|
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 ... |
864-1943 |
0e+00 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 1449.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 864 TRQEEELVAKDEELLKVKEKQSKVEGELVDMEQKHQQLVEEKNILAEQLHAETELFAEAEEMRARLAIKKQEMEEILRDL 943
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 944 EIRMEEEEERNQVLQNEKKKMQTHVQDLEEQ-LDEEEAAQKLQLEKVTAEAKIKKMEEDILVLEDQNSKFLKEKKLLEER 1022
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQlDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1023 IAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKKEEKTRQELEKAKRKLDGETTDFQDQIAELQAQIEELKLQLAK 1102
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1103 KEEELQAALARGDEEVLQKNNTLKLVRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQE 1182
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1183 LRTKREQEVAELRKSIEEETRNHEAQIQEMRQRQATALEELSEQLEQAKRFKVNLEKNKQSLESDNKELATEVKSLQQMK 1262
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1263 AESEYKRKKLEGQVQELHAKVLEGDRLRADMVEKSSKLQNELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQEE 1342
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1343 TRQKLNQSSRIRQLEEEKNNLQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLKDTEGLGQR 1422
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1423 LEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARHAEERDRAEADAREKETKALS 1502
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1503 LARALDEALEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDELQGTEDAKLRLEV 1582
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1583 NMQAMKAQFERDLQTRDEQNEEKKRALVKQVRELEAELEDERKQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIKQL 1662
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1663 RKLQAQTKDYQRELEEARASRDDIFAQSKENEKKLKGLEAEILQLQEELAASERSRRHAEQERDELADEISNSTSGKSAL 1742
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1743 LDEKRRLEARIAHLEEELEEEQSNMELLNDRFRKTTLQVDTLNSELAAERSSGQKSENARQQLERQNKELKAKLQELEGS 1822
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1823 VKSKFKATIATLESKIAQLEEQLEQEAKERVASNKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANTRMKQLKRQLE 1902
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 148223878 1903 EAEEEATRANASARKLQRELDDATEANEVLSREVSTLKNRL 1943
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-787 |
0e+00 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 1422.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 179 ESGAGKTENTKKVIQYLAHVASSHKGKKDHTIPtespkaikhqsgsllyGELERQLLQANPILESFGNAKTVKNDNSSRF 258
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIP----------------GELERQLLQANPILESFGNAKTVKNDNSSRF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 259 GKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVSNGYIPIPGQQD 338
Cdd:cd14920 145 GKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 339 KDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGLNIMEFTRAILTPRIK 418
Cdd:cd14920 225 KDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 419 VGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEK 498
Cdd:cd14920 305 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 499 LQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANSPGVLALLDEECWFPKATDKTFVDKLVQEQGTHSK 578
Cdd:cd14920 385 LQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 579 FQKPRQLKDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVDRIVGLDQVAGMAETAFGAA 658
Cdd:cd14920 465 FQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSA 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 659 YKTKKGMFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 738
Cdd:cd14920 545 YKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 148223878 739 EFRQRYEILTPNSIPRGFMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd14920 625 EFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
99-787 |
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: 1306.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 179 ESGAGKTENTKKVIQYLAHVASSHKGKKDHTIPtespkaikhqsgsllYGELERQLLQANPILESFGNAKTVKNDNSSRF 258
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKK---------------KGTLEDQILQANPILEAFGNAKTVRNNNSSRF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 259 GKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYR-FVSNGYIPIPGQQ 337
Cdd:cd01377 146 GKFIRIHFGSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 338 DKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGLNIMEFTRAILTPRI 417
Cdd:cd01377 226 DAEEFKLTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 418 KVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNE 497
Cdd:cd01377 306 KVGREWVTKGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 498 KLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPanSPGVLALLDEECWFPKATDKTFVDKLVQEQGTHS 577
Cdd:cd01377 385 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKS 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 578 K-FQKPRQLKDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVDRivgldqvagmaETAFG 656
Cdd:cd01377 463 KnFKKPKPKKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE-----------SGGGG 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 657 AAYKTKKGMFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIV 736
Cdd:cd01377 532 GKKKKKGGSFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRII 611
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 148223878 737 FQEFRQRYEILTPNSIPRGFMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd01377 612 FAEFKQRYSILAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-787 |
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: 1223.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 179 ESGAGKTENTKKVIQYLAHVASSHKGKKDHTiptespkaikhqSGSLLYGELERQLLQANPILESFGNAKTVKNDNSSRF 258
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQS------------SIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 259 GKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVSNGYIPIPGQQD 338
Cdd:cd14932 149 GKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 339 KDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGLNIMEFTRAILTPRIK 418
Cdd:cd14932 229 KELFAETMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 419 VGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEK 498
Cdd:cd14932 309 VGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 499 LQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANSPGVLALLDEECWFPKATDKTFVDKLVQEQGTHSK 578
Cdd:cd14932 389 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 579 FQKPRQLKDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVDRIVGLDQVAGMAETAFGaA 658
Cdd:cd14932 469 FQKPKKLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHG-A 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 659 YKTKKGMFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 738
Cdd:cd14932 548 FKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 148223878 739 EFRQRYEILTPNSIPRGFMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd14932 628 EFRQRYEILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-787 |
0e+00 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 1199.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 179 ESGAGKTENTKKVIQYLAHVASSHKGKKDHtiptespkaikhqsgsllyGELERQLLQANPILESFGNAKTVKNDNSSRF 258
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ-------------------GELERQLLQANPILEAFGNAKTVKNDNSSRF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 259 GKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVSNGYIPIPGQQD 338
Cdd:cd14919 142 GKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 339 KDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGLNIMEFTRAILTPRIK 418
Cdd:cd14919 222 KDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 419 VGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEK 498
Cdd:cd14919 302 VGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 499 LQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANSPGVLALLDEECWFPKATDKTFVDKLVQEQGTHSK 578
Cdd:cd14919 382 LQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 579 FQKPRQLKDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVDRIVGLDQVAGMAETAFGAA 658
Cdd:cd14919 462 FQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGA 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 659 YKTKKGMFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 738
Cdd:cd14919 542 FKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQ 621
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 148223878 739 EFRQRYEILTPNSIPRGFMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd14919 622 EFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
99-787 |
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: 1184.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 179 ESGAGKTENTKKVIQYLAHVASSHKGKKDHTIptespkaikhqsgsllYGELERQLLQANPILESFGNAKTVKNDNSSRF 258
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSI----------------TGELEKQLLQANPILEAFGNAKTVKNDNSSRF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 259 GKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVSNGYIPIPGQQD 338
Cdd:cd14921 145 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 339 KDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGLNIMEFTRAILTPRIK 418
Cdd:cd14921 225 DEMFQETLEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 419 VGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEK 498
Cdd:cd14921 305 VGRDVVQKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 499 LQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANSPGVLALLDEECWFPKATDKTFVDKLVQEQGTHSK 578
Cdd:cd14921 385 LQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 579 FQKPRQLKDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVDRIVGLDQVAGMAETAFGAA 658
Cdd:cd14921 465 FQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSA 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 659 YKTKKGMFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 738
Cdd:cd14921 545 SKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQ 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 148223878 739 EFRQRYEILTPNSIPRGFMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd14921 625 EFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-787 |
0e+00 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 1168.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 179 ESGAGKTENTKKVIQYLAHVASSHKGKKDHtiptespkaikhQSGSLLYGELERQLLQANPILESFGNAKTVKNDNSSRF 258
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQ------------NSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 259 GKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVSNGYIPIPGQQD 338
Cdd:cd15896 149 GKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 339 KDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGLNIMEFTRAILTPRIK 418
Cdd:cd15896 229 KDLFTETMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 419 VGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEK 498
Cdd:cd15896 309 VGRDYVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 499 LQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANSPGVLALLDEECWFPKATDKTFVDKLVQEQGTHSK 578
Cdd:cd15896 389 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 579 FQKPRQLKDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVDRIVGLDQVAGMAEtaFGAA 658
Cdd:cd15896 469 FFKPKKLKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSE--MPGA 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 659 YKTKKGMFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 738
Cdd:cd15896 547 FKTRKGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 148223878 739 EFRQRYEILTPNSIPRGFMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd15896 627 EFRQRYEILTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
99-787 |
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: 1157.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 179 ESGAGKTENTKKVIQYLAHVASShKGKKDHTIPTESPKAIKHQsgsllyGELERQLLQANPILESFGNAKTVKNDNSSRF 258
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAAS-KPKGSGAVPHPAVNPAVLI------GELEQQLLQANPILEAFGNAKTVKNDNSSRF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 259 GKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVSNGYIPIPGQQD 338
Cdd:cd14911 154 GKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 339 KDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGLNIMEFTRAILTPRIK 418
Cdd:cd14911 234 YAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 419 VGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEK 498
Cdd:cd14911 314 VGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 499 LQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnspGVLALLDEECWFPKATDKTFVDKLVQEQGTHSK 578
Cdd:cd14911 394 LQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPK 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 579 FQKpRQLKDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVDrIVGLDQVAgMAETAFGAa 658
Cdd:cd14911 471 FMK-TDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQFGA- 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 659 yKTKKGMFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 738
Cdd:cd14911 547 -RTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQ 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 148223878 739 EFRQRYEILTPNSIPRGFMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd14911 626 EFRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-787 |
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: 1126.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 179 ESGAGKTENTKKVIQYLAHVASSHKGKKDHTIPtespkaikhqsgsllyGELERQLLQANPILESFGNAKTVKNDNSSRF 258
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP----------------GELERQLLQANPILEAFGNAKTVKNDNSSRF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 259 GKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVSNGYIPIPGQQd 338
Cdd:cd14930 145 GKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 339 KDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGLNIMEFTRAILTPRIK 418
Cdd:cd14930 224 RELFQETLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 419 VGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEK 498
Cdd:cd14930 304 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 499 LQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANSPGVLALLDEECWFPKATDKTFVDKLVQEQGTHSK 578
Cdd:cd14930 384 LQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPK 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 579 FQKPRQLKDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVDRIVGLDQVAGMAETAFGAa 658
Cdd:cd14930 464 FQRPRHLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGG- 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 659 yKTKKGMFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 738
Cdd:cd14930 543 -RPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQ 621
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 148223878 739 EFRQRYEILTPNSIPRGFMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd14930 622 EFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
87-787 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1096.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 87 VEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 167 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGKKdhtiptespkaikhqsgsllYGELERQLLQANPILESFGN 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN--------------------VGRLEEQILQSNPILEAFGN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 247 AKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFV 326
Cdd:pfam00063 141 AKTVRNNNSSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 327 SN-GYIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGLNI 405
Cdd:pfam00063 221 SQsGCYTIDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 406 MEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKRQGASFIGILDIAGFEIFELN 485
Cdd:pfam00063 301 TELEKALCKRRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 486 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanSPGVLALLDEECWFPKATDKTF 565
Cdd:pfam00063 381 SFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 566 VDKLVQEQGTHSKFQKPRQlKDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVDRIVGLD 645
Cdd:pfam00063 458 LDKLYSTFSKHPHFQKPRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAA 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 646 QVAGMAETafgaAYKTKKGMFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIR 725
Cdd:pfam00063 537 ANESGKST----PKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIR 612
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148223878 726 ICRQGFPNRIVFQEFRQRYEILTPNSIPRGFMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:pfam00063 613 IRRAGFPNRITFQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
80-799 |
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: 998.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 80 NPPKFSKVEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISE 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 160 SAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGKkdhtiptespkaikhqsgsllyGELERQLLQANP 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV----------------------GSVEDQILESNP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 240 ILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDG 319
Cdd:smart00242 139 ILEAFGNAKTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 320 FNNYRFVSNG-YIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENT-AAQKL 397
Cdd:smart00242 219 PEDYRYLNQGgCLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 398 CHLLGLNIMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDrTKRQGASFIGILDIA 477
Cdd:smart00242 299 AELLGVDPEELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLS-FKDGSTYFIGVLDIY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 478 GFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANSPGVLALLDEECWF 557
Cdd:smart00242 378 GFEIFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRF 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 558 PKATDKTFVDKLVQEQGTHSKFQKPRQlKDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKD 637
Cdd:smart00242 455 PKGTDQTFLEKLNQHHKKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 638 vdrivgldqvagmaetafGAAYKTKKGMFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRC 717
Cdd:smart00242 534 ------------------GVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRY 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 718 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNSIPRGFMDGKQACERMIRSLELDPNLYRIGQSKIFFRAGVLAHLEEE 797
Cdd:smart00242 596 LGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEEL 675
|
..
gi 148223878 798 RD 799
Cdd:smart00242 676 RE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
36-1363 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 911.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 36 VWVPSERHGFEAASIKEERGDEVVVELA---ENGKKAIVNKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLKDRYY 110
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEEgkkEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 111 SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKK 190
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 191 VIQYLAHVASSHkgkkdhtiPTESpkaikhqsgsllyGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 270
Cdd:COG5022 172 IMQYLASVTSSS--------TVEI-------------SSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 271 YIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVSNGYIP-IPGQQDKDNFQETMEAM 349
Cdd:COG5022 231 EICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDAL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 350 HIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNtDQASMPENTAAQKLCHLLGLNIMEFTRAILTPRIKVGRDYVQKAQT 429
Cdd:COG5022 311 KTIGIDEEEQDQIFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 430 KEQADFAVEALRKATYERLFRWLVYRINKALDRTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 509
Cdd:COG5022 390 LEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 510 LEQEEYQREGIEWNFIDFgLDLQPCIDLIERpANSPGVLALLDEECWFPKATDKTFVDKLVQ--EQGTHSKFQKPRQLKD 587
Cdd:COG5022 469 LEQEEYVKEGIEWSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDN 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 588 KadFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVDRIVgldqvagmaetafgaayktKKGMFR 667
Cdd:COG5022 547 K--FVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-------------------SKGRFP 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 668 TVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 747
Cdd:COG5022 606 TLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRIL 685
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 748 TPNSIPRG----FMDGKQACERMIRSLELDPNLYRIGQSKIFFRAGVLAHLEEERDLKITDIIVLFQAVCRGYLARKAFA 823
Cdd:COG5022 686 SPSKSWTGeytwKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYL 765
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 824 KKQQQLIALKVLQRNCAAYLKLRHWQWWRLFTKVKPLLQVTRQEEELVAKDEELLKVKEKqskvegelVDMEQKHQQLVE 903
Cdd:COG5022 766 QALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKT--------IKREKKLRETEE 837
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 904 EK-NILAEQLHAETELFAEAEEMRARLaikkqEMEEILRDLEIRMEEEEERNQVLQNEKKKMQthvqdleeqldeEEAAQ 982
Cdd:COG5022 838 VEfSLKAEVLIQKFGRSLKAKKRFSLL-----KKETIYLQSAQRVELAERQLQELKIDVKSIS------------SLKLV 900
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 983 KLQLEKVTAEAKIKKMEEDILVLEDQNSKFLKEKKLLEERIAE--STSQLAEEEEKAKNLAKLKNKQEmMISDLEERLKK 1060
Cdd:COG5022 901 NLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEegPSIEYVKLPELNKLHEVESKLKE-TSEEYEDLLKK 979
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1061 EEKTRQELEKAKRKLDG---ETTDFQDQIAELQAQIEELKlQLAKKEEELQAALARGDEEvlqknntlklvRELQAQIAE 1137
Cdd:COG5022 980 STILVREGNKANSELKNfkkELAELSKQYGALQESTKQLK-ELPVEVAELQSASKIISSE-----------STELSILKP 1047
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1138 LQEdlesekaSRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELRKSIEEETRNH--EAQIQEMRQR 1215
Cdd:COG5022 1048 LQK-------LKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLvkPANVLQFIVA 1120
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1216 QATALEELSEQLEQAKRFKVNLEKNKQSLESDNKELAT--EVKSLQQ---------MKAESEYKRKKLEGQVQELHAKVL 1284
Cdd:COG5022 1121 QMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGlfWEANLEAlpspppfaaLSEKRLYQSALYDEKSKLSSSEVN 1200
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1285 EgdrLRADMVEKSSKLQNELeNVSSLLEEAEKKGI------KLAKDVASMESQLQDTQELLQEETRQKLNQSSRIRQLEE 1358
Cdd:COG5022 1201 D---LKNELIALFSKIFSGW-PRGDKLKKLISEGWvpteysTSLKGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYK 1276
|
....*
gi 148223878 1359 EKNNL 1363
Cdd:COG5022 1277 LEEEV 1281
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
99-787 |
0e+00 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 851.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 178 GESGAGKTENTKKVIQYLAHVASSHKGKKDHTiptespkaikhqsgsllYGELERQLLQANPILESFGNAKTVKNDNSSR 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSS-----------------ASSIEQQILQSNPILEAFGNAKTVRNDNSSR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 258 FGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRF-----VSNGYIP 332
Cdd:cd00124 144 FGKFIELQFDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYlndylNSSGCDR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 333 IPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNT--DQASMPENTAAQKLCHLLGLNIMEFTR 410
Cdd:cd00124 224 IDGVDDAEEFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 411 AILTPRIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKRQ-GASFIGILDIAGFEIFELNSFEQ 489
Cdd:cd00124 304 ALTTRTIKVGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 490 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPanSPGVLALLDEECWFPKATDKTFVDKL 569
Cdd:cd00124 384 LCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 570 VQEQGTHSKFQKPRQLKDKAdFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDkfvselwkdvdrivgldqvag 649
Cdd:cd00124 461 YSAHGSHPRFFSKKRKAKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ--------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 650 maetafgaayktkkgmfrtvgqlYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQ 729
Cdd:cd00124 519 -----------------------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRA 575
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 148223878 730 GFPNRIVFQEFRQRYEILTPNSIPRGFMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd00124 576 GYPVRLPFDEFLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
99-787 |
0e+00 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 782.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 179 ESGAGKTENTKKVIQYLAHVASShkgkkdhtipTESPKAIKHQSGSLLYGELERQLLQANPILESFGNAKTVKNDNSSRF 258
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAAL----------GDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 259 GKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKsDLLLDGFN--NYRFVSNGYIPIPGQ 336
Cdd:cd14927 151 GKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLVSMNpyDYHFCSQGVTTVDNM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 337 QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGLNIMEFTRAILTPR 416
Cdd:cd14927 230 DDGEELMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 417 IKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTN 496
Cdd:cd14927 310 VKVGNEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 497 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnspGVLALLDEECWFPKATDKTFVDKLVQEQ-GT 575
Cdd:cd14927 389 EKLQQFFNHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 576 HSKFQKPR---QLKDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVdriVGLDQVagmAE 652
Cdd:cd14927 466 SPNFQKPRpdkKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENY---VGSDST---ED 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 653 TAFGAAYKTKKGM-FRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGF 731
Cdd:cd14927 540 PKSGVKEKRKKAAsFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGF 619
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 148223878 732 PNRIVFQEFRQRYEILTPNSIPR-GFMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd14927 620 PNRILYADFKQRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-787 |
0e+00 |
|
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276878 [Multi-domain] Cd Length: 668 Bit Score: 767.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 180 SGAGKTENTKKVIQYLAHVASSHKGKKdhtiptespkaikhQSGSLLYGELERQLLQANPILESFGNAKTVKNDNSSRFG 259
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGDLAK--------------KKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 260 KFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLkSDLLLDGFN--NYRFVSNGYIPIPGQQ 337
Cdd:cd14913 148 KFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNpyDYPFISQGEILVASID 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 338 DKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGLNIMEFTRAILTPRI 417
