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQE 1151
Cdd:COG4477 344 TELGSVR--KFEKELK-ELESVLDEILENIEAQEVAYSELQDNLEEIEKALTDIEDEQEKVQEHLTSLRKDELEARENLE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1152 DMESEKLARAKAEKQRR-------------DLGEELEALKTELEDTLDSTAAQQELRSKREQEVTELKKTIEEEVK--VH 1216
Cdd:COG4477 421 RLKSKLHEIKRYMEKSNlpglpetflslffTAGHEIQDLMKELSEVPINMEAVSALVDIATEDMNTLEDETEEVVEnaVL 500
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1033370542 1217 EAQVLDMRQRHTSALEELSEQLEQS-RRFKIN------LEKTKQALE 1256
Cdd:COG4477 501 AEQLIQYGNRYRSRNAEVAKSLNEAeRLFENAfdydasFEIASQALE 547
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1391-1645 |
5.30e-03 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 41.55 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1391 QMQSLQQQVMETKKKLEEDAGVAEAIEEARRRAAKDLESLSVRYEERVQACDKLEKGRTRLQQELDDVTVALDQQRQVVS 1470
Cdd:COG4372 89 ELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQQELARLTKQAQDLQTRLKTLAEQRRQLEAQAQ 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1471 ALEKKQKKFDQMLAEEKLISARYAEERDRAEADAREKETKvlslsralEEALETREEMERQNKQLRAEMDDLVSSKDdvg 1550
Cdd:COG4372 169 SLQASQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLATR--------ANAAQARTEELARRAAAAQQTAQAIQQRD--- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1551 KNVHELERFKRALEQQVQEMRAQMEELEDELQATEDGKLRLEVNMQALKAQHERELQnrddanddkkkLLSKQVRELEAE 1630
Cdd:COG4372 238 AQISQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQLEAYYQAYVRLRQQAAA-----------TQRGQVLAGAAQ 306
|
250
....*....|....*
gi 1033370542 1631 LDAERKQRAQALAGR 1645
Cdd:COG4372 307 RVAQAQAQAQAQAQL 321
|
|
| ERM |
pfam00769 |
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ... |
963-1188 |
5.36e-03 |
|
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.
Pssm-ID: 425860 [Multi-domain] Cd Length: 247 Bit Score: 40.69 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 963 RCQQLQGDKKKMQQHVQDLEEQLEEEEAARQKLQLEKVSTEAKLKKMEEdllvledqnsklhkerklMEERLSEftSHMA 1042
Cdd:pfam00769 14 RLKQYEEETRKAQEELEESEETAELLEEKLRVAEEEAELLEQKAQEAEE------------------EKERLEE--SAEM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1043 EEEEKVKSLSKLRNKYEAVMADMEDRLKKEEkgrqeleklkrkldgEAGDLQEQVAELQQQLEELRQALARKEAELQAAL 1122
Cdd:pfam00769 74 EAEEKEQLERELREAQEEVARLEEESERKEE---------------EAERLQEELEEAREEEEEAKEKLLAASTSPSHHH 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1033370542 1123 ARVEDEA---AQKNAVLKSLRELQAQLAELQEDMESEKLARAKAEKQRRdLGEELEALKTELEDTLDST 1188
Cdd:pfam00769 139 SEESENEddeEEEESYEGGSAELSNDGDMDQLSDRIEEERVTEAEKNER-LQKQLKALKSELAQARDET 206
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
1093-1475 |
5.81e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 434900 [Multi-domain] Cd Length: 384 Bit Score: 41.20 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1093 LQEQVAELQQQLEELRQALARKEAELqaalaRVEDEaaqKNAVLKSlrelqaQLAELQEDMESEKLARAKAEKQRRDLGE 1172
Cdd:pfam15742 11 QQEEVQQLRQDLQRLQILCTSAEREL-----RYERE---KNLDLKQ------HNSLLQEENIKIKAELKQAQQKLLDSTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1173 ELEALKTELEDtLDSTAAQQELRSKREQEVTELKKTIEEEVKVHEAQVLDMRQRhtsaLEELSEQLEQSRrfKINLEKT- 1251
Cdd:pfam15742 77 MCSSLTAEWEH-CQQKIRELELEVLKQAQSIKSQNSLQEKLAQEKSKVADAEKK----ILELQQKLEHAH--KVCLTETc 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1252 ---KQALEGENAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQ-----LRAGEG--ERAKAELVERLVKLQNELdGVSGT 1321