Cdd:cd14913 227 DAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 418 KVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNE 497
Cdd:cd14913 307 KVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 498 KLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnspGVLALLDEECWFPKATDKTFVDKLV-QEQGTH 576
Cdd:cd14913 386 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKS 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 577 SKFQKPRQLKDKAD--FCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDvdrIVGLDqvagmAETA 654
Cdd:cd14913 463 NNFQKPKVVKGRAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYAT---FATAD-----ADSG 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 655 FGAAYKTKKGMFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNR 734
Cdd:cd14913 535 KKKVAKKKGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNR 614
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 148223878 735 IVFQEFRQRYEILTPNSIPRG-FMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd14913 615 ILYGDFKQRYRVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-787 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 747.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 179 ESGAGKTENTKKVIQYLAHVASSHKGkkdhtiPTESPKAikhqsgsllyGELERQLLQANPILESFGNAKTVKNDNSSRF 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKT------DEAAKSK----------GSLEDQVVQTNPVLEAFGNAKTVRNDNSSRF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 259 GKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLL-DGFNNYRFVSNGYIPIPGQQ 337
Cdd:cd14909 145 GKFIRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 338 DKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGLNIMEFTRAILTPRI 417
Cdd:cd14909 225 DGEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 418 KVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNE 497
Cdd:cd14909 305 KVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 498 KLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnspGVLALLDEECWFPKATDKTFVDKLVQEQ-GTH 576
Cdd:cd14909 384 KLQQFFNHHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 577 SKFQKPRQLK---DKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDvdrivGLDQVAGMAET 653
Cdd:cd14909 461 APFQKPKPPKpgqQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAD-----HAGQSGGGEQA 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 654 AFGAAykTKKGMFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 733
Cdd:cd14909 536 KGGRG--KKGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPN 613
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 148223878 734 RIVFQEFRQRYEILTPNSIpRGFMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd14909 614 RMMYPDFKMRYKILNPAGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
99-787 |
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: 734.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 179 ESGAGKTENTKKVIQYLAHVASSHKGKKDHTiptespkaikhqsgsllyGELERQLLQANPILESFGNAKTVKNDNSSRF 258
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDGK------------------GSLEDQIIQANPVLEAFGNAKTTRNNNSSRF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 259 GKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHL-KSDLLLDGFNNYRFVSNGYIPIPGQQ 337
Cdd:cd14934 143 GKFIRIHFGTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELiESLLLVPNPKEYHWVSQGVTVVDNMD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 338 DKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGLNIMEFTRAILTPRI 417
Cdd:cd14934 223 DGEELQITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 418 KVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNE 497
Cdd:cd14934 303 KVGNEFVQKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 498 KLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnspGVLALLDEECWFPKATDKTFVDKLVQEQ-GTH 576
Cdd:cd14934 382 KLQQFFNHHMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKS 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 577 SKFQKPRQLKDK---ADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSdkfvselwkdvdriVGLDQVAGMAET 653
Cdd:cd14934 459 SNFLKPKGGKGKgpeAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSS--------------LGLLALLFKEEE 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 654 AFGAAYKTKKGM-FRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFP 732
Cdd:cd14934 525 APAGSKKQKRGSsFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFP 604
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 148223878 733 NRIVFQEFRQRYEILTPNSIPRGFMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd14934 605 NRLQYPEFKQRYQVLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-787 |
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: 709.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 100 SVLHNLKDRYYSG-LIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 179 ESGAGKTENTKKVIQYLAHVASSHKGKKdhtiptespkaikhqsgsllygELERQLLQANPILESFGNAKTVKNDNSSRF 258
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSGET----------------------QVEEKVLASNPIMEAFGNAKTTRNDNSSRF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 259 GKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVSNG-YIPIPGQQ 337
Cdd:cd01380 140 GKYIEILFDKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGgSPVIDGVD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 338 DKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGLNIMEFTRAILTPRI 417
Cdd:cd01380 220 DAAEFEETRKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 418 KVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTN 496
Cdd:cd01380 300 VTRSEVIVKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYAN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 497 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpaNSPGVLALLDEECWFPKATDKTFVDKLVQEQGTH 576
Cdd:cd01380 380 EKLQQQFNQHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 577 SK--FQKPRQLKDKadFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSsdkfvselwkdvdrivgldqvagmaeta 654
Cdd:cd01380 456 PNkhFKKPRFSNTA--FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKAS---------------------------- 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 655 fgaayKTKKgmfRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNR 734
Cdd:cd01380 506 -----KNRK---KTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSR 577
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 148223878 735 IVFQEFRQRYEILTPnSIPRGFMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd01380 578 WTYEEFFSRYRVLLP-SKEWLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
99-787 |
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: 707.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 179 ESGAGKTENTKKVIQYLAHVASSHKGKKDhtiptespkaikhqsgsllYGELERQLLQANPILESFGNAKTVKNDNSSRF 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKK-------------------LGALEDQIMQANPVLEAFGNAKTLRNDNSSRF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 259 GKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEhlKSDLLLDGFN--NYRFVSNGYIPIPGQ 336
Cdd:cd14929 142 GKFIRMHFGARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE--LRDLLLVSANpsDFHFCSCGAVAVESL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 337 QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGLNIMEFTRAILTPR 416
Cdd:cd14929 220 DDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 417 IKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTN 496
Cdd:cd14929 300 IKVGNEYVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTN 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 497 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnspGVLALLDEECWFPKATDKTFVDKLVQEQ-GT 575
Cdd:cd14929 379 EKLQQFFNQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 576 HSKFQKPRQLKDK--ADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDvdrivglDQVAGMAeT 653
Cdd:cd14929 456 SVHFQKPKPDKKKfeAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEN-------YISTDSA-I 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 654 AFGAAYKTKKGMFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 733
Cdd:cd14929 528 QFGEKKRKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPN 607
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 148223878 734 RIVFQEFRQRYEILTPNSIPRG-FMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd14929 608 RLLYADFKQRYCILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-787 |
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: 705.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 180 SGAGKTENTKKVIQYLAHVAS-SHKGKKDhtiptESPKAikhqsgsllyGELERQLLQANPILESFGNAKTVKNDNSSRF 258
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAiGDRSKKD-----QTPGK----------GTLEDQIIQANPALEAFGNAKTVRNDNSSRF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 259 GKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLkSDLLLDGFN--NYRFVSNGYIPIPGQ 336
Cdd:cd14917 147 GKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPEL-LDMLLITNNpyDYAFISQGETTVASI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 337 QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGLNIMEFTRAILTPR 416
Cdd:cd14917 226 DDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 417 IKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTN 496
Cdd:cd14917 306 VKVGNEYVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 497 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnspGVLALLDEECWFPKATDKTFVDKLVQEQ-GT 575
Cdd:cd14917 385 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 576 HSKFQKPRQLKDK--ADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDvdrivgldqVAGMAET 653
Cdd:cd14917 462 SNNFQKPRNIKGKpeAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN---------YAGADAP 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 654 AFGAAYKTKKG-MFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFP 732
Cdd:cd14917 533 IEKGKGKAKKGsSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFP 612
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 148223878 733 NRIVFQEFRQRYEILTPNSIPRG-FMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd14917 613 NRILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
101-787 |
0e+00 |
|
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276882 [Multi-domain] Cd Length: 668 Bit Score: 688.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 101 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGES 180
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 181 GAGKTENTKKVIQYLAHVASSHKGKKDhtiptESPKaikhqsgslLYGELERQLLQANPILESFGNAKTVKNDNSSRFGK 260
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKE-----ESGK---------MQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 261 FIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLL-DGFNNYRFVSNGYIPIPGQQDK 339
Cdd:cd14918 149 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 340 DNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGLNIMEFTRAILTPRIKV 419
Cdd:cd14918 229 EELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 420 GRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 499
Cdd:cd14918 309 GNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 500 QQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnspGVLALLDEECWFPKATDKTFVDKLV-QEQGTHSK 578
Cdd:cd14918 388 QQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSAN 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 579 FQKPRQLKDKAD--FCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVdrivgldqVAGMAETAFG 656
Cdd:cd14918 465 FQKPKVVKGKAEahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY--------ASAEADSGAK 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 657 AAYKTKKGMFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIV 736
Cdd:cd14918 537 KGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRIL 616
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 148223878 737 FQEFRQRYEILTPNSIPRG-FMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd14918 617 YGDFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-787 |
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: 688.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 180 SGAGKTENTKKVIQYLAHVAS-SHKGKKDHTIPTEspkaikhqsgsllyGELERQLLQANPILESFGNAKTVKNDNSSRF 258
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKENPNANK--------------GTLEDQIIQANPALEAFGNAKTVRNDNSSRF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 259 GKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLL-DGFNNYRFVSNGYIPIPGQQ 337
Cdd:cd14916 148 GKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtNNPYDYAFVSQGEVSVASID 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 338 DKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGLNIMEFTRAILTPRI 417
Cdd:cd14916 228 DSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 418 KVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNE 497
Cdd:cd14916 308 KVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 498 KLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnspGVLALLDEECWFPKATDKTFVDKLVQEQ-GTH 576
Cdd:cd14916 387 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 577 SKFQKPRQLKDK--ADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVdrivgldQVAGMAETA 654
Cdd:cd14916 464 NNFQKPRNVKGKqeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY-------ASADTGDSG 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 655 FGAAYKTKKGMFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNR 734
Cdd:cd14916 537 KGKGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNR 616
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 148223878 735 IVFQEFRQRYEILTPNSIPRG-FMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd14916 617 ILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-787 |
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: 684.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 180 SGAGKTENTKKVIQYLAHVASSHKGKKDhtiptespkaikhQSGSLLYGELERQLLQANPILESFGNAKTVKNDNSSRFG 259
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKE-------------QQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 260 KFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLkSDLLLDGFN--NYRFVSNGYIPIPGQQ 337
Cdd:cd14923 149 KFIRIHFGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNpfDFPFVSQGEVTVASID 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 338 DKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGLNIMEFTRAILTPRI 417
Cdd:cd14923 228 DSEELLATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 418 KVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNE 497
Cdd:cd14923 308 KVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 498 KLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnspGVLALLDEECWFPKATDKTFVDKLV-QEQGTH 576
Cdd:cd14923 387 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 577 SKFQKPRQLKDKAD--FCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVdriVGLDQVAGMAETA 654
Cdd:cd14923 464 NNFQKPKPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNY---AGAEAGDSGGSKK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 655 FGaayKTKKGMFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNR 734
Cdd:cd14923 541 GG---KKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSR 617
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 148223878 735 IVFQEFRQRYEILTPNSIPRG-FMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd14923 618 ILYADFKQRYRILNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-787 |
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: 684.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 180 SGAGKTENTKKVIQYLAHVASSHKGKKDHTiptespkaikhqSGSLLYGELERQLLQANPILESFGNAKTVKNDNSSRFG 259
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEI------------TSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 260 KFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLL-DGFNNYRFVSNGYIPIPGQQD 338
Cdd:cd14912 150 KFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 339 KDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGLNIMEFTRAILTPRIK 418
Cdd:cd14912 230 QEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 419 VGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEK 498
Cdd:cd14912 310 VGNEYVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 499 LQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnspGVLALLDEECWFPKATDKTFVDKLV-QEQGTHS 577
Cdd:cd14912 389 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 578 KFQKPRQLKDKAD--FCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVDRIVGldqvagmaETAF 655
Cdd:cd14912 466 NFQKPKVVKGKAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEG--------ASAG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 656 GAAYK--TKKG-MFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFP 732
Cdd:cd14912 538 GGAKKggKKKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFP 617
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 148223878 733 NRIVFQEFRQRYEILTPNSIPRG-FMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd14912 618 SRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-787 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 683.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 180 SGAGKTENTKKVIQYLAHVASSHKGKKDHTiptespkaikhqSGSLLYGELERQLLQANPILESFGNAKTVKNDNSSRFG 259
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEA------------TSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 260 KFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLL-DGFNNYRFVSNGYIPIPGQQD 338
Cdd:cd14910 150 KFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 339 KDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGLNIMEFTRAILTPRIK 418
Cdd:cd14910 230 QEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 419 VGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEK 498
Cdd:cd14910 310 VGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 499 LQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnspGVLALLDEECWFPKATDKTFVDKLVQEQ-GTHS 577
Cdd:cd14910 389 LQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 578 KFQKPRQLKDK--ADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVdrivgldqVAGMAETAF 655
Cdd:cd14910 466 NFQKPKPAKGKveAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGA--------AAAEAEEGG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 656 GAAYKTKKG-MFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNR 734
Cdd:cd14910 538 GKKGGKKKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSR 617
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 148223878 735 IVFQEFRQRYEILTPNSIPRG-FMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd14910 618 ILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-787 |
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: 673.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 180 SGAGKTENTKKVIQYLAHVASSHKGKKDHTiptespkaikhqSGSLLYGELERQLLQANPILESFGNAKTVKNDNSSRFG 259
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEA------------ASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 260 KFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLkSDLLLDGFNNYRF--VSNGYIPIPGQQ 337
Cdd:cd14915 150 KFIRIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEITVPSID 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 338 DKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGLNIMEFTRAILTPRI 417
Cdd:cd14915 229 DQEELMATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 418 KVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNE 497
Cdd:cd14915 309 KVGNEYVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 498 KLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnspGVLALLDEECWFPKATDKTFVDKLVQEQ-GTH 576
Cdd:cd14915 388 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKS 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 577 SKFQKPRQLKDKAD--FCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVDrivgldqvAGMAETA 654
Cdd:cd14915 465 NNFQKPKPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQ--------TAEAEGG 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 655 FGAAYKTKKG-MFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 733
Cdd:cd14915 537 GGKKGGKKKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPS 616
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 148223878 734 RIVFQEFRQRYEILTPNSIPRG-FMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd14915 617 RILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-787 |
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: 637.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRgkKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 180 SGAGKTENTKKVIQYLAHVASSHKGkkdhtiptespkaikhqsgsllygeLERQLLQANPILESFGNAKTVKNDNSSRFG 259
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG-------------------------IENEILQTNPILEAFGNAKTLRNDNSSRFG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 260 KFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVS-NGYIPIPGQQD 338
Cdd:cd01383 135 KLIDIHFDAAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNqSNCLTIDGVDD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 339 KDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGLNIMEFTRAILTPRIK 418
Cdd:cd01383 215 AKKFHELKEALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQ 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 419 VGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEK 498
Cdd:cd01383 295 AGGDKIVKKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANER 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 499 LQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIE-RPAnspGVLALLDEECWFPKATDKTFVDKLVQEQGTHS 577
Cdd:cd01383 375 LQQHFNRHLFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPL---GLISLLDEESNFPKATDLTFANKLKQHLKSNS 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 578 KFQKPRqlkDKAdFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELwkdvdrivgldqVAGMAETAFGA 657
Cdd:cd01383 451 CFKGER---GGA-FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLF------------ASKMLDASRKA 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 658 AYKTKKGMF----RTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 733
Cdd:cd01383 515 LPLTKASGSdsqkQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPT 594
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 148223878 734 RIVFQEFRQRYEILTPNSIpRGFMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd01383 595 RMTHQEFARRYGFLLPEDV-SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
100-787 |
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: 630.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 180 SGAGKTENTKKVIQYLAHVASSHKgkkdhtiptespkaikhqsgsllygELERQLLQANPILESFGNAKTVKNDNSSRFG 259
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS-------------------------WVEQQILEANTILEAFGNAKTVRNDNSSRFG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 260 KFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAG--SGEHLKSDLLLDGFNNYRFVS-NGYIPIPGQ 336
Cdd:cd14883 137 KFIEVCFDASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGakHSKELKEKLKLGEPEDYHYLNqSGCIRIDNI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 337 QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQK-LCHLLGLNIMEFTRAILTP 415
Cdd:cd14883 217 NDKKDFDHLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALTVEDKEILKiVAKLLGVDPDKLKKALTIR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 416 RIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKRQGaSFIGILDIAGFEIFELNSFEQLCINYT 495
Cdd:cd14883 297 QINVRGNVTEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 496 NEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanSPGVLALLDEECWFPKATDKTFVDKLVQEQGT 575
Cdd:cd14883 376 NEKLHKFFNHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEK 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 576 HSKFQKPRQLKDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVDrIVGLDQVAGMAETAf 655
Cdd:cd14883 453 HPYYEKPDRRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPD-LLALTGLSISLGGD- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 656 GAAYKTKKGMfRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRI 735
Cdd:cd14883 531 TTSRGTSKGK-PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHL 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 148223878 736 VFQEFRQRYEILTPNSIPRGFMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd14883 610 TFKEFVDRYLCLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
100-787 |
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: 630.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 180 SGAGKTENTKKVIQYLAHVASSHKGKKDHtiptespkaIKHqsgsllygelerQLLQANPILESFGNAKTVKNDNSSRFG 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESEVER---------VKD------------MLLASNPLLEAFGNAKTLRNDNSSRFG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 260 KFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDG-FNNYRFVSNGYIPIPGQQD 338
Cdd:cd01378 141 KYMEIQFDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRpEQYYYYSKSGCFDVDGIDD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 339 KDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNtDQASMPENTAAQKLCHLLGLNIMEFTRAILTPRIK 418
Cdd:cd01378 221 AADFKEVLNAMKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 419 VG---RDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYT 495
Cdd:cd01378 300 TGgggRSVYEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 496 NEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpANSPGVLALLDEECWFP-KATDKTFVDKLVQEQG 574
Cdd:cd01378 380 NEKLQQIFIELTLKAEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFS 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 575 THSKFQKPRQLKD--KADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVDRivgldqvagmae 652
Cdd:cd01378 457 NHPHFECPSGHFElrRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD------------ 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 653 tafgaayKTKKGMFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFP 732
Cdd:cd01378 525 -------LDSKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFA 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 148223878 733 NRIVFQEFRQRYEILTPNSIPRGFMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd01378 598 YRQTYEKFLERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
99-787 |
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: 605.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 179 ESGAGKTENTKKVIQYLAHVASSHKgkkdhtiptespkaikhqsgsllygELERQLLQANPILESFGNAKTVKNDNSSRF 258
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS-------------------------WIEQQILEANPILEAFGNAKTIRNDNSSRF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 259 GKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVSNG-YIPIPGQQ 337
Cdd:cd01381 136 GKYIDIHFNKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGnCLTCEGRD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 338 DKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKK--ERNTDQASMPENTAAQKLCHLLGLNIMEFTRAILTP 415
Cdd:cd01381 216 DAAEFADIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 416 RIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKRQGAS--FIGILDIAGFEIFELNSFEQLCIN 493
Cdd:cd01381 296 TIFTRGETVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCIN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 494 YTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLI-ERPANspgVLALLDEECWFPKATDKTFVDKLVQE 572
Cdd:cd01381 376 FANENLQQFFVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHST 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 573 QGTHSKFQKPRQLKDKAdFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVdrivgldqVAGMAE 652
Cdd:cd01381 452 HGNNKNYLKPKSDLNTS-FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNED--------ISMGSE 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 653 TAfgaayktKKGMfrTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFP 732
Cdd:cd01381 523 TR-------KKSP--TLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYP 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 148223878 733 NRIVFQEFRQRYEILTPNSIPRGFMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd01381 594 IRHTFEEFVERYRVLVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
99-787 |
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: 591.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 178 GESGAGKTENTKKVIQYLAHVASsHKGKKDHTIptespkaikhqsgsllygelERQLLQANPILESFGNAKTVKNDNSSR 257
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGG-RAVTEGRSV--------------------EQQVLESNPLLEAFGNAKTVRNNNSSR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 258 FGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFV--SNGYiPIPG 335
Cdd:cd01384 140 FGKFVEIQFDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLnqSKCF-ELDG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 336 QQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKL---CHLLGLNIMEFTRAi 412
Cdd:cd01384 219 VDDAEEYRATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDA- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 413 LTPRIKVGRD-YVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLC 491
Cdd:cd01384 298 LCKRVIVTPDgIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFC 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 492 INYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANspGVLALLDEECWFPKATDKTFVDKLVQ 571
Cdd:cd01384 377 INLANEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEKKPG--GIIALLDEACMFPRSTHETFAQKLYQ 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 572 EQGTHSKFQKPRqlKDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVDRivgldqvagma 651
Cdd:cd01384 454 TLKDHKRFSKPK--LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR----------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 652 etafgaaYKTKKGM-FRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQG 730
Cdd:cd01384 521 -------EGTSSSSkFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAG 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 148223878 731 FPNRIVFQEFRQRYEILTPNsIPRGFMDGKQACERMIRSLELDPnlYRIGQSKIFFR 787
Cdd:cd01384 594 YPTRKPFEEFLDRFGLLAPE-VLKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
99-787 |
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: 567.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 178 GESGAGKTENTKKVIQYLAHVASSHKGkkdhtiptespkaikhqsgsllygELERQLLQANPILESFGNAKTVKNDNSSR 257
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSGAG------------------------PIEQRILEANPLLEAFGNAKTVRNNNSSR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 258 FGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNyrfvsngyipipgqq 337
Cdd:cd01382 137 FGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDPLLD--------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 338 DKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNT-------DQASMPENTAAQKlchLLGLNIMEF-- 408
Cdd:cd01382 202 DVGDFIRMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYAAE---LLGLDQDELrv 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 409 ---TRAILTPRIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKrqGASFIGILDIAGFEIFELN 485
Cdd:cd01382 279 sltTRVMQTTRGGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVN 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 486 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANspGVLALLDEECWFPKATDKTF 565
Cdd:cd01382 357 SFEQFCINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHF 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 566 VDKLVQEQGTHSKFQKPRQ--------LKDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKD 637
Cdd:cd01382 434 TSAVHQKHKNHFRLSIPRKsklkihrnLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFES 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 638 VDRIVGldqvagmaetafGAAYKTKKGMFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRC 717
Cdd:cd01382 514 STNNNK------------DSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQC 581
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 718 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNSIPRgfMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd01382 582 SGMVSVLDLMQGGFPSRTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
99-787 |
5.50e-179 |
|
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: 558.24 E-value: 5.50e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 179 ESGAGKTENTKKVIQYLAHVASSHKGkkdhtiptespkaikhqsgsllygeLERQLLQANPILESFGNAKTVKNDNSSRF 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG-------------------------VEQRVLLANPILEAFGNAKTLRNNNSSRF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 259 GKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSgeHLKSDLLLDGFNNYRFVS-NGYIPIPGQQ 337
Cdd:cd14872 136 GKWVEIHFDNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASP--DPASRGGWGSSAAYGYLSlSGCIEVEGVD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 338 DKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKLCH---LLGLNIMEFTRAILT 414
Cdd:cd14872 214 DVADFEEVVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLEEALTS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 415 PRIKV-GRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCIN 493
Cdd:cd14872 294 RLMEIkGCDPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCIN 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 494 YTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNSPGVLALLDEECWFPKATDKTFVDKLVQEQ 573
Cdd:cd14872 374 FTNEKLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTH 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 574 GTHSKFQKPRQLKDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVDrivgLDQvagmaet 653
Cdd:cd14872 451 AAKSTFVYAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSE----GDQ------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 654 afgaayKTKKGmfrTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 733
Cdd:cd14872 520 ------KTSKV---TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPF 590
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 148223878 734 RIVFQEFRQRYEILtPNSIPRGFM-DGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd14872 591 RYSHERFLKRYRFL-VKTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
99-787 |
1.86e-174 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 546.68 E-value: 1.86e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQ----DREDQS 173
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 174 ILCTGESGAGKTENTKKVIQYLAHVASSHKGKKdhtiPTESPKAIkhQSGSLLYGELERQLLQANPILESFGNAKTVKND 253
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGA----SGEGEAAS--EAIEQTLGSLEDRVLSSNPLLESFGNAKTLRND 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 254 NSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVSNGYIPI 333
Cdd:cd14890 155 NSSRFGKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 334 PGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKErntDQASMPEN-TAAQKLCH---LLGLNIMEFT 409
Cdd:cd14890 235 PSCDDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESE---NDTTVLEDaTTLQSLKLaaeLLGVNEDALE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 410 RAILTPRIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQ 489
Cdd:cd14890 312 KALLTRQLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 490 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIE-RPANSPGVLALLDeECWFPKAT--DKTFV 566
Cdd:cd14890 391 LCINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 567 DKLVQEQGT-------------HSKFQKPRQLKDKAdFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSdkfvse 633
Cdd:cd14890 469 SQLHASFGRksgsggtrrgssqHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR------ 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 634 lwkdvdrivgldqvagmaetafgaayKTKKGMfrTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLD 713
Cdd:cd14890 542 --------------------------RSIREV--SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLR 593
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148223878 714 QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNSiprgfMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd14890 594 QLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
99-787 |
1.56e-170 |
|
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: 535.87 E-value: 1.56e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 179 ESGAGKTENTKKVIQYLAHVAsshkgkkdhtiptespkaikhQSGSLLYGElerQLLQANPILESFGNAKTVKNDNSSRF 258
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN---------------------QRRNNLVTE---QILEATPLLEAFGNAKTVRNDNSSRF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 259 GKFIRINFDvTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDL-LLDGFNNYRFVSNGYIPIPGQQ 337
Cdd:cd01387 137 GKYLEVFFE-GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYgLQEAEKYFYLNQGGNCEIAGKS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 338 DKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQ---ASMPENTAAQKLCHLLGLNIMEFTRAILT 414
Cdd:cd01387 216 DADDFRRLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 415 PRIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINkALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINY 494
Cdd:cd01387 296 KVTETRRERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINY 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 495 TNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIerpANSP-GVLALLDEECWFPKATDKTFVDKLVQEQ 573
Cdd:cd01387 375 ANENLQYYFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLI---SKKPvGILHILDDECNFPQATDHSFLEKCHYHH 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 574 GTHSKFQKPRQlkDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVdrivgLDQVAGMAET 653
Cdd:cd01387 451 ALNELYSKPRM--PLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSH-----RAQTDKAPPR 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 654 AFGAAYKTKKGMFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 733
Cdd:cd01387 524 LGKGRFVTMKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPV 603
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 148223878 734 RIVFQEFRQRYEILTPNSIPRGfMDGKQACERMIRSLELDP-NLYRIGQSKIFFR 787
Cdd:cd01387 604 RLPFQVFIDRYRCLVALKLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
99-787 |
8.63e-170 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 533.97 E-value: 8.63e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 178 GESGAGKTENTKKVIQYLAHVASshkGKKDHTIptespkaikhqsgsllygeleRQLLQANPILESFGNAKTVKNDNSSR 257
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG---GLNDSTI---------------------KKIIEVNPLLESFGNAKTVRNDNSSR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 258 FGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSgeHLKSDLLLDGFNNYRFV-SNGYIPIPGQ 336
Cdd:cd14903 137 FGKFTQLQFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASP--DVEERLFLDSANECAYTgANKTIKIEGM 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 337 QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASM--PENTAAQKLCHLLGLNIMEFTRAILT 414
Cdd:cd14903 215 SDRKHFARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCS 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 415 PRIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINY 494
Cdd:cd14903 295 RTMRAAGDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINY 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 495 TNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpaNSPGVLALLDEECWFPKATDKTFVDKLVqeqG 574
Cdd:cd14903 374 ANEKLQQKFTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---S 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 575 THSKFQK----PRqlKDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDvdrIVGLDQVAGM 650
Cdd:cd14903 447 IHKDEQDviefPR--TSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKE---KVESPAAAST 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 651 AETAFGAAYKTKKGMFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQG 730
Cdd:cd14903 522 SLARGARRRRGGALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAA 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 148223878 731 FPNRIVFQEFRQRYEILTPNSiPRGFMDGKQACERMIRSLELD-PNLYRIGQSKIFFR 787
Cdd:cd14903 602 YPNRLLHEEFLDKFWLFLPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
99-787 |
4.68e-165 |
|
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: 521.94 E-value: 4.68e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 179 ESGAGKTENTKKVIQYLahVASSHKGkkdhtiptespkaikHQSGsllygeLERQLLQANPILESFGNAKTVKNDNSSRF 258
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKG---------------YGSG------VEQTILGAGPVLEAFGNAKTAHNNNSSRF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 259 GKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVS-NGYIPIPGQQ 337
Cdd:cd01385 138 GKFIQVNYRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNqSDCYTLEGED 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 338 DKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKER-NTDQASMPENTAAQKL-CHLLGLNIMEFTRAILTP 415
Cdd:cd01385 218 EKYEFERLKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDIiSELLRVKEETLLEALTTK 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 416 RIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKAL----DRTKRQGASfIGILDIAGFEIFELNSFEQLC 491
Cdd:cd01385 298 KTVTVGETLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFC 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 492 INYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANspGVLALLDEECWFPKATDKTFVDKLVQ 571
Cdd:cd01385 377 INYANEHLQYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISKKPT--GLLCLLDEESNFPGATNQTLLAKFKQ 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 572 EQGTHSKFQKPrQLKDKAdFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELwkdvdriVGLDQVA--- 648
Cdd:cd01385 454 QHKDNKYYEKP-QVMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDPVAvfr 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 649 -GMAETAFGAAY--------------------------------KTKKGMfrTVGQLYKESLAKLMATLRNTNPNFVRCI 695
Cdd:cd01385 525 wAVLRAFFRAMAafreagrrraqrtaghsltlhdrttksllhlhKKKKPP--SVSAQFQTSLSKLMETLGQAEPFFIRCI 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 696 IPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtpnsIPRGFMDGKQACERMIRSLELDPN 775
Cdd:cd01385 603 KSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRD 678
|
730
....*....|..
gi 148223878 776 LYRIGQSKIFFR 787
Cdd:cd01385 679 NYQIGKTKVFLK 690
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
99-787 |
8.75e-162 |
|
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: 511.65 E-value: 8.75e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 178 GESGAGKTENTKKVIQYLAHVASSHKGKKDHTIPTEspkaikhqsgsllygeLERQLLQANPILESFGNAKTVKNDNSSR 257
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSC----------------VEQAILESSPIMEAFGNAKTVYNNNSSR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 258 FGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVS-NGYIPIPGQ 336
Cdd:cd14873 145 FGKFVQLNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 337 QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKkerNTDQASMPENTAAQKLCHLLGLNIMEFTRAiLTPR 416
Cdd:cd14873 225 SDQESFREVITAMEVMQFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTDA-LTQR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 417 IKVGR-DYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKaldRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINY 494
Cdd:cd14873 301 SMFLRgEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINS---RIKGKEDfKSIGILDIFGFENFEVNHFEQFNINY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 495 TNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPAnspGVLALLDEECWFPKATDKTFVDKLVQEQG 574
Cdd:cd14873 378 ANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 575 THSKFQKPRQLKDkaDFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVDRivgldqvAGMAETA 654
Cdd:cd14873 454 NNHFYVKPRVAVN--NFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSS-------RNNQDTL 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 655 FGAAYKTKKgmfrTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNR 734
Cdd:cd14873 525 KCGSKHRRP----TVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVR 600
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 148223878 735 IVFQEFRQRYEILTPNSIPRGFMDGKqaCERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd14873 601 RPFQDFYKRYKVLMRNLALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-787 |
1.43e-161 |
|
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: 510.28 E-value: 1.43e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 180 SGAGKTENTKKVIQYLAhvasshkgkkdhtiptespkaikhQSGSLLYGELERQLLQANPILESFGNAKTVKNDNSSRFG 259
Cdd:cd01379 82 SGAGKTESANLLVQQLT------------------------VLGKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 260 KFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAG--SGEHLKSDLLLDGFNNYRFVSNGYIPIPGQQ 337
Cdd:cd01379 138 KYLEMKFTSTGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGlaEDKKLAKYKLPENKPPRYLQNDGLTVQDIVN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 338 D---KDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFK---KERNTDQASMPENTAA-QKLCHLLGLNIMEFTR 410
Cdd:cd01379 218 NsgnREKFEEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRISNPEAlNNVAKLLGIEADELQE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 411 AiLTPRIKVGR-DYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKAL--DRTKRQGASFIGILDIAGFEIFELNSF 487
Cdd:cd01379 298 A-LTSHSVVTRgETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 488 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCID-LIERPAnspGVLALLDEECWFPKATDKTFV 566
Cdd:cd01379 377 EQLCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLV 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 567 DKLvqEQGTHSKFQKpRQLKDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSElwkdvdrivgldq 646
Cdd:cd01379 453 EKF--HNNIKSKYYW-RPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 647 vagmaetafgaayktkkgmfrTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRI 726
Cdd:cd01379 517 ---------------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRI 575
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148223878 727 CRQGFPNRIVFQEFRQRYEIL--TPNSIPRGfmdGKQACERMIRSLELDPnlYRIGQSKIFFR 787
Cdd:cd01379 576 RRQGFSHRILFADFLKRYYFLafKWNEEVVA---NRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
99-785 |
2.51e-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: 510.49 E-value: 2.51e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMY------RGKKRHEMPPHIYAISESAYRCMLQDRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 171 --DQSILCTGESGAGKTENTKKVIQYLAHVASSHkgkkdhtipTESPKAIKHQSgsllygeLERQLLQANPILESFGNAK 248
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSAT---------THGQNATEREN-------VRDRVLESNPILEAFGNAR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 249 TVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFV-- 326
Cdd:cd14901 145 TNRNNNSSRFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLns 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 327 SNGYIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVF-KKERNTDQASMPENTAAQKLCHLLGLNI 405
Cdd:cd14901 225 SQCYDRRDGVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDM 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 406 MEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKRQGAS-FIGILDIAGFEIFEL 484
Cdd:cd14901 305 DVLEKTLCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFAT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 485 NSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgldlqP----CIDLIErpANSPGVLALLDEECWFPKA 560
Cdd:cd14901 385 NSLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLFSLLDEQCLLPRG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 561 TDKTFVDKLVQEQGTHSKFQKPRQLKDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSElwkdvdr 640
Cdd:cd14901 458 NDEKLANKYYDLLAKHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 641 ivgldqvagmaetafgaayktkkgmfrTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGV 720
Cdd:cd14901 531 ---------------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGV 583
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148223878 721 LEGIRICRQGFPNRIVFQEFRQRYEILTPNSIPRGFMDGKQACERMIR------SLELDPNLYrIGQSKIF 785
Cdd:cd14901 584 LEAVKISRSGYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQlqhselNIEHLPPFQ-VGKTKVF 653
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
99-749 |
7.48e-160 |
|
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: 506.92 E-value: 7.48e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRgKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 178 GESGAGKTENTKKVIQYLAHVASSHKGKKDhtiptespkaikhqsgsllygELERQLLQANPILESFGNAKTVKNDNSSR 257
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS---------------------LVEAQVLESNPLLEAFGNARTLRNDNSSR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 258 FGKFIRINFDVT---------GYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVSN 328
Cdd:cd14888 139 FGKFIELQFSKLkskrmsgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 329 GYIP------------------------IPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTD 384
Cdd:cd14888 219 DAKPisidmssfephlkfryltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 385 QASMPENTAAQKL---CHLLGLNIMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALD 461
Cdd:cd14888 299 EGAVVSASCTDDLekvASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 462 RTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErp 541
Cdd:cd14888 379 YSKDNSLLFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ-- 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 542 ANSPGVLALLDEECWFPKATDKTFVDKLVQEQGTHSKFQKPRqlKDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVAT 621
Cdd:cd14888 456 EKPLGIFCMLDEECFVPGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQE 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 622 LLHQSSDKFVSELWKD-VDRIVGLdqvagmaetafgaayKTKKGMFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHE 700
Cdd:cd14888 534 VIKNSKNPFISNLFSAyLRRGTDG---------------NTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQ 598
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 148223878 701 KRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 749
Cdd:cd14888 599 NVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
99-787 |
7.80e-156 |
|
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: 494.59 E-value: 7.80e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKK-RHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 178 GESGAGKTENTKKVIQYLAHVASShkgkkDHTiptespkaikhqsgsllygELERQLLQANPILESFGNAKTVKNDNSSR 257
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPS-----DDS-------------------DLLDKIVQINPLLEAFGNASTVMNDNSSR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 258 FGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVSNGYIPIPGQQ 337
Cdd:cd14897 137 FGKFIELHFTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFN 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 338 D-------KDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGLNIMEFTR 410
Cdd:cd14897 217 DseeleyyRQMFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 411 AILTPRIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKAL----DRTKRQGASFIGILDIAGFEIFELNS 486
Cdd:cd14897 297 ALISNVNTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 487 FEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERpaNSPGVLALLDEECWFPKATDKTFV 566
Cdd:cd14897 377 FDQLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLV 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 567 DKLVQEQGTHSKFQKPrqLKDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKdvdrivgldq 646
Cdd:cd14897 454 QKLNKYCGESPRYVAS--PGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT---------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 647 vagmaetafgaayktkkgmfrtvgQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRI 726
Cdd:cd14897 522 ------------------------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKI 577
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148223878 727 CRQGFPNRIVFQEFRQRYEILTPNSiPRGFMDGKQACERMIRSLELDPnlYRIGQSKIFFR 787
Cdd:cd14897 578 RRDGYPIRIKYEDFVKRYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
99-787 |
1.25e-155 |
|
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: 495.05 E-value: 1.25e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEM---PPHIYAISESAYRCMLQDR----ED 171
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 172 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGKKDHTIPTESPKAIkhqsgsllygelERQLLQANPILESFGNAKTVK 251
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAHESI------------EECVLLSNLILEAFGNAKTIR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 252 NDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVSNG-Y 330
Cdd:cd14892 149 NDNSSRFGKYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGnC 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 331 IPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFkkERNTDQ----ASMPENTAAQKLCHLLGLNIM 406
Cdd:cd14892 229 VEVDGVDDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 407 EFTRAILTPRIKVGRDYV-QKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKRQ---------GASFIGILDI 476
Cdd:cd14892 307 ELMFKLVTQTTSTARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 477 AGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPansP-GVLALLDEEC 555
Cdd:cd14892 387 FGFEIMPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK---PlGLLPLLEEQM 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 556 WFP-KATDKTFVDKLVQEQ-GTHSKFQKPRQLKDkaDFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDkfvse 633
Cdd:cd14892 463 LLKrKTTDKQLLTIYHQTHlDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK----- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 634 lwkdvdrivgldqvagmaetafgaayktkkgmFRTvgqlykeSLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLD 713
Cdd:cd14892 536 --------------------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRD 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 714 QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNSipRGFMDGKQACE--------RMIRSLELDPNLYRIGQSKIF 785
Cdd:cd14892 577 QLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLARNK--AGVAASPDACDattarkkcEEIVARALERENFQLGRTKVF 654
|
..