Cdd:pfam15742 150 ileKKQLEEEIKEAQENEAKLKQQYQEEQQKRKLLDQNVNELQqqvrsLQDKEAqlEMTNSQQQLRIQQQEAQL-KQLEN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1322 LGSTESKTIKLAKDLATVESHLQDTQELLQEETRQKLN-LSSRVRQLEEEKAamleqleeeeAAKANFSRQMQSLQQQVM 1400
Cdd:pfam15742 229 EKRKSDEHLKSNQELSEKLSSLQQEKEALQEELQQVLKqLDVHVRKYNEKHH----------HHKAKLRRAKDRLVHEVE 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1033370542 1401 ---ETKKKLEEDagvaeaIEEARRRaakdLESLSVRYEERVQACDKLEKGRTRLQQELDDVTVALDQQRQVVSALEKK 1475
Cdd:pfam15742 299 qrdERIKQLENE------IRILRQQ----IEKEKAFQKQVTAENDTLLLEKRKLLEQLTEQEEVIKNNKRTISSVQNR 366
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
990-1252 |
5.92e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 990 AARQKL--QLEKVSTEAKLKKMEEDLL-VLEDQNSKLHKERKLMEERLSEFTSHMAEEEEKVKS-LSKLRNKYEavmadm 1065
Cdd:PHA02562 150 PARRKLveDLLDISVLSEMDKLNKDKIrELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGEnIARKQNKYD------ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1066 eDRLKKEEKGRQELEKLkrkldgeagdlQEQVAELQQQLEELRQALARkeaeLQAALARVEDEAAQKNAVLKSLRELQ-- 1143
Cdd:PHA02562 224 -ELVEEAKTIKAEIEEL-----------TDELLNLVMDIEDPSAALNK----LNTAAAKIKSKIEQFQKVIKMYEKGGvc 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1144 ----AQLAELQEDMESEKLARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVTELK------KTIEEEV 1213
Cdd:PHA02562 288 ptctQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLItlvdkaKKVKAAI 367
|
250 260 270
....*....|....*....|....*....|....*....
gi 1033370542 1214 KVHEAQVLDmrqrHTSALEELSEQLEQSRRFKINLEKTK 1252
Cdd:PHA02562 368 EELQAEFVD----NAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
993-1454 |
6.28e-03 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes. Proteins in this family are typically between and 840 amino acids in length.
Pssm-ID: 434436 [Multi-domain] Cd Length: 521 Bit Score: 41.18 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 993 QKLQLEKVSTEAKLKkmEEDLLVLEDQNSKLHKERKLMEERlsefTSHMAEEEEKVKSLSKLRNKYEAVMADMEDRL--- 1069
Cdd:pfam15070 7 KQLQAERDQYAENLK--EEGAVWQQKMQQLSEQVRTLREEK----ERSVSQVQELETSLAELKNQAAVPPAEEQPPAgps 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1070 KKEEKGRQELEKLKRKLDGEAGDLQEQVAElQQQLEELRQALARKEAELQAALARVEDEAAQKNAVLkslrelqaqlael 1149
Cdd:pfam15070 81 EEEQRLQEEAEQLQKELEALAGQLQAQVRD-NEQLSRLNQEQEQRLLELERAAERWGEQAEDRKQIL------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1150 qEDMESEKLARAKAEKQRRDLGEELEAL-----KTELEDTLDSTAAQQELRSKRE---------QEVTELKKTIEEevKV 1215
Cdd:pfam15070 147 -EDMQSDRATISRALSQNRELKEQLAELqngfvKLTNENMELTSALQSEQHVKKElakklgqlqEELGELKETLEL--KS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1216 HEAQVLdMRQRhtsalEELSEQLEQsrrfkinLEKTKQALEGENAEMQKEVkLLQA------------AKLESEQRRKKL 1283
Cdd:pfam15070 224 QEAQSL-QEQR-----DQYLAHLQQ-------YVAAYQQLASEKEELHKQY-LLQTqlmdrlqheevqGKVAAEMARQEL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1284 EGQVQELQLRAGEGERAKAELveRLVKLQNELDGVSGTLGSTESKTIKLA--KDLatvEShlqdtqellQEETRQKLNls 1361
Cdd:pfam15070 290 QETQERLEALTQQNQQLQAQL--SLLANPGEGDGLESEEEDEEAPRPSLSipEDF---ES---------REAMVAFFN-- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1362 SRVRQLEEEKAAMLEQLEEEEaakanfsRQMQSLQQQVMETKKKLEEDAGVAEAIEEarrraakdlESLSVRYEERVQ-A 1440
Cdd:pfam15070 354 SALAQAEEERAELRRQLKEQK-------RRCRALAHQAAPARQEEQEHHAHAPGTGG---------DSVPVEVHQALQvA 417
|
490
....*....|....