gi 148223878 786 FR 787
Cdd:cd14892 655 LR 656
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
100-754 |
7.41e-145 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 464.01 E-value: 7.41e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY-----------RGKKRHEMPPHIYAISESAYRCM-- 165
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 166 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHVasshkGKKDHTIPTESPKAIKHQSGsllygelerQLLQANPILES 243
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQA-----GDNNLAASVSMGKSTSGIAA---------KVLQTNILLES 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 244 FGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEhlksdllldgfnny 323
Cdd:cd14900 148 FGNARTLRNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE-------------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 324 rfvsngyipipGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTD-QASMPENTAAQKL----- 397
Cdd:cd14900 214 -----------AARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrda 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 398 -CHLLGLNIMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKAL---DRTKRQGAS-FIG 472
Cdd:cd14900 283 aATLLSVDATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 473 ILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLI-ERPAnspGVLALL 551
Cdd:cd14900 363 ILDIFGFEVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIsQRPT---GILSLI 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 552 DEECWFPKATDKTFVDKLVQEQGTHSKFQKPRQLKDKADFCIIHYAGRVDYKADEWLLKNMDplndnvatLLHQSSdkfv 631
Cdd:cd14900 439 DEECVMPKGSDTTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQEA---- 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 632 selwkdVDrivgldqvagmaetafgaayktkkgMFRTVGQlYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLV 711
Cdd:cd14900 507 ------VD-------------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERV 554
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 148223878 712 LDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNSIPR 754
Cdd:cd14900 555 LNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSLARAKNRL 597
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
101-787 |
1.34e-143 |
|
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: 461.68 E-value: 1.34e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 101 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML----QDREDQSILC 176
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 177 TGESGAGKTENTKKVIQYLAHVASSHKgkkdhtiptespkaikhqsgsllygELERQLLQANPILESFGNAKTVKNDNSS 256
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELCRGNS-------------------------QLEQQILQVNPLLEAFGNAQTVMNDNSS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 257 RFGKFIRINFDvTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAG-SGEHLKSDLLLDGfNNYRFVSNGYipipG 335
Cdd:cd14889 138 RFGKYIQLRFR-NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGiSAEDRENYGLLDP-GKYRYLNNGA----G 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 336 QQD-----KDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFkkERNTDQASMPENTAAQKL---CHLLGLNIME 407
Cdd:cd14889 212 CKRevqywKKKYDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEALKVENDSNGWLkaaAGQFGVSEED 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 408 FTRAiLTPRIKVGR-DYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKRQG--ASFIGILDIAGFEIFEL 484
Cdd:cd14889 290 LLKT-LTCTVTFTRgEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 485 NSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIerpANSP-GVLALLDEECWFPKATDK 563
Cdd:cd14889 369 NRFEQACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLF---LNKPiGILSLLDEQSHFPQATDE 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 564 TFVDKLVQEQGTHSKFQKPRQLKDKadFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWK-DVDRIV 642
Cdd:cd14889 445 SFVDKLNIHFKGNSYYGKSRSKSPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTaTRSRTG 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 643 GLDQVAGMAETAFGAAYKTKKgmfRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLE 722
Cdd:cd14889 523 TLMPRAKLPQAGSDNFNSTRK---QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLE 599
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148223878 723 GIRICRQGFPNRIVFQEFRQRYEIL--TPNsIPrgfmDGKQACERMIRSLELDPnlYRIGQSKIFFR 787
Cdd:cd14889 600 TIRIRREGFSWRPSFAEFAERYKILlcEPA-LP----GTKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-787 |
1.58e-141 |
|
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: 455.66 E-value: 1.58e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRyySGLI----YTYSGLFCVVINPYKNLPiysENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE---D 171
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 172 QSILCTGESGAGKTENTKKVIQYLAHvaSSHKGKKDHTIPTESPKAIKHQSGSllygELERQLLQANPILESFGNAKTVK 251
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTT--RAVGGKKASGQDIEQSSKKRKLSVT----SLDERLMDTNPILESFGNAKTLR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 252 NDNSSRFGKFIRINFDVTGY-IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVS-NG 329
Cdd:cd14891 150 NHNSSRFGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 330 YIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQK----LCHLLGLNI 405
Cdd:cd14891 230 CVSDDNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAEIASESDKEalatAAELLGVDE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 406 MEFTRAILTPRIkVGRDYVQKAQ-TKEQADFAVEALRKATYERLFRWLVYRINKALDRtKRQGASFIGILDIAGFEIFEL 484
Cdd:cd14891 310 EALEKVITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFET 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 485 -NSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIerpANSP-GVLALLDEECWFPKATD 562
Cdd:cd14891 388 kNDFEQLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLI---ASKPnGILPLLDNEARNPNPSD 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 563 KTFVDKLVQEQGTHSKFQKPRQlKDKAD-FCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHqSSDKFvselwkdvdri 641
Cdd:cd14891 464 AKLNETLHKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLA-SSAKF----------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 642 vgLDQVAGMAEtafgaayktkkgmfrtvgqlykeslaklmaTLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVL 721
Cdd:cd14891 531 --SDQMQELVD------------------------------TLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGIL 578
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148223878 722 EGIRICRQGFPNRIVFQEFRQRYEILTPNSIPRGFMDGKQA-CERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd14891 579 QTCEVLKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
99-750 |
4.26e-140 |
|
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: 452.56 E-value: 4.26e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH--------EMPPHIYAISESAYRCMLQDR 169
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 170 EDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGKKDHTIPTESPKAIKHQSGSLlygelERQLLQANPILESFGNAKT 249
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSSIRATSKSTKSI-----EQKILSCNPILEAFGNAKT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 250 VKNDNSSRFGKFIRINFD-VTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLD----GFNNYR 324
Cdd:cd14907 156 VRNDNSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKnqlsGDRYDY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 325 FVSNGYIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFK-KERNTDQASMPENTAA-QKLCHLLG 402
Cdd:cd14907 236 LKKSNCYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDdSTLDDNSPCCVKNKETlQIIAKLLG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 403 LNIMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKAL-------DRTKRQGASFIGILD 475
Cdd:cd14907 316 IDEEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 476 IAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WNFIDFgLDLQPCIDLIERPANspGVLALLDE 553
Cdd:cd14907 396 IFGFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKPPI--GIFNLLDD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 554 ECWFPKATDKTFVDKLVQEQGTHSKFQKPRQLKdKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSE 633
Cdd:cd14907 473 SCKLATGTDEKLLNKIKKQHKNNSKLIFPNKIN-KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISS 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 634 LWKDVDRIvgldqvagmaETAFGAAYKTKKGMFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLD 713
Cdd:cd14907 552 IFSGEDGS----------QQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLN 621
|
650 660 670
....*....|....*....|....*....|....*..
gi 148223878 714 QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 750
Cdd:cd14907 622 QIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
99-787 |
2.05e-136 |
|
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276869 Cd Length: 653 Bit Score: 441.69 E-value: 2.05e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 178 GESGAGKTENTKKVIQYLAHVASshkGKKDHTIPtespkaikhqsgsllygelerQLLQANPILESFGNAKTVKNDNSSR 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA---------------------KVIDVNPLLESFGNAKTTRNDNSSR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 258 FGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFV--SNGYIPIPG 335
Cdd:cd14904 137 FGKFTQLQFDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 336 QQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKerNTDQASMPENTAA-QKLCHLLGLNIMEFTRAILT 414
Cdd:cd14904 217 LDDAKLFASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDK--SDENGSRISNGSQlSQVAKMLGLPTTRIEEALCN 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 415 PRIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINY 494
Cdd:cd14904 295 RSVVTRNESVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINY 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 495 TNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpaNSPGVLALLDEECWFPKATDKTFVDKL---VQ 571
Cdd:cd14904 375 ANEKLQQKFTTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQ 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 572 EQGTHSKFQKPRQlkDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVDrivgldqvaGMA 651
Cdd:cd14904 451 TKKDNESIDFPKV--KRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE---------APS 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 652 ETAFGAAYKTKKGMfRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGF 731
Cdd:cd14904 520 ETKEGKSGKGTKAP-KSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGY 598
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 148223878 732 PNRIVFQEFRQRYEILTPNSIPRGfmDGKQACERMIRSL-ELDPNLYRIGQSKIFFR 787
Cdd:cd14904 599 PSRLTPKELATRYAIMFPPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-787 |
9.30e-133 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 431.13 E-value: 9.30e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 179 ESGAGKTENTKKVIQYLAHVASSHKGKKdhtiptespkaikhqsgsllygelERQLLQANPILESFGNAKTVKNDNSSRF 258
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQTEDR------------------------LRQPEDVLPILESFGHAKTILNANASRF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 259 GKFIRINFDvTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVSNGYI-PIPGQQ 337
Cdd:cd14896 137 GQVLRLHLQ-HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 338 DKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQ--ASMPENTAAQKLCHLLGLNiMEFTRAILTP 415
Cdd:cd14896 216 DAQDFEGLLKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVP-PERLEGAVTH 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 416 RIKV-GRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKRQGA-SFIGILDIAGFEIFELNSFEQLCIN 493
Cdd:cd14896 295 RVTEtPYGRVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCIN 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 494 YTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDfGLDLQPCIDLIerpANSP-GVLALLDEECWFPKATDKTFVDKLVQE 572
Cdd:cd14896 375 LASERLQLFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLL---VDQPhSLLSILDDQTWLSQATDHTFLQKCHYH 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 573 QGTHSKFQKPRQlkDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVDRIVGLDQVAGMAE 652
Cdd:cd14896 451 HGDHPSYAKPQL--PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKPTLA 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 653 TAFgaayktkkgmfrtvgqlyKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFP 732
Cdd:cd14896 529 SRF------------------QQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFP 590
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 148223878 733 NRIVFQEFRQRYEILTPNSIPrGFMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd14896 591 VRVPFQAFLARFGALGSERQE-ALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
99-749 |
5.64e-131 |
|
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: 428.54 E-value: 5.64e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYR--------GKKRHEMPPHIYAISESAYRCMLQ-D 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 169 REDQSILCTGESGAGKTENTKKVIQYLAHVASShkgkkdhTIPTESPKaikhqSGSLlygELERQLLQANPILESFGNAK 248
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRD-------QSSTEQEG-----SDAV---EIGKRILQTNPILESFGNAQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 249 TVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVsN 328
Cdd:cd14902 146 TIRNDNSSRFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELL-N 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 329 GYIP----IPGQQDKDN--FQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKE-RNTDQASMPENTAAQ--KLCH 399
Cdd:cd14902 225 SYGPsfarKRAVADKYAqlYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAEnGQEDATAVTAASRFHlaKCAE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 400 LLGLNIMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALD--------RTKRQGASFI 471
Cdd:cd14902 305 LMGVDVDKLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 472 GILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANspGVLALL 551
Cdd:cd14902 385 GILDIFGFESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 552 DEECWFPKATDKTFVDKLVQEQGTHSKfqkprqlkdkadFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFV 631
Cdd:cd14902 462 DQECLMPKGSNQALSTKFYRYHGGLGQ------------FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVV 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 632 SELwkdvdrivGLDQVAGMAETAFGAAYKTKKGMFRT--VGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPH 709
Cdd:cd14902 530 VAI--------GADENRDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRE 601
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 148223878 710 LVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 749
Cdd:cd14902 602 RMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-749 |
9.99e-131 |
|
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: 426.63 E-value: 9.99e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR--GKKRHE-------MPPHIYAISESAYRCMLQD- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 169 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGkkdhtiptespkaIKHQSGSLLYGELERQLLQANPILESFGNAK 248
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEG-------------APNEGEELGKLSIMDRVLQSNPILEAFGNAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 249 TVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGE--------HLKSDLLLDGF 320
Cdd:cd14908 148 TLRNDNSSRFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEeehekyefHDGITGGLQLP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 321 NNYRFVSNGYIPIPGQ-QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPE---NTAAQK 396
Cdd:cd14908 228 NEFHYTGQGGAPDLREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEegnEKCLAR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 397 LCHLLGLNIMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKAL--DRTKRQGASfIGIL 474
Cdd:cd14908 308 VAKLLGVDVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSS-VGVL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 475 DIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANSPGVLALLDEE 554
Cdd:cd14908 387 DIFGFECFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDE 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 555 CWFP-KATDKTFVDKLV--------QEQGTHSKFQKPRQLKDKADFCIIHYAGRVDYKADE-WLLKNMDPLNdnvatllh 624
Cdd:cd14908 464 CRLGiRGSDANYASRLYetylpeknQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETtFCEKNKDEIP-------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 625 qssdkfvselwkdvdrivgldqvagmaetafgaayKTKKGMFRTvGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAG 704
Cdd:cd14908 536 -----------------------------------LTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPD 579
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 148223878 705 KLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 749
Cdd:cd14908 580 LVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP 624
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
100-748 |
5.78e-130 |
|
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: 425.14 E-value: 5.78e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPiyseniiEMYRGKKRHE-------MPPHIYAISESAYRCMLQ----- 167
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 168 --DREDQSILCTGESGAGKTENTKKVIQYLAHVASshkgkkdHTIPTESPKAIKHQSGSllygelerQLLQANPILESFG 245
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAESSK-------HTTATSSSKRRRAISGS--------ELLSANPILESFG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 246 NAKTVKNDNSSRFGKFIRINF-----DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGF 320
Cdd:cd14895 140 NARTLRNDNSSRFGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 321 N--NYRFVSNG--YIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTD------------ 384
Cdd:cd14895 220 SaqEFQYISGGqcYQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapc 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 385 ---QASMPENTAAQKL---CHLLGLNIMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINK 458
Cdd:cd14895 300 rlaSASPSSLTVQQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNS 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 459 ALDRTK----------RQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFG 528
Cdd:cd14895 380 ASPQRQfalnpnkaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 529 LDlQPCIDLIE-RPAnspGVLALLDEECWFPKATDKTFVDKLVQEQGTHSKFQKPRqlKDKAD--FCIIHYAGRVDYKAD 605
Cdd:cd14895 460 DN-SVCLEMLEqRPS---GIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAE 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 606 EWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVDRIVGLDQVAGMAETAFGAAYKTKKGmfrtVGQLYKESLAKLMATLR 685
Cdd:cd14895 534 GFCEKNKDQPNAELFSVLGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSSVG----IGSQFKQQLASLLDVVQ 609
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148223878 686 NTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 748
Cdd:cd14895 610 QTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
97-840 |
1.81e-128 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 424.83 E-value: 1.81e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 97 NEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHE-MPPHIYAISESAYRCMLQDREDQSIL 175
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 176 CTGESGAGKTENTKKVIQYLAhvaSSHKGKKDHTIPTespkaikhqsgsllygelerQLLQANPILESFGNAKTVKNDNS 255
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA---SSKSGNMDLKIQN--------------------AIMAANPVLEAFGNAKTIRNNNS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 256 SRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVSNGYIPIPG 335
Cdd:PTZ00014 245 SRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPG 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 336 QQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVF--KKERNTDQASM--PENTAA-QKLCHLLGLNIMEFTR 410
Cdd:PTZ00014 325 IDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESLEVfNEACELLFLDYESLKK 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 411 AILTPRIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKRQGAsFIGILDIAGFEIFELNSFEQL 490
Cdd:PTZ00014 405 ELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQL 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 491 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANSpgVLALLDEECWFPKATDKTFVDKLV 570
Cdd:PTZ00014 484 FINITNEMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGKS--VLSILEDQCLAPGGTDEKFVSSCN 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 571 QEQGTHSKFQKPRQLKDKaDFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVDRIVGldqvagm 650
Cdd:PTZ00014 561 TNLKNNPKYKPAKVDSNK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKG------- 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 651 aetafgaayKTKKGMFrtVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQG 730
Cdd:PTZ00014 633 ---------KLAKGQL--IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLG 701
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 731 FPNRIVFQEFRQRYEILTPNSIPRGFMDGKQACERMIRSLELDPNLYRIGQSKIFFR---AGVLAHLEEERDLKITDIIV 807
Cdd:PTZ00014 702 FSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVS 781
|
730 740 750
....*....|....*....|....*....|...
gi 148223878 808 LFQAVCRGYLARKAFAKKqqqliaLKVLQRNCA 840
Cdd:PTZ00014 782 VLEALILKIKKKRKVRKN------IKSLVRIQA 808
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-785 |
1.06e-123 |
|
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: 405.53 E-value: 1.06e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 178 GESGAGKTENTKKVIQYLAhvaSSHKGKKDHTIPTespkAIkhqsgsllygelerqlLQANPILESFGNAKTVKNDNSSR 257
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMDLRIQT----AI----------------MAANPVLEAFGNAKTIRNNNSSR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 258 FGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVSNGYIPIPGQQ 337
Cdd:cd14876 138 FGRFMQLDVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGID 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 338 DKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVF--KKERNTDQASMPENTAAQKL---CHLLGLNIMEFTRAI 412
Cdd:cd14876 218 DVADFEEVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKItgKTEQGVDDAAAISNESLEVFkeaCSLLFLDPEALKREL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 413 LTPRIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDrtKRQG-ASFIGILDIAGFEIFELNSFEQLC 491
Cdd:cd14876 298 TVKVTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLF 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 492 INYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANSpgVLALLDEECWFPKATDKTFVDKLVQ 571
Cdd:cd14876 376 INITNEMLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGKS--VLSILEDQCLAPGGSDEKFVSACVS 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 572 EQGTHSKFqKPRQLKDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVDRIVGldqvagma 651
Cdd:cd14876 453 KLKSNGKF-KPAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKG-------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 652 etafgaayKTKKGMFrtVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGF 731
Cdd:cd14876 524 --------KIAKGSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGY 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 148223878 732 PNRIVFQEFRQRYEILTPNSIPRGFMDGKQACERMIRSLELDPNLYRIGQSKIF 785
Cdd:cd14876 594 SYRRPFEEFLYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
99-787 |
1.30e-123 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 406.70 E-value: 1.30e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 179 ESGAGKTENTKKVIQYLAHVASShkgkkdhtiptespkaikhQSGSLLYGELErqllQANPILESFGNAKTVKNDNSSRF 258
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGS-------------------VGGVLSVEKLN----AALTVLEAFGNVRTALNGNATRF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 259 GKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLD--GFNNYRFVSNGYIPIPGQ 336
Cdd:cd01386 138 SQLFSLDFDQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNqlAESNSFGIVPLQKPEDKQ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 337 QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGLNIMEFTRAI---- 412
Cdd:cd01386 218 KAAAAFSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhh 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 413 --------LTPRIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKRQGASfIGILDIAGFEIFEL 484
Cdd:cd01386 298 lsggpqqsTTSSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSS-ITIVDTPGFQNPAH 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 485 N------SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIER-PANSP-----------G 546
Cdd:cd01386 377 SgsqrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQaPQQALvrsdlrdedrrG 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 547 VLALLDEECWFPKATDKTFVDKLVQEQG--THSKFQKPRQLKDKA-DFCIIHYAGR--VDYKADEWLLK-NMDPLNDNVA 620
Cdd:cd01386 457 LLWLLDEEALYPGSSDDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNAT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 621 TLLHQSSDKFvselwkdvdrivgldqvagmaetafgAAYKtKKGMFRTVgqlyKESLAKLMATLRNTNPNFVRCIIPNH- 699
Cdd:cd01386 537 QLLQESQKET--------------------------AAVK-RKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQHn 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 700 -EKRAGK----------LDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP-----NSIPRGFMDGKQAC 763
Cdd:cd01386 586 aGKDERStsspaagdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPpltkkLGLNSEVADERKAV 665
|
730 740
....*....|....*....|....
gi 148223878 764 ERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd01386 666 EELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
99-749 |
1.79e-113 |
|
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: 376.50 E-value: 1.79e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDRE--DQSI 174
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 175 LCTGESGAGKTENTKKVIQYLAHVASSHKGKKDHTIPTEspkaikhqsgsllygeLERQLLQANPILESFGNAKTVKNDN 254
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAER----------------IEQRILNSNPVMEAFGNACTLRNNN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 255 SSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRfvsngYIPIP 334
Cdd:cd14880 145 SSRFGKFIQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFS-----WLPNP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 335 GQQ-DKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTA---AQKLCHLLGLNIMEFTR 410
Cdd:cd14880 220 ERNlEEDCFEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 411 AILTPRIKVGRDYV--QKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKRQGASFIGILDIAGFEIFELNSFE 488
Cdd:cd14880 300 TLQIRTIRAGKQQQvfKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 489 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANSPGVLALLDEECWFPKATDKTFVDK 568
Cdd:cd14880 380 QLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQT 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 569 LVQEQGTHSKFQKPRQLKDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVDRIVGLDQVA 648
Cdd:cd14880 457 RIESALAGNPCLGHNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPS 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 649 GMAETAfgaayktkkgmFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICR 728
Cdd:cd14880 537 GQSRAP-----------VLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISA 605
|
650 660
....*....|....*....|.
gi 148223878 729 QGFPNRIVFQEFRQRYEILTP 749
Cdd:cd14880 606 AGFPIRVSHQNFVERYKLLRR 626
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
99-750 |
2.35e-112 |
|
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: 375.47 E-value: 2.35e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDREDQSILC 176
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 177 TGESGAGKTENTKKVIQYLAHVASSHKGKKDHtiptespkaIKHQSGSLlygelERQLLQANPILESFGNAKTVKNDNSS 256
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQNNN---------NNNNNNSI-----EKDILTSNPILEAFGNSRTTKNHNSS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 257 RFGKFIRINFDVTGYIV-GANIETYLLEKSR-AVRQAKDERTFHIFYQLLAGSGehlKSDLLLDGFNN----YRFV---- 326
Cdd:cd14906 147 RFGKFLKIEFRSSDGKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGAS---KDERSKWGLNNdpskYRYLdard 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 327 ----------SNGYIPIPGQQDKD-NFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQAS--MPENTA 393
Cdd:cd14906 224 dvissfksqsSNKNSNHNNKTESIeSFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 394 A-QKLCHLLGLNIMEFTRAILTPRIKV-GRDYVQ-KAQTKEQADFAVEALRKATYERLFRWLVYRINKALDR-------- 462
Cdd:cd14906 304 SlESVSKLLGYIESVFKQALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndla 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 463 --TKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIER 540
Cdd:cd14906 384 ggSNKKNNLFIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 541 paNSPGVLALLDEECWFPKATDKTFVDKLVQE-QGTHSKFQkpRQLKdKADFCIIHYAGRVDYKADEWLLKNMDPLNDNV 619
Cdd:cd14906 463 --KSDGILSLLDDECIMPKGSEQSLLEKYNKQyHNTNQYYQ--RTLA-KGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDV 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 620 ATLLHQSSDKFVSELWKdvdrivgldqvagMAETAFGAAYKTKKGMFRTVGQlYKESLAKLMATLRNTNPNFVRCIIPNH 699
Cdd:cd14906 538 EDLLLASSNFLKKSLFQ-------------QQITSTTNTTKKQTQSNTVSGQ-FLEQLNQLIQTINSTSVHYIRCIKPNQ 603
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 148223878 700 EKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 750
Cdd:cd14906 604 TMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
99-787 |
1.46e-110 |
|
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: 368.06 E-value: 1.46e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH-----EMPPHIYAISESAYRCMLQDREDQ 172
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 173 SILCTGESGAGKTENTKKVIQYLAHVASSHKGKkdhtiptespkaikhqsgsllygeLERQLLQANPILESFGNAKTVKN 252
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSSTD------------------------VQSLILGSNPLLESFGNAKTLRN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 253 DNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVSNGYI- 331
Cdd:cd14886 137 NNSSRFGKFIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCy 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 332 PIPGQQDKDNFQETMEAMHIMgFSHEEILSMLKVVSSVLQFGNIVFKKERN--TDQASMPENTAA-QKLCHLLGLNIMEF 408
Cdd:cd14886 217 DAPGIDDQKEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 409 TRAILTPRIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKAL---DRTKRqgasFIGILDIAGFEIFELN 485
Cdd:cd14886 296 AQAIITKVVVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfdADARP----WIGILDIYGFEFFERN 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 486 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanSPGVLALLDEECWFPKATDKTF 565
Cdd:cd14886 372 TYEQLLINYANERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKP--NLSIFSFLEEQCLIQTGSSEKF 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 566 VdklvqeQGTHSKFQKPRQLKDKA---DFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVDRIV 642
Cdd:cd14886 449 T------SSCKSKIKNNSFIPGKGsqcNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNED 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 643 GLdqvagmaetafgaayktKKGMFrtVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLE 722
Cdd:cd14886 523 GN-----------------MKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFE 583
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148223878 723 GIRICRQGFPNRIVFQEFRQRYEILT--PNSIPRGFMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd14886 584 SIQTIHRGFAYNDTFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
99-787 |
3.52e-110 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 367.21 E-value: 3.52e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYS-GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRG-KKRHEMPPHIYAISESAYRCM-LQDREDQSIL 175
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 176 CTGESGAGKTENTKKVIQYLAHVASSHKGkkdhtipTESPKAIKHQsgsllygeLERQLLQANPILESFGNAKTVKNDNS 255
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSS-------NTSQRSIADK--------IDENLKWSNPVMESFGNARTVRNDNS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 256 SRFGKFIRINFD-VTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDL-LLDGFNNYR-------FV 326
Cdd:cd14875 146 SRFGKYIKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKclnggntFV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 327 SNGyipIPGQ--QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNtDQASMPENTAAQKLCHLLGLN 404
Cdd:cd14875 226 RRG---VDGKtlDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 405 IMEFTRAILtprIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALD-RTKRQGASFIGILDIAGFEIFE 483
Cdd:cd14875 302 PAKLRECFL---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFT 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 484 LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANSPGVLALLDEECWFPKATDK 563
Cdd:cd14875 379 RNSFEQLCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 564 TFVDKLVQEQGTHSK-FQKPRQLKDKaDFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELwkdvdriv 642
Cdd:cd14875 456 RFTTNLWDQWANKSPyFVLPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTL-------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 643 gLDQVAGMAETAfgaayktkkgmfRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLE 722
Cdd:cd14875 527 -LSTEKGLARRK------------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQ 593
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148223878 723 GIRICRQGFPNRIVFQEFRQRYEILTPNSIPRGFMDGK--QACERMIRSLE-----LDPNlYRIGQSKIFFR 787
Cdd:cd14875 594 TIALKRQGYPVRRPIEQFCRYFYLIMPRSTASLFKQEKysEAAKDFLAYYQrlygwAKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
99-744 |
1.19e-105 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 355.94 E-value: 1.19e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY----------RGKKRHEMPPHIYAISESAYRCMLQ 167
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 168 DREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGKKDHTIPTESPKAIKHQSgsllygeLERQLLQANPILESFGNA 247
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISPPASPSRTT-------IEEQVLQSNPILEAFGNA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 248 KTVKNDNSSRFGKFIRINF-DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAG-----SGEHLKSDLLLDGFN 321
Cdd:cd14899 154 RTVRNDNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 322 NYRFVSNGYIPI--PGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVF-----KKERNT--DQASMPENT 392
Cdd:cd14899 234 SFRLLNQSLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVMSST 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 393 AA-----QKLCHLLGLNIMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRT---- 463
Cdd:cd14899 314 TGafdhfTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasap 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 464 ----------KRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQP 533
Cdd:cd14899 394 wgadesdvddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRA 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 534 CIDLIE-RPAnspGVLALLDEECWFPKATDKTFVDKL---VQEQGTHSKFQKPRQLKDKADFCIIHYAGRVDYKADEWLL 609
Cdd:cd14899 473 CLELFEhRPI---GIFSLTDQECVFPQGTDRALVAKYyleFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLA 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 610 KNMDPLNDNVATLLHQSSDKFVSEL-WKDVDRIVGLDQVAGMAETAFGAAYKTKKGMFrTVGQLYKESLAKLMATLRNTN 688
Cdd:cd14899 550 KNKDSFCESAAQLLAGSSNPLIQALaAGSNDEDANGDSELDGFGGRTRRRAKSAIAAV-SVGTQFKIQLNELLSTVRATT 628
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 148223878 689 PNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 744
Cdd:cd14899 629 PRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
99-787 |
7.64e-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: 7.64e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYS--------GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 171 DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGKKDHTiptespkaikhqsgsllygeLERQLLQANPILESFGNAKTV 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG--------------------LEARLLQSGPVLEAFGNAHTV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 251 KNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFvsngy 330
Cdd:cd14887 141 LNANSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAGEGDPEST----- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 331 ipipgqqDKDNFQETMEAMHIMGFSHEEIlsmLKVVSSVLQFGNIVFKKERNTDQASMPENTA--------AQKLCHLL- 401
Cdd:cd14887 216 -------DLRRITAAMKTVGIGGGEQADI---FKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSe 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 402 ------GLNIMEFTRAILT--------PRIKVGRDYV------------QKAQTKEQADFAVEALRKATYERLFRWLVYR 455
Cdd:cd14887 286 vkclssGLKVTEASRKHLKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVAR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 456 INKALDRTKR-------------QGASFIGILDIAGFEIFE---LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREG 519
Cdd:cd14887 366 INAGLQRSAKpsesdsdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEG 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 520 IEWNFI--DFGLDLQPCIDLIERPANS---------------------PGVLALLDE------ECWFPKATDKTFVDKLV 570
Cdd:cd14887 446 VFQNQDcsAFPFSFPLASTLTSSPSSTspfsptpsfrsssafatspslPSSLSSLSSslssspPVWEGRDNSDLFYEKLN 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 571 QEQGTHSKFQK--PRQLKDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLhQSSDKFVSElwkdvdriVGLDQVA 648
Cdd:cd14887 526 KNIINSAKYKNitPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYTRL--------VGSKKNS 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 649 GMaetafgAAYKTKKgmfRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICR 728
Cdd:cd14887 597 GV------RAISSRR---STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMA 667
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 148223878 729 QGFPNRIVFQEFRQRYEILTPNSIpRGFMDGKQACERMIRSLELDPNLYRIGQSKIFFR 787
Cdd:cd14887 668 DGFPCRLPYVELWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
96-786 |
1.65e-93 |
|
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: 318.34 E-value: 1.65e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 96 LNEASVLHNLKDRYYSGLIYTY---SGLfcVVINPYKNLPIYSENIIEMYR-------GKKRHEMPPHIYAISESAYRCM 165
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 166 LQDREDQSILCTGESGAGKTENTKKVIQYLAHVaSSHkgkkdhtipteSPKAIKHQSgsllygelerQLLQANPILESFG 245
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRL-SSH-----------SKKGTKLSS----------QISAAEFVLDSFG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 246 NAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRF 325
Cdd:cd14879 137 NAKTLTNPNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 326 V--SNGY--IPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVF--KKERNTDQASMpENTAA-QKLC 398
Cdd:cd14879 217 LasYGCHplPLGPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVV-KNTDVlDIVA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 399 HLLGLNIMEFtRAILTPRIK-VGRD----YVQKAQTKEQADFAVEALrkatYERLFRWLVYRINKALDRTKRQGASFIGI 473
Cdd:cd14879 296 AFLGVSPEDL-ETSLTYKTKlVRKElctvFLDPEGAAAQRDELARTL----YSLLFAWVVETINQKLCAPEDDFATFISL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 474 LDIAGFEIF---ELNSFEQLCINYTNEKLQ-----QLFNHTMFILEQEEYQREGIEWNfidfglDLQPCIDLIERPANsp 545
Cdd:cd14879 371 LDFPGFQNRsstGGNSLDQFCVNFANERLHnyvlrSFFERKAEELEAEGVSVPATSYF------DNSDCVRLLRGKPG-- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 546 GVLALLDEEC-WFPKATDKTFVDKLVQEQGTHSKFQKPRQLKDKAD---FCIIHYAGRVDYKADEWLLKNMDPLndnvat 621
Cdd:cd14879 443 GLLGILDDQTrRMPKKTDEQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVL------ 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 622 llhqSSDkFVSelwkdvdrivgldqvagmaetafgaayktkkgMFRTVGQLyKESLAKLMATLRNTNPNFVRCIIPNHEK 701
Cdd:cd14879 517 ----SPD-FVN--------------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQ 558
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 702 RAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnsiprgFMDGKQACERMIRSLELDPNLYRIGQ 781
Cdd:cd14879 559 LPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGN 632
|
....*
gi 148223878 782 SKIFF 786
Cdd:cd14879 633 TKVFL 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
100-749 |
2.66e-93 |
|
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: 315.30 E-value: 2.66e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNlpIYSENIIEMYRGKKRHeMPPHIYAISESAYRCMLQdREDQSILCTGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 180 SGAGKTENTKKVIQYLAhvasshkgkkDHTIPTESpkaikhqsgsllygeLERQLLQANPILESFGNAKTVKNDNSSRFG 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLV----------ERTASTTS---------------IEKLITAANLILEAFGNAKTQLNDNSSRFG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 260 KFIRINFDvtGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDllldgFNNYRF-VSNGYIPIPGQQd 338
Cdd:cd14898 133 KRIKLKFD--GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKND-----FIDTSStAGNKESIVQLSE- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 339 kdNFQETMEAMHIMGFSHeeILSMLKVVSSVLQFGNIVFKKERNTDQASmpeNTAAQKLCHLLGLNIMEFTRAILTPRIK 418
Cdd:cd14898 205 --KYKMTCSAMKSLGIAN--FKSIEDCLLGILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQ 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 419 VGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTkrqGASFIGILDIAGFEIFELNSFEQLCINYTNEK 498
Cdd:cd14898 278 VKGETIEVFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEK 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 499 LQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPAnspGVLALLDEECWFPKATDKTFVDKLvqeqgthSK 578
Cdd:cd14898 355 IQNDFIKKMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKI-------KK 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 579 FQKPRqLKDKADFCII--HYAGRVDYKADEWLLKNMDplndnvatllhqssdkfvselwKDVDRIVGLDQVAgmaetafg 656
Cdd:cd14898 424 YLNGF-INTKARDKIKvsHYAGDVEYDLRDFLDKNRE----------------------KGQLLIFKNLLIN-------- 472
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 657 aayktKKGMFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIV 736
Cdd:cd14898 473 -----DEGSKEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIP 547
|
650
....*....|...
gi 148223878 737 FQEFRQRYEILTP 749
Cdd:cd14898 548 KDRFEERYRILGI 560
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
99-787 |
1.07e-89 |
|
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: 307.51 E-value: 1.07e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR---GKKRHEMPPHIYAISESAYRCMLQDREDQSIL 175
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 176 CTGESGAGKTENTKKVIQYLAHVASSHKgkkdhtiPTESPKaIKHqsgsllygelerqllqANPILESFGNAKTVKNDNS 255
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSR-------TTFDSR-FKH----------------VNCILEAFGHAKTTLNDLS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 256 SRFGKFIRINF-DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVSNGY---- 330
Cdd:cd14878 137 SCFIKYFELQFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMredv 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 331 IPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGLNIMEFTR 410
Cdd:cd14878 217 STAERSLNREKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELAS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 411 AILTPRIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKAL---DRTKRQGASFIGILDIAGFEIFELNSF 487
Cdd:cd14878 297 ALTTDIQYFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 488 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCID-LIERPAnspGVLALLDEECWFPKATDKTFV 566
Cdd:cd14878 377 EQLCVNMTNEKMHHYINEVLFLQEQTECVQEGVTMETAYSPGNQTGVLDfFFQKPS---GFLSLLDEESQMIWSVEPNLP 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 567 DKL---VQEQGTHSKFQKPRQ------LKDK-ADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELwk 636
Cdd:cd14878 454 KKLqslLESSNTNAVYSPMKDgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHL-- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 637 dvdrivgldqvagmaetafgaaYKTKkgmFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLR 716
Cdd:cd14878 532 ----------------------FQSK---LVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQ 586
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148223878 717 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTpNSIPRGfmDGKQACERMIRSLELDPNL--YRIGQSKIFFR 787
Cdd:cd14878 587 YIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA-DTLLGE--KKKQSAEERCRLVLQQCKLqgWQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
99-787 |
3.04e-86 |
|
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: 296.93 E-value: 3.04e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYseniIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 179 ESGAGKTENTKKVIQ-YLAHVasshkgKKDHtiptespkaikhqsgsllygELERQLLQANPILESFGNAKTVKNDNSSR 257
Cdd:cd14937 77 ESGSGKTEASKLVIKyYLSGV------KEDN--------------------EISNTLWDSNFILEAFGNAKTLKNNNSSR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 258 FGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVSNGYIPIPGQQ 337
Cdd:cd14937 131 YGKYIKIELDEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEID 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 338 DKDNFQETMEAMHIMGFsHEEILSMLKVVSSVLQFGNIVFK---KERNTDQASMPENT--AAQKLCHLLGLNIMEFTRAI 412
Cdd:cd14937 211 DAKDFGNLMISFDKMNM-HDMKDDLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 413 LTPRIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKrQGASFIGILDIAGFEIFELNSFEQLCI 492
Cdd:cd14937 290 VFTEKTIANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 493 NYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPCIDLIErpaNSPGVLALLDEECWFPKATDKTFVDKLVQE 572
Cdd:cd14937 369 NIANEEIHSIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLR---GKTSIISILEDSCLGPVKNDESIVSVYTNK 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 573 QGTHSKFQKPRQLKDKaDFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELWKDVDRIVGLdqvagmae 652
Cdd:cd14937 445 FSKHEKYASTKKDINK-NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESL-------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 653 tafgaayktkkGMFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRIcRQGFP 732
Cdd:cd14937 516 -----------GRKNLITFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQ 583
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 148223878 733 NRIVFQEFRQRYEILTPNSIPRGFMDGKQACERMIRSlELDPNLYRIGQSKIFFR 787
Cdd:cd14937 584 YKYTFDVFLSYFEYLDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
99-739 |
7.75e-79 |
|
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: 276.40 E-value: 7.75e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHE-------MPPHIYAISESAYRCMLQDRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 171 DQSILCTGESGAGKTENTKKVIQYLahvasshkgkkdHTIPTESpkaikhqsgslLYGELERQLLQANPILESFGNAKTV 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYF------------HYIQTDS-----------QMTERIDKLIYINNILESMSNATTI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 251 KNDNSSRFGKFIRINFD---------VTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAG-SGEHLKSDLLLDGF 320
Cdd:cd14884 138 KNNNSSRCGRINLLIFEeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNC 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 321 NNYRFV--------------------SNGYIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKke 380
Cdd:cd14884 218 GVYGLLnpdeshqkrsvkgtlrlgsdSLDPSEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK-- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 381 rntdqasmpentaaqKLCHLLGLNIMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKAL 460
Cdd:cd14884 296 ---------------AAAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNV 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 461 DRTKRQGA-----------SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGl 529
Cdd:cd14884 361 LKCKEKDEsdnediysineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP- 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 530 DLQPCIDLIERpanspgVLALLDE-----ECWFPKATDKTFVD-----KLVQEQGTHS---------KFQKPRQLKDKAD 590
Cdd:cd14884 440 SYSDTLIFIAK------IFRRLDDitklkNQGQKKTDDHFFRYllnneRQQQLEGKVSygfvlnhdaDGTAKKQNIKKNI 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 591 FCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSElwkdvdrivgldqvagmaetafgAAYKTKKGMFRTVG 670
Cdd:cd14884 514 FFIRHYAGLVTYRINNWIDKNSDKIETSIETLISCSSNRFLRE-----------------------ANNGGNKGNFLSVS 570
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148223878 671 QLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 739
Cdd:cd14884 571 KKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
100-767 |
4.64e-75 |
|
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: 263.90 E-value: 4.64e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYknlpiyseniieMYRGKKRH-------EMPPHIYAISESAYRCMLQDREDQ 172
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTltstrssPLAPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 173 SILCTGESGAGKTENTKKVIQYLAHVAsshkGKKDHTiptespKAIKHqsgsllygelerqLLQANPILESFGNAKTVKN 252
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVA----GGGPET------DAFKH-------------LAAAFTVLRSLGSAKTATN 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 253 DNSSRFGKFIRINFdVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFN--NYRFVSNGY 330
Cdd:cd14881 127 SESSRIGHFIEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 331 IPIPGQQDKDNFQETMEAMHIMGFsheEILSMLKVVSSVLQFGNIVFkKERNTDQASMPENTAAQKLCHLLGLNIMEFTR 410
Cdd:cd14881 206 TRQNEAEDAARFQAWKACLGILGI---PFLDVVRVLAAVLLLGNVQF-IDGGGLEVDVKGETELKSVAALLGVSGAALFR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 411 AiLTPRIK-VGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKaldrTKRQGAS--------FIGILDIAGFEI 481
Cdd:cd14881 282 G-LTTRTHnARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMFGFED 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 482 FELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNF-IDFgLDLQPCIDLIERPANspGVLALLDEECwFPKA 560
Cdd:cd14881 357 PKPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLISSLRT--GLLSMLDVEC-SPRG 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 561 TDKTFVDKLVQEQGTHSKFQKPRQLKDKAdFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSdkfvselwkdvdr 640
Cdd:cd14881 433 TAESYVAKIKVQHRQNPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN------------- 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 641 ivgldqvagmaeTAFGaayktkkgmFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGV 720
Cdd:cd14881 499 ------------CNFG---------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQV 557
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 148223878 721 LEGIRICRQGFPNRIVFQEFRQRYEILTPNSIPRGFMDGKQACERMI 767
Cdd:cd14881 558 LETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALI 604
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
99-754 |
6.98e-69 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 245.55 E-value: 6.98e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYrgkkrhemppHIYAISESAYRCMLQDRED-QSILCT 177
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 178 GESGAGKTENTKKVIQYLAHVASShkgkkdhTIPTESPKAIKHqsgsllygelerqllqanpILESFGNAKTVKNDNSSR 257
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKS-------KVTTKHSSAIES-------------------VFKSFGCAKTLKNDEATR 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 258 FGKFIRINFDvTGYIVGANIE-TYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVSNGYIPIPGQ 336
Cdd:cd14874 125 FGCSIDLLYK-RNVLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 337 QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNTD-QASMPE--NTAAQK-LCHLLGLNIMEFTrAI 412
Cdd:cd14874 204 SDVNHFKHLEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNPNvEQDVVEigNMSEVKwVAFLLEVDFDQLV-NF 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 413 LTPRIKVGRDYVQKAQTKEQADFAVealrkATYERLFRWLVYRINKALDRTKRQGAsfIGILDIAGFEIFELNSFEQLCI 492
Cdd:cd14874 283 LLPKSEDGTTIDLNAALDNRDSFAM-----LIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLI 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 493 NYTNEKLQQLFNHTMFILEQEEYQREGIEWNF-IDFGLDLQPCIDLI-ERPAnspGVLALLDEECWFPKATDKTFVDKLV 570
Cdd:cd14874 356 NSVNERIENLFVKHSFHDQLVDYAKDGISVDYkVPNSIENGKTVELLfKKPY---GLLPLLTDECKFPKGSHESYLEHCN 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 571 QEQGTHSKFQKPRQlKDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELwkdvdrivgldqvagm 650
Cdd:cd14874 433 LNHTDRSSYGKARN-KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLL---------------- 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 651 aetaFGAAYKTKKGMFRTVGQLYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQG 730
Cdd:cd14874 496 ----FESYSSNTSDMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKG 571
|
650 660
....*....|....*....|....