gi 1033370542 1441 CDKLEKGRTRLQQE 1454
Cdd:pfam15070 418 MEKLQSRFTELMQE 431
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1493-1720 |
7.20e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 224259 [Multi-domain] Cd Length: 294 Bit Score: 40.43 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1493 YAEERDRAEADAREKETKVLSLSRALEEALETREEMERQNKQLRAEMDDLVSSKDDVGKNVHELERFKRALEqqvqEMRA 1572
Cdd:COG1340 39 LAEKRDELNAKVRELREKAQELREERDEINEEVQELKEKRDEINAKLQELRKEYRELKEKRNEFNLGGRSIK----SLER 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1573 QMEELEdELQATEDGKLRLEVNMQALKAQHERELQNRDDANDDKKKLlskqvRELEAELDAERKQRAQALAGRKKLELDL 1652
Cdd:COG1340 115 EIERLE-KKQQTSVLTPEEERELVQKIKELRKELEDAKKALEENEKL-----KELKAEIDELKKKAREIHEKIQELANEA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1033370542 1653 QEAMAQLDAANKGRDEAGKQLRKLQAQMKELWREVEEARAAREEIFIQSRESEKKLKNLEAELLQLQE 1720
Cdd:COG1340 189 QEYHEEMIKLFEEADELRKEADELHEEFVELSKKIDELHEEFRNLQNELRELEKKIKALRAKEKAAKR 256
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
880-1117 |
7.33e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 880 MQAKAVELQKVQEK----HTKTQMD------LKELENKYQQLSEEKTILAEQLQAETELFaeaEEMRARLAARKQELEDI 949
Cdd:PHA02562 145 MQLSAPARRKLVEDlldiSVLSEMDklnkdkIRELNQQIQTLDMKIDHIQQQIKTYNKNI---EEQRKKNGENIARKQNK 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 950 LHELESRVEEEEERCQQLQGDKKKMQQHVQDLEEQLEEEEAARQKLQlEKVSTEAKLKKMEEDLLV-------LEDQN-- 1020
Cdd:PHA02562 222 YDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIK-SKIEQFQKVIKMYEKGGVcptctqqISEGPdr 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1021 -SKLHKERKLMEERLSEFTSHMAEEEEKV-------KSLSKLRNKYEAVMADMEDRLKKEEKGRQELEKLKrkldGEAGD 1092
Cdd:PHA02562 301 iTKIKDKLKELQHSLEKLDTAIDELEEIMdefneqsKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQ----AEFVD 376
|
250 260
....*....|....*....|....*
gi 1033370542 1093 LQEQVAELQQQLEELRQALARKEAE 1117
Cdd:PHA02562 377 NAEELAKLQDELDKIVKTKSELVKE 401
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
991-1168 |
8.21e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 225177 [Multi-domain] Cd Length: 548 Bit Score: 40.97 E-value: 8.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 991 ARQKLQLEKVSTEAKLKKMEEDllVLEDQNSKLHKERKLMEerlsefTSHMAEEEEKVKSLSKLRNKYEAVMADMEDRLK 1070
Cdd:COG2268 272 AETEAEVAAWKAETRREAEQAE--ILAEQAIQEEKAQAEQE------VQHAKALEAREMRVGLIERQKETELEPQERSYF 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1071 KEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQALARKEAELQAALARVEDEAAQKNAVLKSLRELQAQLAELQ 1150
Cdd:COG2268 344 INAAQRQAQEEAKAAANIAEAIGAQAEAAVETARETEEAERAEQAALVAAAEAAEQEQVEIAVRAEAAKAEAEAQAAEIK 423
|
170
....*....|....*....