gi 148223878 731 FPNRIVFQEFRQRYEILTPNSIPR 754
Cdd:cd14874 572 YPVKISKTTFARQYRCLLPGDIAM 595
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
100-787 |
5.27e-67 |
|
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: 241.15 E-value: 5.27e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYrgKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 179 ESGAGKTENTKKVIQYLAHV-ASSHKGKKDHtiptespkaikhqsgsllygelerqLLQANPILESFGNAKTVKNDNSSR 257
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTdLSRSKYLRDY-------------------------ILESGIILESFGHASTDSNHNSSR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 258 FGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVSN-GYIPIPGQ 336
Cdd:cd14905 135 WGKYFEMFYSLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 337 QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKERNtdQASMPENTAAQKLCHLLGLNIMEFTRAILTPR 416
Cdd:cd14905 215 DDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 417 IKVGRDYVQKAqtkeqadfavEALRKATYERLFRWLVYRINKALDRTkrQGASFIGILDIAGFEIFELNSFEQLCINYTN 496
Cdd:cd14905 293 SMPVNEAVENR----------DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 497 EKLQQLFNHTMFILEQEEYQREGIEW-NFIDFGlDLQPCIDLIERpanspgVLALLDEECWFPKATDKTFVDKLVQEQGT 575
Cdd:cd14905 361 ERLQQIYLQTVLKQEQREYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSR 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 576 HSKF-QKPRQlkdkadFCIIHYAGRVDYKADEWLLKNMDPLNDNvATLLHQSSdkfVSELWKDVDRIVGLDQVAGMAETA 654
Cdd:cd14905 434 HHLFgKKPNK------FGIEHYFGQFYYDVRGFIIKNRDEILQR-TNVLHKNS---ITKYLFSRDGVFNINATVAELNQM 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 655 FGAAYKTKKGMFrtvgqlykeSLAKLMATLRNTNPN-------------------------------------------- 690
Cdd:cd14905 504 FDAKNTAKKSPL---------SIVKVLLSCGSNNPNnvnnpnnnsgggggggnsgggsgsggstyttysstnkainnsnc 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 691 ---FVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNSipRGFMD-GKQACERM 766
Cdd:cd14905 575 dfhFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQNQ--RNFQNlFEKLKEND 652
|
730 740
....*....|....*....|.
gi 148223878 767 IRSLELDPNLYRIGQSKIFFR 787
Cdd:cd14905 653 INIDSILPPPIQVGNTKIFLR 673
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-786 |
6.72e-67 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 242.57 E-value: 6.72e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 102 LHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKR----------HEMPPHIYAISESAYRCMLQDRED 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 172 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGKKDhtipTESPKAIKHQSGsllygeleRQLLQANPILESFGNAKTVK 251
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPD----SEGASGVLHPIG--------QQILHAFTILEAFGNAATRQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 252 NDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSgEH---LKSDLLLD-GFNNYRFVS 327
Cdd:cd14893 152 NRNSSRFAKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGV-QHdptLRDSLEMNkCVNEFVMLK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 328 NGyIPIPGQ--QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVF------KKERN-------TDQASMPENT 392
Cdd:cd14893 231 QA-DPLATNfaLDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpegGKSVGgansttvSDAQSCALKD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 393 AAQKL--CHLLGLNIMEFTRAILTPRI--KVGRDYVQ--KAQTKEQADFAVEALRKATYERLFRWLVYRINKAL----DR 462
Cdd:cd14893 310 PAQILlaAKLLEVEPVVLDNYFRTRQFfsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 463 TKRQG----ASFIGILDIAGFEIFE--LNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWNFIDFGL 529
Cdd:cd14893 390 YEKSNivinSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 530 DLQPCIDLIERPanSPGVLALLDEECWFPKATDKTFVDKLVQEQGTHSKFQKPRQLKDKAD------------FCIIHYA 597
Cdd:cd14893 470 EQEKCLQLFEDK--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHC 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 598 GRVDYKADEWLLKNMDPLNDNVATLLHQSSDKfvselwkdVDRIVGLDQVAGmAETAFGAAYKTKKG----MFRTVGQLY 673
Cdd:cd14893 548 GKVTYNGKGLSSKNMLSISSTCAAIMQSSKNA--------VLHAVGAAQMAA-ASSEKAAKQTEERGstssKFRKSASSA 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 674 KESLA--------------KLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 739
Cdd:cd14893 619 RESKNitdsaatdvynqadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGH 698
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 148223878 740 FRQRYEILTPNsipRGFMdgkqacERMIRSLE----LDPNLYRIGQSKIFF 786
Cdd:cd14893 699 FFRRYKNVCGH---RGTL------ESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
100-747 |
6.59e-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: 219.23 E-value: 6.59e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 180 SGAGKTENTKKVIQYLAHVasshkgkkdhtiptespkaikhqsGSLLYGELERqLLQANPILESFGNAKTVKNDNSSRFG 259
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYL------------------------GDGNRGATGR-VESSIKAILALVNAGTPLNADSTRCI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 260 KFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAG--SGEHLKsDLLLDGFNNYRfvsngYIPIPGQQ 337
Cdd:cd14882 137 LQYQLTFGSTGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYR-----YLRIPPEV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 338 DKDN--------------FQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNIVFKKerNTDQASMPENTAAQKLCHLLGL 403
Cdd:cd14882 211 PPSKlkyrrddpegnverYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 404 NIMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKrqgASF-----IGILDIAG 478
Cdd:cd14882 289 DEKKFMWALTNYCLIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 479 FEIFELNSFEQLCINYTNEKLQQLFNHTMFI---LEQEEYQREGIEWNFIDFGLDLQpciDLIERPAnspGVLALLDEEC 555
Cdd:cd14882 366 FECFHRNRLEQLMVNTLNEQMQYHYNQRIFIsemLEMEEEDIPTINLRFYDNKTAVD---QLMTKPD---GLFYIIDDAS 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 556 wfPKATDKTFVDKLVQEQgtHSKFQKPrqlKDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVSELW 635
Cdd:cd14882 440 --RSCQDQNYIMDRIKEK--HSQFVKK---HSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMF 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 636 KDvdrivglDQVAGMaetafgaayktkkgmfRTVGQLYKESLAKLMATLRNtNPN-----FVRCIIPNHEKRAGKLDPHL 710
Cdd:cd14882 513 TN-------SQVRNM----------------RTLAATFRATSLELLKMLSI-GANsggthFVRCIRSDLEYKPRGFHSEV 568
|
650 660 670
....*....|....*....|....*....|....*..
gi 148223878 711 VLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 747
Cdd:cd14882 569 VRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFL 605
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
100-785 |
4.73e-59 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 218.55 E-value: 4.73e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR-GKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 179 ESGAGKTENTKKVIQYLAHVASSHKGKKDHTIpTESPKAIKHQSGSLLYGELERQLLQANPILESFGNAKTVKNDNSSRF 258
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKGSRRLPTNLN-DQEEDNIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 259 GKFIRINFDvTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGSGEHLKSDLLLDGFNNYRFVSNGYIPIPGQQD 338
Cdd:cd14938 161 SKFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 339 KDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNI-----VFKKE---------------------RNTDQASMPENT 392
Cdd:cd14938 240 SGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkaFRKKSllmgknqcgqninyetilselENSEDIGLDENV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 393 AAQKL-CHLLGLNIMEFTRAILTPRIkVGRDYVQKAQTKEQADFAVEALRKATYERLFRWLVYRINKALDRTKR--QGAS 469
Cdd:cd14938 320 KNLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 470 FIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANspGVLA 549
Cdd:cd14938 399 YINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 550 LLDEECWFPKATDKT-FVDKLVQEQGTHSKF-QKPRQLKDKADFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSS 627
Cdd:cd14938 477 SLLENVSTKTIFDKSnLHSSIIRKFSRNSKYiKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 628 DKFVSEL-----WKDVDRIVGLDQVAGM--AETAFGAAYKTKKGMFRTvgqLYKESLAKLMATLRNTNPNFVRCIIPNHE 700
Cdd:cd14938 557 NEYMRQFcmfynYDNSGNIVEEKRRYSIqsALKLFKRRYDTKNQMAVS---LLRNNLTELEKLQETTFCHFIVCMKPNES 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 701 KRA-GKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnsiprgfmDGKQACERMIRSLELDPNLYRI 779
Cdd:cd14938 634 KRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISNYEWMI 705
|
....*.
gi 148223878 780 GQSKIF 785
Cdd:cd14938 706 GNNMIF 711
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
121-271 |
9.38e-59 |
|
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: 200.26 E-value: 9.38e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 121 FCVVINPYKNLPIYSEN-IIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148223878 200 SSHKGKKDHTIPTESPKaikhqsgslLYGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 271
Cdd:cd01363 81 FNGINKGETEGWVYLTE---------ITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1059-1876 |
2.60e-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: 144.43 E-value: 2.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1059 KKEEKTRQELEKAKRKLDgettDFQDQIAELQAQIEELKLQlAKKEEELQAAlaRGDEEVLQKNNTLKLVRELQAQIAEL 1138
Cdd:TIGR02168 172 ERRKETERKLERTRENLD----RLEDILNELERQLKSLERQ-AEKAERYKEL--KAELRELELALLVLRLEELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1139 QEDLESEKASRNKAEKQKRDLSEELEALKTEledtldttaaQQELRTKREQEVAELrKSIEEETRNHEAQIQEMRQRQA- 1217
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLE----------VSELEEEIEELQKEL-YALANEISRLEQQKQILRERLAn 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1218 --TALEELSEQLEQAKRFKVNLEKNKQSLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELHAKVLEGDRLRADMVE 1295
Cdd:TIGR02168 314 leRQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1296 KSSKLQNELENVSSLLEEAEKKGIKLAKDVASM-----ESQLQDTQELLQEETRQKLNQSSRIRQLEEEKNNLQEQQEEE 1370
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEA 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1371 EEARKSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLlKDTEGLGQRLEEKIIAYEKLEKTKNR-LQQELDDLMV 1449
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ-SGLSGILGVLSELISVDEGYEAAIEAaLGGRLQAVVV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1450 -DLDHQRQIVSNLEKKQKKFDQLLaEEKNISARHAEERDRAEADAREKETKALSLARALDEALEA--------------Q 1514
Cdd:TIGR02168 553 eNLNAAKKAIAFLKQNELGRVTFL-PLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllggvlvvddL 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1515 DEFERLNKQLRAEME------DLMSSK---------------------DDVGKNVHELEKSKRALDQQVEEMRTQLEELE 1567
Cdd:TIGR02168 632 DNALELAKKLRPGYRivtldgDLVRPGgvitggsaktnssilerrreiEELEEKIEELEEKIAELEKALAELRKELEELE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1568 DELQGTEDAKLRLEVNMQAMKAQFERdLQTRDEQNEEKKRALVKQVRELEAELEDERKQRAMAVAIKKKLEMDMKDFESQ 1647
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1648 IEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDIFAQSKENEKKLKGLEAEILQLQEELAASERSRRHAEQERDE 1727
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1728 LADEISnstsgksALLDEKRRLEARIAHLEEELEEEQSNMELLNDRFRKTTLQVDTLNSELAAERSSGQKSENARQQLER 1807
Cdd:TIGR02168 871 LESELE-------ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1808 QNKELKAKLQELEGSVKSKFKATIATLESKIAQLEEQLE-------------QEAKERV-------------------AS 1855
Cdd:TIGR02168 944 RLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvnlaaieeyEELKERYdfltaqkedlteaketleeAI 1023
|
890 900
....*....|....*....|.
gi 148223878 1856 NKLVRRTEKKLKEVFMQVEDE 1876
Cdd:TIGR02168 1024 EEIDREARERFKDTFDQVNEN 1044
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1088-1949 |
5.22e-32 |
|
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: 137.11 E-value: 5.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1088 ELQAQIEE----LKLQLAKKEEELQAALARGDeevlqknntlkLVReLQAQIAELQEDLESEKASRNKAEKQKrDLSEEL 1163
Cdd:TIGR02168 156 ERRAIFEEaagiSKYKERRKETERKLERTREN-----------LDR-LEDILNELERQLKSLERQAEKAERYK-ELKAEL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1164 EALKTELEdTLDTTAAQQELRTKREQEvaelrksieeetrnheAQIQEMRQRQATALEELSEQLEQAKRFKVNLEKNKQS 1243
Cdd:TIGR02168 223 RELELALL-VLRLEELREELEELQEEL----------------KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1244 LESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELHAKVLEGDRLRADMVEKSSKLQNELENVSSLLEEAEKKGIKLAK 1323
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1324 DVASMESQLQDTQELLQeetrqklNQSSRIRQLEEEKNnlqeqqeeeeearkSLEKQILSLQSQLIEAKKKVDDEVGTIE 1403
Cdd:TIGR02168 366 ELEELESRLEELEEQLE-------TLRSKVAQLELQIA--------------SLNNEIERLEARLERLEDRRERLQQEIE 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1404 GLEevKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARHA 1483
Cdd:TIGR02168 425 ELL--KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1484 EERDRAEADAREKETKALSLARaLDEALEAQDEFER-LNKQLRAEMEDL-MSSKDDVGKNVHELEKSKR------ALDQQ 1555
Cdd:TIGR02168 503 GFSEGVKALLKNQSGLSGILGV-LSELISVDEGYEAaIEAALGGRLQAVvVENLNAAKKAIAFLKQNELgrvtflPLDSI 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1556 VEemrTQLEELEDELQGTEDAKLRLEVNMQAMKAQFERDLQ---------TRDEQNEEKKRALVKQVR--ELEAEL---- 1620
Cdd:TIGR02168 582 KG---TEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvDDLDNALELAKKLRPGYRivTLDGDLvrpg 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1621 ------EDERKQRAMAVAIK-KKLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARasrddifAQSKEN 1693
Cdd:TIGR02168 659 gvitggSAKTNSSILERRREiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS-------RQISAL 731
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1694 EKKLKGLEAEILQLQEELAASERSRRHAEQERDELADEISNSTSGKSALLDEKRRLEARIAhleeeleEEQSNMELLNDR 1773
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE-------QLKEELKALREA 804
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1774 FRKTTLQVDTLNSELAAERSSGQKSENARQQLERQNKELKAKLQELEGSVKSkFKATIATLESKIAQLEEQLEQEAKERV 1853
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-LAAEIEELEELIEELESELEALLNERA 883
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1854 ASNKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANTRMKQLKRQLEEAEEEATRANASAR-KLQRELDDA------- 1925
Cdd:TIGR02168 884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAealenki 963
|
890 900
....*....|....*....|....
gi 148223878 1926 TEANEVLSREVSTLKNRLRRGGPV 1949
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKIKELGPV 987
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1051-1873 |
7.81e-32 |
|
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: 136.35 E-value: 7.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1051 ISDLEERLKKEEKTRQELEKAKRKLDgettDFQDQIAELQAQIEELKLQLAKKEE--ELQAAL--ARGDEEVLQKNNTLK 1126
Cdd:TIGR02169 162 IAGVAEFDRKKEKALEELEEVEENIE----RLDLIIDEKRQQLERLRREREKAERyqALLKEKreYEGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1127 LVRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELED-TLDTTAAQQELRTKREQEVAELRKSIEEETRNH 1205
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1206 E------AQIQEMRQRQATALEELSEQLEQAKRFKVNL----EKNKQSLESDNKELATEVKSLQQMKAESEYKRKKLEGQ 1275
Cdd:TIGR02169 318 EdaeerlAKLEAEIDKLLAEIEELEREIEEERKRRDKLteeyAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1276 VQELHAKVLEGDRLRADMVEKSSK---LQNELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQEETRQKLNQSSR 1352
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEEladLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1353 IRQLEEEKNNLQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLKDTE-GLGQRLE------- 1424
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEvAAGNRLNnvvvedd 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1425 ---EKIIAYEKLEKTK-------NRLQQELDDL--------------MVDLDHQRQ-----------IVSNLEKKQKKFD 1469
Cdd:TIGR02169 558 avaKEAIELLKRRKAGratflplNKMRDERRDLsilsedgvigfavdLVEFDPKYEpafkyvfgdtlVVEDIEAARRLMG 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1470 QL--------LAE-----------EKNISARHAEERDRAEADAREKEtkalSLARALDEALEAQDEFERLNKQLRAEMED 1530
Cdd:TIGR02169 638 KYrmvtlegeLFEksgamtggsraPRGGILFSRSEPAELQRLRERLE----GLKRELSSLQSELRRIENRLDELSQELSD 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1531 LMSSKDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDELQGTEDAKLRLEVNMQAMKAQFErdlQTRDEQNEEKKRALV 1610
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH---KLEEALNDLEARLSH 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1611 KQVRELEAELEDERKQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDIFAQS 1690
Cdd:TIGR02169 791 SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1691 KEN-------EKKLKGLEAEILQLQEELAASERSRRHAEQERDELADEISNSTSGKSALLDEkrrleariahleeeleee 1763
Cdd:TIGR02169 871 EELeaalrdlESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE------------------ 932
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1764 qsnmellndrfrkttlqvdtlNSELAAERSSGQKSENARQQLERQNKELKAKLQELE--GSVKSKFKATIATLESKIAQL 1841
Cdd:TIGR02169 933 ---------------------LSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRalEPVNMLAIQEYEEVLKRLDEL 991
|
890 900 910
....*....|....*....|....*....|..
gi 148223878 1842 EEQLEQEAKERVASNKLVRRTEKKLKEVFMQV 1873
Cdd:TIGR02169 992 KEKRAKLEEERKAILERIEEYEKKKREVFMEA 1023
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1057-1754 |
7.53e-31 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 132.75 E-value: 7.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1057 RLKKEEkTRQELEKAKRKLDgettDFQDQIAELQAQIEELKLQ--LAKKEEELQAALargdeEVLQKNNTLKLVRELQAQ 1134
Cdd:COG1196 171 KERKEE-AERKLEATEENLE----RLEDILGELERQLEPLERQaeKAERYRELKEEL-----KELEAELLLLKLRELEAE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1135 IAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEdtldttAAQQELRTKREQEvAELRKSIEEETRNHEAQiQEMRQ 1214
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELE------ELELELEEAQAEE-YELLAELARLEQDIARL-EERRR 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1215 RQATALEELSEQLEQAKRFKVNLEKNKQSLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELHAKVLEGDRLRADMV 1294
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1295 EKSSKLQNELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQEETRQKLNQSSRIRQLEEEKNNLQEQQEEEEEAR 1374
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1375 KSLEKQILSLQSQLIEAKKKvddevgtieglEEVKKKLLKDTEGLGQrleekIIAYEKLEKTKNRLQQELDDLMVDldhq 1454
Cdd:COG1196 473 ALLEAALAELLEELAEAAAR-----------LLLLLEAEADYEGFLE-----GVKAALLLAGLRGLAGAVAVLIGV---- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1455 rqivsnlekkQKKFDQLLAEEKNISARHAEERDRAEADAREKETKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSS 1534
Cdd:COG1196 533 ----------EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1535 KDDVgKNVHELEKSKRALDQQVEEMRTQLEELEDELQGTEDAKLRLEVNmQAMKAQFERDLQTRDEQNEEKKRALVKQVR 1614
Cdd:COG1196 603 LVAS-DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVT-LEGEGGSAGGSLTGGSRRELLAALLEAEAE 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1615 ELEAELEDERKQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDiFAQSKENE 1694
Cdd:COG1196 681 LEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE-ALEELPEP 759
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1695 KKLKGLEAEILQLQEELAASERSRRHAEQERDELADEISNSTSGKSALLDEKRRLEARIA 1754
Cdd:COG1196 760 PDLEELERELERLEREIEALGPVNLLAIEEYEELEERYDFLSEQREDLEEARETLEEAIE 819
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
896-1621 |
2.03e-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: 125.17 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 896 QKHQQLVEEKNILaeQLHAETELFAEAEEMRARLAIKKQEMEEILRDLEIRmeeeeernqvLQNEKKKMQTHVQDLEEQL 975
Cdd:TIGR02168 213 ERYKELKAELREL--ELALLVLRLEELREELEELQEELKEAEEELEELTAE----------LQELEEKLEELRLEVSELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 976 DEEEAAQKLQLEKVtaeAKIKKMEEDILVLEDQNSKFLKEKKLLEERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLE 1055
Cdd:TIGR02168 281 EEIEELQKELYALA---NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1056 ERLKKEEKTRQELEKAKRKLDGETTDFQDQIAELQAQIEELKLQ---LAKKEEELQAALARGDEEV--LQKNNTLKLVRE 1130
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEierLEARLERLEDRRERLQQEIeeLLKKLEEAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1131 LQAQIAELQ---EDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELRKSIEEETRNHE- 1206
Cdd:TIGR02168 438 LQAELEELEeelEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSg 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1207 --------AQIQEMRQRQATALEE---------LSEQLEQAKRFKVNLEKNK--------------QSLESDNKELATEV 1255
Cdd:TIGR02168 518 lsgilgvlSELISVDEGYEAAIEAalggrlqavVVENLNAAKKAIAFLKQNElgrvtflpldsikgTEIQGNDREILKNI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1256 KSLQQMKAESEYKRKKLEGQVQELHAKV------------------------LEGDRLRAD-------------MVEKSS 1298
Cdd:TIGR02168 598 EGFLGVAKDLVKFDPKLRKALSYLLGGVlvvddldnalelakklrpgyrivtLDGDLVRPGgvitggsaktnssILERRR 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1299 ---KLQNELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQEETRQKLNQSSRIRQLEEEKNNLQEQQEEEEEARK 1375
Cdd:TIGR02168 678 eieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1376 SLEKQILSLQSQLIEAkkkvddevgtieglEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQR 1455
Cdd:TIGR02168 758 ELEAEIEELEERLEEA--------------EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1456 QIVSNLEKKQKKFDQLLAEEKNISARHAEERDRAEADAREKETKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSSK 1535
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1536 DDVGKNVHELEKSKRALDQQVEEMRTQLEELEDELQGTEDaKLRLEVNMQAMkaqferDLQTRDEQNEEKKRALVKQVRE 1615
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE-RLSEEYSLTLE------EAEALENKIEDDEEEARRRLKR 976
|
....*.
gi 148223878 1616 LEAELE 1621
Cdd:TIGR02168 977 LENKIK 982
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
991-1627 |
1.42e-27 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 122.35 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 991 AEAKIKKMEEDILVLEDQNSKFLKEKKLLEERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKKEEKTRQELEK 1070
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1071 AKRKLDGETTDFQDQIAELQAQIEELKLQLAKKEEELQAALArgdeevlQKNNTLKLVRELQAQIAELQEDLESEKASRN 1150
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA-------ELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1151 KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELRKSIEEEtRNHEAQIQEMRQRQATALEELSEQLEQA 1230
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE-EEALEEAAEEEAELEEEEEALLELLAEL 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1231 KRFKVNLEKNKQSLESDNKELATEVKSLQQMKAESEYKRK--KLEGQVQELHAKVLEGDRLRADmvekssklqnelenvs 1308
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEgvKAALLLAGLRGLAGAVAVLIGV---------------- 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1309 sllEEAEKKGIKLAKDVASMESQLQDTQELLQEETRQKLNQSSRIRQLEEEKnnlqeqQEEEEEARKSLEKQILSLQSQL 1388
Cdd:COG1196 533 ---EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDK------IRARAALAAALARGAIGAAVDL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1389 IEAKKKVDDEVGTIEGLEEVKKKLLKDTEGLGQRLeekiiayekLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKF 1468
Cdd:COG1196 604 VASDLREADARYYVLGDTLLGRTLVAARLEAALRR---------AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1469 DQLLAEEKNISARHAEERDRAEADAREKETKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKS 1548
Cdd:COG1196 675 LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALE 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1549 KRALDQQVEEMRTQLEELEDELQgtedaklRLE-VNMQAM---KAQFERdLQTRDEQNEEkkraLVKQVRELE---AELE 1621
Cdd:COG1196 755 ELPEPPDLEELERELERLEREIE-------ALGpVNLLAIeeyEELEER-YDFLSEQRED----LEEARETLEeaiEEID 822
|
....*.
gi 148223878 1622 DERKQR 1627
Cdd:COG1196 823 RETRER 828
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
823-1707 |
4.63e-27 |
|
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: 120.93 E-value: 4.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 823 AKKQQQLIALKVlqrncaaylKLRHWQWWRLftkvkpLLQVTRQEEELvakdeellkvkekqSKVEGELVDMEQKHQQLV 902
Cdd:TIGR02168 209 AEKAERYKELKA---------ELRELELALL------VLRLEELREEL--------------EELQEELKEAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 903 EEKNILAEQLhaetelfaeaEEMRARLAIKKQEMEEIlrdleirmeeeeernqvlqnekkkmqthvqdleeqldeeeaaQ 982
Cdd:TIGR02168 260 AELQELEEKL----------EELRLEVSELEEEIEEL------------------------------------------Q 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 983 KLQLEKVtaeAKIKKMEEDILVLEDQNSKFLKEKKLLEERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKKEE 1062
Cdd:TIGR02168 288 KELYALA---NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1063 KTRQELEKAKRKLDGETTDFQDQIAELQAQIEELKLQLAKKEEELQAALARGDEevLQKNNTLKLVRELQAQIAELQEDL 1142
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER--LQQEIEELLKKLEEAELKELQAEL 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1143 ESEKASRNKAEKQKRDLSEELEALKTELEdtldttAAQQELRTKREQevaelrksiEEETRNHEAQIQEMRQRQATALEE 1222
Cdd:TIGR02168 443 EELEEELEELQEELERLEEALEELREELE------EAEQALDAAERE---------LAQLQARLDSLERLQENLEGFSEG 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1223 LSEQLEQAKRFKVNLEKNKQSLESDNK-ELATE-----------VKSLQQMKAESEYKRKKLEGQVQELHAKVLEGDRLR 1290
Cdd:TIGR02168 508 VKALLKNQSGLSGILGVLSELISVDEGyEAAIEaalggrlqavvVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQ 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1291 ADMVEksskLQNELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQE-ETRQKLNQSSRIRQLEEEK--------- 1360
Cdd:TIGR02168 588 GNDRE----ILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNAlELAKKLRPGYRIVTLDGDLvrpggvitg 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1361 --NNLQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKN 1438
Cdd:TIGR02168 664 gsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1439 RLQQELDDLMVDL-DHQRQIVSNLEKKQKKFDQLLAEEKNIsarhaeERDRAEADAREKETKALSlaraldealEAQDEF 1517
Cdd:TIGR02168 744 QLEERIAQLSKELtELEAEIEELEERLEEAEEELAEAEAEI------EELEAQIEQLKEELKALR---------EALDEL 808
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1518 ERLNKQLRAEMEDLMSSKDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDELQGTEDAKLRLEVNMQAMKAQFERDLQT 1597
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1598 RDEQNEEkKRALVKQVRELEAELEDERKQRAMAVAIKKKLEMDMKDFESQIEaankgredaikqlRKLQAQTKDYQRELE 1677
Cdd:TIGR02168 889 LALLRSE-LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID-------------NLQERLSEEYSLTLE 954
|
890 900 910
....*....|....*....|....*....|
gi 148223878 1678 EARASRDDIFAQSKENEKKLKGLEAEILQL 1707
Cdd:TIGR02168 955 EAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
105-728 |
4.82e-25 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 113.68 E-value: 4.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 105 LKDRYYSGLIYTYSGLFCV-VINPYKNL------PIYSENIIEMYRGKKRHE--MPPHIYAISE---------------- 159
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 160 ----SAYRCMLQDReDQSILCTGESGAGKTENTKKVIQYLAHVAS-------------------------SHKGKKDHTI 210
Cdd:cd14894 87 pstiSSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAQpalskgseetckvsgstrqpkiklfTSSTKSTIQM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 211 PTESPKAIK-------------------------------------HQSGsLLYG--------ELERQL----------- 234
Cdd:cd14894 166 RTEEARTIAlleakgvekyeivlldlhperwdemtsvsrskrlpqvHVDG-LFFGfyeklehlEDEEQLrmyfknphaak 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 235 -----LQANPILESFGNAKTVKNDNSSRFGKF--IRINFDVTGY---IVGANIETYLLEKSRAVRQA------KDERTFH 298
Cdd:cd14894 245 klsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFH 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 299 IFYQLLAGSGEH-----LKSDLLLDGFN----NYRFVSN----GYIPIPG--QQDKDNFQETMEAMHIMGFSHEEILSML 363
Cdd:cd14894 325 ILYAMVAGVNAFpfmrlLAKELHLDGIDcsalTYLGRSDhklaGFVSKEDtwKKDVERWQQVIDGLDELNVSPDEQKTIF 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 364 KVVSSVLQFGNIVFKKERNTDQASMPEN---TAAQKLCHLLGLNIME-FTRAILTPRIKV--GRDYVQKAQTKEQADFAV 437
Cdd:cd14894 405 KVLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEkLERMLMTKSVSLqsTSETFEVTLEKGQVNHVR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 438 EALRKATYERLFRWLVYRINKAL-------DRTKRQ---------GASFIGILDIAGFEIFELNSFEQLCINYTNEKLqq 501
Cdd:cd14894 485 DTLARLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL-- 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 502 lfnhtmfileqeeYQREGiewNFIDFGLDLQPciDLIERPANSP---------GVLALLDEECWFPKAT----------D 562
Cdd:cd14894 563 -------------YAREE---QVIAVAYSSRP--HLTARDSEKDvlfiyehplGVFASLEELTILHQSEnmnaqqeekrN 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 563 KTFVdKLVQEQGTHSKFQKPRQLKDKA----------DFCIIHYAGRVDYKADEWLLKNMDPLNDNVATLLHQSSDKFVS 632
Cdd:cd14894 625 KLFV-RNIYDRNSSRLPEPPRVLSNAKrhtpvllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFC 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 633 ELWKDVDRivgLDQVAGMAETAFGAAYKTKKGMFRTVGQlYKESLAKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVL 712
Cdd:cd14894 704 RMLNESSQ---LGWSPNTNRSMLGSAESRLSGTKSFVGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVE 779
|
810
....*....|....*.
gi 148223878 713 DQLRCNGVLEGIRICR 728
Cdd:cd14894 780 QQCRSQRLIRQMEICR 795
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1121-1896 |
4.89e-25 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 114.06 E-value: 4.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1121 KNNTLKLVRELQAQIAELQEDLESekaSRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELRKSIEE 1200
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNE---SNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1201 ETRNHEAQ---IQEMRQRQATALEELSEQ-------LEQAKRFKVNLEK--NKQSLESDN------KELATEV-KSLQQM 1261
Cdd:pfam15921 150 TVHELEAAkclKEDMLEDSNTQIEQLRKMmlshegvLQEIRSILVDFEEasGKKIYEHDSmstmhfRSLGSAIsKILREL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1262 KAESEYkrkkLEGQVQELHakvlegDRLRADMVEKSSK----LQNELENVSSLLEEAEKKGIKLAKDVASMESQ---LQD 1334
Cdd:pfam15921 230 DTEISY----LKGRIFPVE------DQLEALKSESQNKiellLQQHQDRIEQLISEHEVEITGLTEKASSARSQansIQS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1335 TQELLQEETRQKlnQSSRIRQLEEeknnlqeqqeeeeearksLEKQILSLQSQLIEAKKKVDDEVgtieglEEVKKKLLK 1414
Cdd:pfam15921 300 QLEIIQEQARNQ--NSMYMRQLSD------------------LESTVSQLRSELREAKRMYEDKI------EELEKQLVL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1415 DTEGLGQRLEEKiiayEKLEKTKNRLQQELDDLMVDLdHQRQIVSNLEKKQKKFDQLLAEEKNISARHAeerdRAEADAR 1494
Cdd:pfam15921 354 ANSELTEARTER----DQFSQESGNLDDQLQKLLADL-HKREKELSLEKEQNKRLWDRDTGNSITIDHL----RRELDDR 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1495 EKETKAL-SLARALDEalEAQDEFERLNKQLRAEMEDLmsskDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDELQGT 1573
Cdd:pfam15921 425 NMEVQRLeALLKAMKS--ECQGQMERQMAAIQGKNESL----EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTV 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1574 EDAKLRLEVNMQAMKAqferdlqTRDEQNEEKKRALVKQVRELEAELEDERKQRAMAVAIKKKLEMDMKD-----FESQI 1648
Cdd:pfam15921 499 SDLTASLQEKERAIEA-------TNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDkvieiLRQQI 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1649 E-----AANKGREDAIKQLRK--LQAQTKDYQRELEEARASRDDIFAQSKENEKKLKGLEAEILQLQEelAASERSR--R 1719
Cdd:pfam15921 572 EnmtqlVGQHGRTAGAMQVEKaqLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVN--AGSERLRavK 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1720 HAEQERDELADEISNSTSGKSALLDEkrrleariahleeeleeeqsnMELLNDRFRKTTLQVDTLNSELAAERSSGQ--- 1796
Cdd:pfam15921 650 DIKQERDQLLNEVKTSRNELNSLSED---------------------YEVLKRNFRNKSEEMETTTNKLKMQLKSAQsel 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1797 -KSENARQQLERQNKELKAKLQELEGSVKSKfKATIATLESKIAQLEEQLEQEAKERvasnKLVRRTEKKLKEVFMQVED 1875
Cdd:pfam15921 709 eQTRNTLKSMEGSDGHAMKVAMGMQKQITAK-RGQIDALQSKIQFLEEAMTNANKEK----HFLKEEKNKLSQELSTVAT 783
|
810 820
....*....|....*....|.
gi 148223878 1876 ERRHADQYKEQMEKANTRMKQ 1896
Cdd:pfam15921 784 EKNKMAGELEVLRSQERRLKE 804
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
862-1565 |
2.47e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 108.61 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 862 QVTRQEEELVAKDEELLKVKEKQSKVEGELVDMEQKHQQLVEEKNILAEQLHAETELFAEAEEMRARLAIKKQEMEEILR 941
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 942 DLE------------IRMEEEEERNQVLQNEKKKMQTHVQDLEEQLDEEEAAQKLQL-EKVTAEAKIKKMEEDILVLEDQ 1008
Cdd:TIGR02168 376 ELEeqletlrskvaqLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1009 NSKFLKEKKLLEERIAESTSQLAEEEEKaknLAKLKNKQEMMiSDLEERLKKEEKTRQELEKAKRKLDGETTDFQDQI-- 1086
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERE---LAQLQARLDSL-ERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIsv 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1087 -AELQAQIEelklqlAKKEEELQAALARGDEEVLQKNNTLKLVRELQAQIAELQE----DLESEKASRNKAEKQKRDLSE 1161
Cdd:TIGR02168 532 dEGYEAAIE------AALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSikgtEIQGNDREILKNIEGFLGVAK 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1162 ELEALKTELE-------------DTLDTTAAQQEL-------------------------------RTKREQEVAELRKS 1197
Cdd:TIGR02168 606 DLVKFDPKLRkalsyllggvlvvDDLDNALELAKKlrpgyrivtldgdlvrpggvitggsaktnssILERRREIEELEEK 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1198 IEEETRNhEAQIQEMRQRQATALEELSEQLEQAKRFKVNLEKNKQSLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQ 1277
Cdd:TIGR02168 686 IEELEEK-IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1278 ELHAKVLEGDRLRADMVEKSSKLQNELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQEETRQKLNQSSRIRQLE 1357
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1358 EEKNNLQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDdevgtieGLEEVKKKLLKDTEGLGQRLEEkiiayekLEKTK 1437
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERA-------SLEEALALLRSELEELSEELRE-------LESKR 910
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1438 NRLQQELDDLMvdlDHQRQIVSNLEKKQKKFDQL---LAEEKNISARHAEER-DRAEADAREKETKALSLARALDEA--- 1510
Cdd:TIGR02168 911 SELRRELEELR---EKLAQLELRLEGLEVRIDNLqerLSEEYSLTLEEAEALeNKIEDDEEEARRRLKRLENKIKELgpv 987
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 148223878 1511 -LEAQDEFERLNKQ---LRAEMEDLMSSKDDvgknvheLEKSKRALDqqvEEMRTQLEE 1565
Cdd:TIGR02168 988 nLAAIEEYEELKERydfLTAQKEDLTEAKET-------LEEAIEEID---REARERFKD 1036
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1128-1932 |
6.11e-23 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 107.46 E-value: 6.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1128 VRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQElrtKREQEVAELRKSIEEetrnHEA 1207
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKE---KREYEGYELLKEKEA----LER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1208 QIQEMRQRqataLEELSEQLEQAKRFKVNLEKNKQSLESDNKELATEVKSLqqmkAESEYKRKK-----LEGQVQELHAK 1282
Cdd:TIGR02169 238 QKEAIERQ----LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL----GEEEQLRVKekigeLEAEIASLERS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1283 VLEGDRLRADMVEKSSKLQNELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQEETRQKLNQSSRIRQLEEEKNN 1362
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1363 LQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQ 1442
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1443 ELDDLMVDLDhqrQIVSNLEKKQKKFDQLLAEeknisARHAEERDRAEADAREKETKALSLARALDEALEAQDE--FERL 1520
Cdd:TIGR02169 470 ELYDLKEEYD---RVEKELSKLQRELAEAEAQ-----ARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGEryATAI 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1521 NKQLRAEMEDLMSSKDDVGKNVHELEKSK---RALDQQVEEMRTQLEELEdelQGTEDAKLRLEVNMQAMKAQFE----- 1592
Cdd:TIGR02169 542 EVAAGNRLNNVVVEDDAVAKEAIELLKRRkagRATFLPLNKMRDERRDLS---ILSEDGVIGFAVDLVEFDPKYEpafky 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1593 --RDlqTRDEQNEEKKRALVKQVR--ELEAELED-----------ERKQRAMAVAIKKKLEMDMKDfesqIEAANKGRED 1657
Cdd:TIGR02169 619 vfGD--TLVVEDIEAARRLMGKYRmvTLEGELFEksgamtggsraPRGGILFSRSEPAELQRLRER----LEGLKRELSS 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1658 AIKQLRKLQAQTKDYQRELEEARASRDDIFAQSKENEKKLKGLEAEILQLQEELAASERSRRHAEQERDELADEISNSTS 1737
Cdd:TIGR02169 693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1738 GKSALLDEKRRLEARIAHLEEELEEEQsnMELLNDRFRKTTLQVDTLNSELAAERSSGQKSENARQQLERQNKELKAKLQ 1817
Cdd:TIGR02169 773 DLHKLEEALNDLEARLSHSRIPEIQAE--LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1818 ELEGSV------KSKFKATIATLESKIAQLEEQLEQEAKERVASNKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKAN 1891
Cdd:TIGR02169 851 SIEKEIenlngkKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930
|
810 820 830 840
....*....|....*....|....*....|....*....|.