gi 1033370542 1151 EDME-SEKLARAKAEKQRR 1168
Cdd:COG2268 424 AEAEaIREKGKAEAEAKRA 442
|
|
| GumC |
COG3206 |
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane ... |
1404-1692 |
8.30e-03 |
|
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225747 [Multi-domain] Cd Length: 458 Bit Score: 40.89 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1404 KKLEEDAGVAEAIEEARRRAAKDLESLSVRYEERVQACDklEKGRTRLQQELDDVTVALDQQRQVvsalEKKQKKFDQML 1483
Cdd:COG3206 121 RLLKDLIGPDPTIFEISYRLDDLLESLKVLRAGRSRVIE--LSYTSNDPKLAAKLANALAQAYLA----DQLEAQLEAFR 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1484 AEEKLISARYAEERDRAEADAREKETKVLS--LSRALEEALETREEMERQNKQL------RAEMDDLVSSKDDVGKNVHE 1555
Cdd:COG3206 195 RASDSLDERLEELRARLQEAEAQVEDFRAQhgLTDAARGQLLSEQQLSALNTQLqsararLAQAEARLASLLQLLPLGRE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1556 LERFK-RALEQQVQEMRAQMEELEDELQA-TEDGKLRLEvNMQALKAQherelqnrddanddkkkllskqVRELEAELDA 1633
Cdd:COG3206 275 AAALReVLESPTIQDLRQQYAQVRQQIADlSTELGAKHP-QLVALEAQ----------------------LAELRQQIAA 331
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1033370542 1634 ERKQRAQALAGRKKLELDLQEAMAQLDAANKGRdeaGKQLRKLQAQMKELWREVEEARA 1692
Cdd:COG3206 332 ELRQILASLPNELALLEQQEAALEKELAQLKGR---LSKLPKLQVQLRELEREAEAARS 387
|
|
| COG1579 |
COG1579 |
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ... |
1510-1682 |
8.50e-03 |
|
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function prediction only];
Pssm-ID: 224495 [Multi-domain] Cd Length: 239 Bit Score: 40.04 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1510 KVLSLSRALEEALETREEMERQNKQLRAEMDDLVSSKDDVGKNVHELERFKRALEQQVQemraqmeELEDELQATEDGKL 1589
Cdd:COG1579 4 NNLKSLLAIQKLDLEKDRLEPRIKEIRKALKKAKAELEALNKALEALEIELEDLENQVS-------QLESEIQEIRERIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1590 RLEVNMQALKAQHERE-LQNRDDANDDKKKLLSKQVRELEAELDAERKQRAQALAGRKKLELDLQEAMAQLDAANKGRDE 1668
Cdd:COG1579 77 RAEEKLSAVKDERELRaLNIEIQIAKERINSLEDELAELMEEIEKLEKEIEDLKERLERLEKNLAEAEARLEEEVAEIRE 156
|
170
....*....|....
gi 1033370542 1669 AGKQLRKLQAQMKE 1682
Cdd:COG1579 157 EGQELSSKREELKE 170
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1060-1291 |
8.54e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1060 AVMADMEDRLKKEEKG-RQELEKLKRKLDGeagdLQEQVAELQQQLEELR----QALARKEAELQAALARVEDEAAQKNa 1134
Cdd:PHA02562 163 SVLSEMDKLNKDKIRElNQQIQTLDMKIDH----IQQQIKTYNKNIEEQRkkngENIARKQNKYDELVEEAKTIKAEIE- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1135 vlkslrELQAQLAELQEDMESEKLARAKAEKQRRDLGEELEALKTEL----EDTLDSTAAQQ-----ELRSKREQEVTEL 1205
Cdd:PHA02562 238 ------ELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIkmyeKGGVCPTCTQQisegpDRITKIKDKLKEL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1206 KKTIEEEVK--VHEAQVLDMRQRHTSALEELSEQLEQSRRfkinlekTKQALEGENAEMQKEVKLLQAaklESEQRRKKL 1283
Cdd:PHA02562 312 QHSLEKLDTaiDELEEIMDEFNEQSKKLLELKNKISTNKQ-------SLITLVDKAKKVKAAIEELQA---EFVDNAEEL 381
|
....*...
gi 1033370542 1284 EGQVQELQ 1291
Cdd:PHA02562 382 AKLQDELD 389
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
995-1181 |
8.86e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.04 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 995 LQLEKVSTEAKLKKMEEDLL-VLEDQNS--KLHKERKLMEERLSEFTSHMAEEEEKVKSLSKLrnKYEAVMADMEDRLKK 1071
Cdd:PLN02939 231 LKEENMLLKDDIQFLKAELIeVAETEERvfKLEKERSLLDASLRELESKFIVAQEDVSKLSPL--QYDCWWEKVENLQDL 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1072 EEKGRQELEKLKRKLDGEAgDLQEQVAELQQQLEE--LRQALARKEAELQAALARVEDEAAQKNAVLKSLREL-QAQLAE 1148
Cdd:PLN02939 309 LDRATNQVEKAALVLDQNQ-DLRDKVDKLEASLKEanVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLyQESIKE 387
|
170 180 190
....*....|....*....|....*....|...
gi 1033370542 1149 LQEDMESeklarAKAEKQRRDLGEELEALKTEL 1181
Cdd:PLN02939 388 FQDTLSK-----LKEESKKRSLEHPADDMPSEF 415
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1207-1651 |
8.96e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 40.90 E-value: 8.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1207 KTIEEEVKVHEAQVLDMRQRHTSALEELSEQLEQSRRFKINLEKTKQALEGENAEmQKEVKLLQAAKLESEQRRKKLEGQ 1286
Cdd:pfam09731 51 LGEDPPLAPKPKTFRPLQPSVVSAVTGESKEPKEEKKQVKIPRQSGVSSEVAEEE-KEATKDAAEAKAQLPKSEQEKEKA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1287 VQE-LQLRAGEGERAKAELVErlvklqneldgvsgtlgstesktiklAKDLAT--VESHLQDTQELLQEETRQKLNLSSR 1363
Cdd:pfam09731 130 LEEvLKEAISKAESATAVAKE--------------------------AKDDAIqaVKAHTDSLKEASDTAEISREKATDS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1364 VRQLEEEKAAmlEQLEEEEAAKANFSRQMQSLQQQVMETKKKLEEDAGVAEAIEEArrraAKDLESLSVRYEERVqacdk 1443
Cdd:pfam09731 184 ALQKAEALAE--KLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEK----AQSLAKLVDQYKELV----- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1444 lEKGRTRLQQELDDVTVALDQqrqVVSALEKKQK-KFDQMLAEEKL----ISARYAEERDRAEADAReketkvlslsRAL 1518
Cdd:pfam09731 253 -ASERIVFQQELVSIFPDIIP---VLKEDNLLSNdDLNSLIAHAHReidqLSKKLAELKKREEKHIE----------RAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1519 EEAletREEMERQNKQLRAEMDDLVSSkddvgknvhELERFKRALEQQVQEMRAQME-ELEDEL-QATEDGKLRLEvnmQ 1596
Cdd:pfam09731 319 EKQ---KEELDKLAEELSARLEEVRAA---------DEAQLRLEFEREREEIRESYEeKLRTELeRQAEAHEEHLK---D 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1033370542 1597 ALKAQhERELQNRDDANDDKKKLLSKQVRELE-AELDAERKQRAQALAGRKKLELD 1651
Cdd:pfam09731 384 VLVEQ-EIELQREFLQDIKEKVEEERAGRLLKlNELLANLKGLEKATSSHSEVEDE 438
|
|
| ClyA_MakA-like |
cd22655 |
Vibrio cholerae cytotoxin MakA (motility associated killing factor A), and similar proteins; ... |
1534-1646 |
8.98e-03 |
|
Vibrio cholerae cytotoxin MakA (motility associated killing factor A), and similar proteins; This model includes Vibrio cholerae motility associated killing factor A (MakA) cytotoxin, a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). The MakA protein is encoded by the mak operon. Transport of the MakA protein from the bacteria is shown to occur by flagellum-dependent secretion, highlighting a non-conventional and direct role of flagella in pathogenesis of V. cholerae; a conserved N-terminal FTPP motif is essential for MakA secretion via the flagellum channel in a proton motive force-dependent manner. Structure of MakA shows an elongated, almost entirely alpha-helical protein, with the head domain consisting of two helices and three beta-strands that together with the short beta-strand of the tail domain forms a four-stranded sheet. MakA has been demonstrated to cause toxicity in both Caenorhabditis elegans and zebrafish.
Pssm-ID: 439153 [Multi-domain] Cd Length: 342 Bit Score: 40.34 E-value: 8.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1534 QLRAEMDDLVSSKDDvgKNVHELERFKRALEQQVQEMRAQMEELEDELQATEDGKLRLEVNMQALKAQhereLQNR-DDA 1612
Cdd:cd22655 79 QILNIFKALPTAPDD--AQVEQIIALLQALQKPVQEIISNIAAYQGKLKAWGDKMQAAHDNLTTGAAQ----IQAAeTDL 152
|
90 100 110
....*....|....*....|....*....|....
gi 1033370542 1613 NDDKKKlLSKQVRELEAELDAERKQRAQALAGRK 1646
Cdd:cd22655 153 QADIDK-INNAIANLNAEIAKDNKAIAAAQIAIG 185
|
|
| PRK06975 |
PRK06975 |
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed |
1100-1192 |
9.14e-03 |
|
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
Pssm-ID: 235899 [Multi-domain] Cd Length: 656 Bit Score: 40.86 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1100 LQQQLEELRQALAR--KEAELQAALARVEDEAAQKnavlkSLRELQAQLAELQEDMESEKLARAKAEKQRRDLGEELEA- 1176
Cdd:PRK06975 344 LNRKVDRLDQELVQrqQANDAQTAELRVKTEQAQA-----SVHQLDSQFAQLDGKLADAQSAQQALEQQYQDLSRNRDDw 418
|
90
....*....|....*.
gi 1033370542 1177 LKTELEDTLdSTAAQQ 1192
Cdd:PRK06975 419 MIAEVEQML-SSASQQ 433
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
829-1138 |
9.21e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 829 RKAFMKKQQQMSALKVMQRNCAaylkLRHWQWWRLFTKVKPLLQVTRQDEVMQAKAVELQKVQEKHTKTQMDLKELENK- 907
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMA----LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKk 1633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 908 ----YQQLSEEKTILAEQLQAEtelfAEAEEMRARLAARKQELEdilhelesrvEEEEERCQQLQGDKKKMQQHVQDLEE 983
Cdd:PTZ00121 1634 kveqLKKKEAEEKKKAEELKKA----EEENKIKAAEEAKKAEED----------KKKAEEAKKAEEDEKKAAEALKKEAE 1699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 984 QLEEEEAARQKLQLEKVSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEERLSE-----FTSHMAEEEEkvKSLSKLRNKY 1058
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDeeekkKIAHLKKEEE--KKAEEIRKEK 1777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1059 EAVMADMEDrlKKEEKGRQELEKLKRKLDGEAGDLQEQVAELQQQLEELRQAL--ARKEAELQAALARVEDEAAQKNAVL 1136
Cdd:PTZ00121 1778 EAVIEEELD--EEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEdsAIKEVADSKNMQLEEADAFEKHKFN 1855
|
..
gi 1033370542 1137 KS 1138
Cdd:PTZ00121 1856 KN 1857
|
|
| DUF812 |
pfam05667 |
Protein of unknown function (DUF812); This family consists of several eukaryotic proteins of ... |
993-1153 |
9.23e-03 |
|
Protein of unknown function (DUF812); This family consists of several eukaryotic proteins of unknown function.
Pssm-ID: 428574 [Multi-domain] Cd Length: 601 Bit Score: 40.76 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 993 QKLQLEKVSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEERLSEFTShmAEEeekvkSLSKLRNKYEAVMADMEDRLKKE 1072
Cdd:pfam05667 353 EELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLLPD--AEE-----NIAKLQALVEASAQRLVELAGQW 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1073 EKGR----QELEKLKRKLDgeagdlqEQVAELQQQLEELRqalarkeaELQAALARVEDEAAQKNAVLKslrELQAQLAE 1148
Cdd:pfam05667 426 EKHRvpliEEYRALKEAKS-------NKESESQRKLEEIK--------ELREKIKEVAEEARSKEELYK---QLVAEYER 487
|
....*
gi 1033370542 1149 LQEDM 1153
Cdd:pfam05667 488 LPKDV 492
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
1088-1193 |
9.35e-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: 40.48 E-value: 9.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1088 GEAGDLQEQVAELQQQLEELRQALARKEAELQAAlarvedeAAQKNAVLKSLRELQAQLAELQEDMESE-KLARAKAEKQ 1166
Cdd:TIGR04320 254 NSLAALQAKLATAQADLAAAQTALNTAQAALTSA-------QTAYAAAQAALATAQKELANAQAQALQTaQNNLATAQAA 326
|
90 100
....*....|....*....|....*..
gi 1033370542 1167 RRDLGEELEALKTELEDTLDSTAAQQE 1193
Cdd:TIGR04320 327 LANAEARLAKAKEALANLNADLAKKQA 353
|
|
| COG1579 |
COG1579 |
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ... |
1172-1364 |
9.46e-03 |
|
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function prediction only];
Pssm-ID: 224495 [Multi-domain] Cd Length: 239 Bit Score: 40.04 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1172 EELEALKTELEDTLDSTAAQQELRSKREQEVTELKKTIEEEVKVHEAQVLDMRQRHTSALEELSeqleqsrrfkinlekt 1251
Cdd:COG1579 20 DRLEPRIKEIRKALKKAKAELEALNKALEALEIELEDLENQVSQLESEIQEIRERIKRAEEKLS---------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1252 kqalegeNAEMQKEVKLLQAAKLESEQRRKKLEGQVQELQLRAGEGERAKAELVERLVKLQNELDGVSGTLGSTESKTIK 1331
Cdd:COG1579 84 -------AVKDERELRALNIEIQIAKERINSLEDELAELMEEIEKLEKEIEDLKERLERLEKNLAEAEARLEEEVAEIRE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 1033370542 1332 LAKDLATVESHLQDT--QELLQEETRQKLNLSSRV 1364
Cdd:COG1579 157 EGQELSSKREELKEKldPELLSEYERIRKNKKGVG 191
|
|
| YhaN |
COG4717 |
Uncharacterized protein YhaN, contains AAA domain [Function unknown]; |
874-1422 |
9.48e-03 |
|
Uncharacterized protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 227061 [Multi-domain] Cd Length: 984 Bit Score: 40.98 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 874 TRQDEVMQAKAVELQKVQEKHTKTQMDLKELENKYQQLSEEKTILAEQLQAETELFAEAEEmRARLAARKQELEDIlhel 953
Cdd:COG4717 331 SAFELTETLAGIEADLRDKEEAAGNGFEAERVHDLRSLECMLRYQSSQRELKQTEAAYCKR-LDEKRLFEDEAEEE---- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 954 esrveeeeeRCQQLQGDKKKMQqhvqdleeqleeeeaARQKLQLEKVSTEAKLKKMEEDLLVLEDQNSKLHKERKLMEEr 1033
Cdd:COG4717 406 ---------ARQRLADDEEEVR---------------AGDEAREEKIAANSQVIDKEEVCNLYDRRDTAWQKQRFLREK- 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1034 LSEFTSHMAEEEEKV--KSLSKLRNKYEAVMADMEDRLKKEEKGRQeleklkrKLDGEAGDLQEQVAELQQQLEELRQAL 1111
Cdd:COG4717 461 QTAFERQKTEHTKIIalRLAGMLLVALSRLLTSLIFQIIFAVAQIV-------FLSAEIKSSSRAVREEKAAVTDIPEEL 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1112 ARKEAELQAALARVEDEAAQKNAvlkslRELQAQLAELQEDMEseklARAKAEKQRRDLGEELEALKTELEDTLDSTAAQ 1191
Cdd:COG4717 534 ARLLITDELPELAVDLLVQSRIR-----QHWQQLRKALDQLEA----AYEALEGRFAAAEAAMAEWQSEWEEALDELGLS 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1192 QELRSKREQEVTELKKTIEEEVKvheaqvldmrqrHTSALEELSEQLEQSRR-FKINLEKTKQALEGENAEMQ---KEVK 1267
Cdd:COG4717 605 RELSPEQQLDILSTMKDLKKLMQ------------KKAELTHQVARLREEQAaFEERVEGLLAVLEAQFIDLStlfCVQR 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1268 LLQAAKLESEQRRKKLEGQVQ-----ELQLRAGEGE--------------------RAKAELVERLVKLQNELDGVSGTL 1322
Cdd:COG4717 673 LRVAAELQKEEARLALEGNIErtkelNDELRAELELhrkeildlfdcgtadtedafREAAREEQQLTQRESRLESLEAQL 752
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033370542 1323 GSTESKTIKLAKDLA---TVESHLQDTQELLQEETRQKLNLSSRVRQLEEEKAAMLEQLEEeeaakANFSRQMQSLQQQV 1399
Cdd:COG4717 753 EGVAAEAYELSASLDqreLKEEELALLEEAIDALDEEVEELHAQVAALSRQIAQLEGGGTV-----AELRQRRESLKEDL 827
|
570 580
....*....|....*....|...
gi 1033370542 1400 METKKKLEEDAGVAEAIEEARRR 1422
Cdd:COG4717 828 EEKARKWASLRLAVQVLEEALRL 850
|
|
|