gi 148223878 1892 TRMKQLKRqLEEAEEEATRANASARKLQRELDDATEANEVL 1932
Cdd:TIGR02169 931 EELSEIED-PKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
860-1698 |
2.39e-22 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 105.54 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 860 LLQVTRQEEELVAKDEEllkVKEKQSKVEGELVDMEqKHQQLVEEKNILA--EQLHAETELFAEAEEMRARLAIKKQEME 937
Cdd:TIGR02169 179 LEEVEENIERLDLIIDE---KRQQLERLRREREKAE-RYQALLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 938 EILRDLEIRMEEEEERNQVLQNEKKKMqthvqdlEEQLDEEEAAQKLQLEKVTAEakIKKMEEDILVLEDQNSKFLKEKK 1017
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKI-------KDLGEEEQLRVKEKIGELEAE--IASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1018 LLEERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKKEEKTRQELEKAKRKLDGETTDFQDQIAELQAQIEELK 1097
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1098 LQLAKKEEELQAALARGDE------EVLQKNNTLKLVRE-LQAQIAELQEDLESEKASRNKAEKQKRDLSE-------EL 1163
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADlnaaiaGIEAKINELEEEKEdKALEIKKQEWKLEQLAADLSKYEQELYDLKEeydrvekEL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1164 EALKTELeDTLDTTAAQQELRTKREQEVAELRKSIEEETRNHEAQIQEMRQRQATALEELSEQLEQAKRFKVNL--EKNK 1241
Cdd:TIGR02169 486 SKLQREL-AEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDAvaKEAI 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1242 QSLESDNKELATEVkSLQQMKAESEYKRKKLEGQVQELHAKVLEGDRLRADMVekSSKLQNELenVSSLLEEAEKKGIKL 1321
Cdd:TIGR02169 565 ELLKRRKAGRATFL-PLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAF--KYVFGDTL--VVEDIEAARRLMGKY 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1322 AkdVASMESQLQDTQELLQEETRQKLNQSSRIRQLEEEKNNLQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDDEVGT 1401
Cdd:TIGR02169 640 R--MVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1402 IEGLEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISAR 1481
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQ 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1482 haEERDRAEADAREKETKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKSKRALDQQVEEMRT 1561
Cdd:TIGR02169 798 --AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1562 QLEELEDELQGTEDAKLRLEVNMQAMKAQFER------DLQTRDEQNEEKKRALVKQVRELEAELEdERKQRAMAVAIKK 1635
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLRELERKIEEleaqieKKRKRLSELKAKLEALEEELSEIEDPKG-EDEEIPEEELSLE 954
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148223878 1636 KLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDIFAQSKENEKKLK 1698
Cdd:TIGR02169 955 DVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKR 1017
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
861-1499 |
6.96e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 104.07 E-value: 6.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 861 LQVTRQEEElVAKDEELLKVKEKQSKVEGELVDMEQKHQQLVE-EKNILAEQLHAETELFAEAEEmrARLAIKKQEMEEI 939
Cdd:PTZ00121 1178 AEAARKAEE-VRKAEELRKAEDARKAEAARKAEEERKAEEARKaEDAKKAEAVKKAEEAKKDAEE--AKKAEEERNNEEI 1254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 940 LRDLEIRMEEEEERNQVLQNEKKKMQTHVQDLEEQLDEEEAAQKLQLEKVTAEAK----IKKMEEDILVLEDQNSKFLKE 1015
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKkaeeAKKADEAKKKAEEAKKKADAA 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1016 KKLLEERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKK--------EEKTRQELEKAKRKLDGETTDFQDQIA 1087
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKadaakkkaEEKKKADEAKKKAEEDKKKADELKKAA 1414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1088 ELQAQIEELK--LQLAKKEEELQ--AALARGDEEVLQKNNTLKLVREL--QAQIAELQEDLESEKASRNKAEKQKRDlSE 1161
Cdd:PTZ00121 1415 AAKKKADEAKkkAEEKKKADEAKkkAEEAKKADEAKKKAEEAKKAEEAkkKAEEAKKADEAKKKAEEAKKADEAKKK-AE 1493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1162 ELEALKTELEDTLDTTAAQQELRTKREQEVAELRKSIEEETRNHEAQIQEmRQRQATALEELSEQLEQAKRFKVNLEKNK 1241
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAE-EKKKADELKKAEELKKAEEKKKAEEAKKA 1572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1242 QSLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELHAKVLEGDRLRADMVEKSSKLQNELENVSSLLEEAEKKGikl 1321
Cdd:PTZ00121 1573 EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA--- 1649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1322 akdvasmesqlqdtQELLQEETRQKLNQSSRIRQLEEEKNNLQEQQEEEEEARKSLekqilslqsqliEAKKKVDDEVGT 1401
Cdd:PTZ00121 1650 --------------EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAA------------EALKKEAEEAKK 1703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1402 IEGLEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISAR 1481
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
650
....*....|....*...
gi 148223878 1482 HAEERDRAEADAREKETK 1499
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIK 1801
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
823-1464 |
1.15e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.09 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 823 AKKQQQLIALKVLQRNCAAYLKLRHWQWWRLftkvkpllQVTRQEEELVAKDEELLKVKEKQSKVEGELVDMEQKHQQLV 902
Cdd:COG1196 209 AEKAERYRELKEELKELEAELLLLKLRELEA--------ELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 903 EEKNILAEQLHAETELFAEAEEMRARLAIKKQEMEEILRDLEIRMEEEEERNQVLQNEKkkmqthvqdleeqldeeeaaQ 982
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL--------------------E 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 983 KLQLEKVTAEAKIKKMEEDILVLEDQNSKFLKEKKLLEERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKKEE 1062
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1063 KTRQELEKAKRKLDGEttdfQDQIAELQAQIEELKLQLAKKEEELQAALARGDEEVLQKNNTLKLVRELQAQIAELQEDL 1142
Cdd:COG1196 421 EELEELEEALAELEEE----EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1143 ESEKASRN------KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVaelrksIEEETRNHEAQIQEMRQRQ 1216
Cdd:COG1196 497 LEAEADYEgflegvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNI------VVEDDEVAAAAIEYLKAAK 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1217 ATALEELSEQLEQAKRFKVNLEKNKQS------LESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELHAKVLEGDRLR 1290
Cdd:COG1196 571 AGRATFLPLDKIRARAALAAALARGAIgaavdlVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVT 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1291 ADMVEKSSKLQNELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQEETRQKLNQSSRIRQLEEEKNNLQEQQEEE 1370
Cdd:COG1196 651 LEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQL 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1371 EEARKSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLKDTEGLG---QR-LEEkiiaYEKLEKTKNRLQQELDD 1446
Cdd:COG1196 731 EAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGpvnLLaIEE----YEELEERYDFLSEQRED 806
|
650
....*....|....*...
gi 148223878 1447 LMVDLDHQRQIVSNLEKK 1464
Cdd:COG1196 807 LEEARETLEEAIEEIDRE 824
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1300-1901 |
1.19e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.09 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1300 LQNELE-NVSSLLEEAEK----KGIKLAKDVASMESQLQDTQELLQEETRQKlnqsSRIRQLEEEKNNLQEQQEEEEEAR 1374
Cdd:COG1196 194 ILGELErQLEPLERQAEKaeryRELKEELKELEAELLLLKLRELEAELEELE----AELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1375 KSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLKDTEGLGQRLEekiiayeklektknRLQQELDDLMVDLDHQ 1454
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE--------------ELEEELAELEEELEEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1455 RQIVSNLEKKQKKFDQLLAEEKNISARHAEERDRAEADAREKETKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSS 1534
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1535 KDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDELQGTEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRAlvKQVR 1614
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA--AARL 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1615 ELEAELEDERKQRAMAVAIKKKLemdmkdfesqieAANKGREDAIKQLRKLQAQTKDYQRELEEARA-----SRDDIFAQ 1689
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALLL------------AGLRGLAGAVAVLIGVEAAYEAALEAALAAALqnivvEDDEVAAA 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1690 SKENEKKLKGLEAEILQLQEELAASERSRRHAEQERDELADEISNSTSGKSALLDEKRRLEARIAHLEEELEEEQSNMEL 1769
Cdd:COG1196 562 AIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVT 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1770 LNDRFRKTTLQVDTLNSELAAERSSGQKSENARQQLERQNKELKAKLQELEGSVKSKFKATIATLESKIAQLEEQLEQEA 1849
Cdd:COG1196 642 LAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEEL 721
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 148223878 1850 KERVASNKLVRRTEKKLKEVFMQVEDERRHADQYKEQM---EKANTRMKQLKRQL 1901
Cdd:COG1196 722 EEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPpdlEELERELERLEREI 776
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
982-1623 |
1.19e-21 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 102.83 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 982 QKLQLEKV-TAEAKIKKMEEDILVLEDQNSKFLKEKKLLEERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKK 1060
Cdd:PRK03918 153 QILGLDDYeNAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1061 EEKTRQELEKAKR---KLDGETTDFQDQIAELQAQIEELKlqlaKKEEELqaalargdEEVLQKNNTLKLVRELQAQIAE 1137
Cdd:PRK03918 233 LEELKEEIEELEKeleSLEGSKRKLEEKIRELEERIEELK----KEIEEL--------EEKVKELKELKEKAEEYIKLSE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1138 LQEDLESEKasrNKAEKQKRDLSEELEALKTELEDtldttaaqqelRTKREQEVAELRKSIEEetrnheaqiqemRQRQA 1217
Cdd:PRK03918 301 FYEEYLDEL---REIEKRLSRLEEEINGIEERIKE-----------LEEKEERLEELKKKLKE------------LEKRL 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1218 TALEELSEQLEQAKRFKVNLEKNKQSLESDNKE-LATEVKSLQQMKAESEYKRKKLEGQVQELHAKVLEgdrlRADMVEK 1296
Cdd:PRK03918 355 EELEERHELYEEAKAKKEELERLKKRLTGLTPEkLEKELEELEKAKEEIEEEISKITARIGELKKEIKE----LKKAIEE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1297 SSKLQNELENVSSLLEEAEKKGI--KLAKDVASMESQLQDTQELLqEETRQKLNQSSRIRQLEEEKNNLQEQQEEEEEAR 1374
Cdd:PRK03918 431 LKKAKGKCPVCGRELTEEHRKELleEYTAELKRIEKELKEIEEKE-RKLRKELRELEKVLKKESELIKLKELAEQLKELE 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1375 KSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQELDDL-MVDLDH 1453
Cdd:PRK03918 510 EKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgFESVEE 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1454 QRQIVSNLEKKQKKFDQLLAEEKNISARHaEERDRAEADAREKETKalsLARALDEALEAQDEFERLNKQLRAE-MEDLM 1532
Cdd:PRK03918 590 LEERLKELEPFYNEYLELKDAEKELEREE-KELKKLEEELDKAFEE---LAETEKRLEELRKELEELEKKYSEEeYEELR 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1533 SSKDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDELQGTEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRALvKQ 1612
Cdd:PRK03918 666 EEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERAL-SK 744
|
650
....*....|.
gi 148223878 1613 VRELEAELEDE 1623
Cdd:PRK03918 745 VGEIASEIFEE 755
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
985-1754 |
2.19e-21 |
|
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: 102.07 E-value: 2.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 985 QLEKVTAEaKIKKMEEDILVLEDQNSKF---LKEKKLLEERIAESTSQLAEEEEKaknLAKLKNKqemmISDLEERLKKE 1061
Cdd:TIGR02169 199 QLERLRRE-REKAERYQALLKEKREYEGyelLKEKEALERQKEAIERQLASLEEE---LEKLTEE----ISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1062 EKTRQEL-EKAKRKLDGETTDFQDQIAELQAQIEELKLQLAKKEEELQAALARGDEEVLQKNNTLKLVRELQAQIAELQE 1140
Cdd:TIGR02169 271 EQLLEELnKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1141 DLES--------------------EKASRNKAEKQK-RDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELRKSIE 1199
Cdd:TIGR02169 351 RRDKlteeyaelkeeledlraeleEVDKEFAETRDElKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIA 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1200 EEtrnhEAQIQEMRQRQATALEELSEQLEQAKRFKVNLEKNKQSLESDNKELA---TEVKSLQQMKAESEYKRKKLE--- 1273
Cdd:TIGR02169 431 GI----EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDrveKELSKLQRELAEAEAQARASEerv 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1274 ------------------------GQVQELHAKVLE---GDRLRADMVE------------KSSKLQ-------NELENV 1307
Cdd:TIGR02169 507 rggraveevlkasiqgvhgtvaqlGSVGERYATAIEvaaGNRLNNVVVEddavakeaiellKRRKAGratflplNKMRDE 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1308 SSLLEEAEKKG-IKLAKDVASMESQ--------LQDT----------------------QELLQEE------TRQKLNQS 1350
Cdd:TIGR02169 587 RRDLSILSEDGvIGFAVDLVEFDPKyepafkyvFGDTlvvedieaarrlmgkyrmvtleGELFEKSgamtggSRAPRGGI 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1351 SRIRQLEEEKNNLQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLKDTEGLGQRLEEKIIAY 1430
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1431 EKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARhaEERDRAEADAREKETKALSLARALDEA 1510
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQ--AELSKLEEEVSRIEARLREIEQKLNRL 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1511 LEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKskraldqQVEEMRTQLEELEdelqgtedaklrlevnmqamkaq 1590
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG-------KKEELEEELEELE----------------------- 874
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1591 ferdlqtrdeqneekkralvKQVRELEAELEDERKQRamavaikKKLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTK 1670
Cdd:TIGR02169 875 --------------------AALRDLESRLGDLKKER-------DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1671 DYQRELEEARASRDDIfAQSKENEKKLKGLEAEILQLQEELAASERSRRHAEQERDELADEISNSTSGKSALLDEKRRLE 1750
Cdd:TIGR02169 928 ALEEELSEIEDPKGED-EEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
....
gi 148223878 1751 ARIA 1754
Cdd:TIGR02169 1007 ERIE 1010
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
878-1565 |
3.01e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.55 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 878 LKVKEKQSKVEGELVDMEQKHQQLVEEKNILAEQLHAETELFAEAEEMRARLAIKKQEMEEILRDLEirmeeeeernqvl 957
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE------------- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 958 qnekkkmqthvqdleeqldeeeaaqKLQLEKVTAEAKIKKMEEDILVLEDQNSKFLKEKKLLEERIAESTSQLAEEEEKA 1037
Cdd:COG1196 285 -------------------------EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1038 KNLAKLKNKQEMMISDLEERLKKEEKTRQELEKAKRKLDGETTDFQDQIAELQAQIEELKLQLAKKEEELQAALARgdee 1117
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER---- 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1118 vlqKNNTLKLVRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELR-- 1195
Cdd:COG1196 416 ---LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAar 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1196 -KSIEEETRNHEAQIQEMRQRQATALEELSEQLEQAKRFKVNLEKNKQSLESDNKELATEVKSLQQMKAESEYKRKKLEG 1274
Cdd:COG1196 493 lLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1275 QVQELHAKVLEGDRLRADMVEKSSKLQNELENVSSLLEEAEKkgiklakdvasmESQLQDTQELLQEETRQKLNQSSRIR 1354
Cdd:COG1196 573 RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADAR------------YYVLGDTLLGRTLVAARLEAALRRAV 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1355 QLEEEKNNLQEQQEEEEEARKSLEKQILSLQSQLIEAKKKvddevgtIEGLEEVKKKLLKDTEGLGQRLEEKIIAYEKLE 1434
Cdd:COG1196 641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE-------LEELAERLAEEELELEEALLAEEEEERELAEAE 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1435 KTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKnisarHAEERDRAEADAREKETKAlSLAR-------AL 1507
Cdd:COG1196 714 EERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE-----LPEPPDLEELERELERLER-EIEAlgpvnllAI 787
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 148223878 1508 DEALEAQDEFERLNKQLraemEDLMSSKDDvgknvheLEKSKRALDqqvEEMRTQLEE 1565
Cdd:COG1196 788 EEYEELEERYDFLSEQR----EDLEEARET-------LEEAIEEID---RETRERFLE 831
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
866-1435 |
3.61e-21 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 101.29 E-value: 3.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 866 QEEELVAKDEELLKVKEKQSKVEGELVDMEQKHQQLVEEKNILAEqlhAETELFAEAEEMRArLAIKKQEMEEILRDLEI 945
Cdd:PRK03918 198 KEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE---LEKELESLEGSKRK-LEEKIRELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 946 RMEEEEERNQVLQNEKKKMQTHVQDLEEQLDEEEAAQKLQLEKVTAEAKIKKMEEDILVLEDQNSkflkEKKLLEERIAE 1025
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE----RLEELKKKLKE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1026 STSQLAEEEEKAKNLAKLKNKQEMM-----------ISDLEERLKKEEKTRQELEKAKRKLDGETTDFQDQIAELQAQIE 1094
Cdd:PRK03918 350 LEKRLEELEERHELYEEAKAKKEELerlkkrltgltPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1095 ELKlqLAKKEEELQAALARGDEEvlqknntLKLVRELQAQIAELQEDLEsekasrnKAEKQKRDLSEELEALKTELEdtl 1174
Cdd:PRK03918 430 ELK--KAKGKCPVCGRELTEEHR-------KELLEEYTAELKRIEKELK-------EIEEKERKLRKELRELEKVLK--- 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1175 dttaaqQELRTKREQEVAELRKSIEEETRNHEAqiqEMRQRQATALEELSEQLEQAKRFKVNLEKNKQSLESDNKELATE 1254
Cdd:PRK03918 491 ------KESELIKLKELAEQLKELEEKLKKYNL---EELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAEL 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1255 VKSLQqmkaESEYKRKKLEGQVQELHAKVLEGDRLRADMVEKSSKLQNELENVSSLLEEAEKKGIKLAKDVASMESQLQD 1334
Cdd:PRK03918 562 EKKLD----ELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1335 TQELLqEETRQKLNQSSRIRQlEEEKNNLQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLK 1414
Cdd:PRK03918 638 TEKRL-EELRKELEELEKKYS-EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
570 580
....*....|....*....|...
gi 148223878 1415 DTEGLG--QRLEEKIIAYEKLEK 1435
Cdd:PRK03918 716 LEKALErvEELREKVKKYKALLK 738
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
904-1735 |
1.74e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 96.36 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 904 EKNILAEQLHAETELFAEAEEMRARLAIKKQEMEEILRDLE-IRMEEEEERNQVLQNEKKKMQTHVQDLEEQLDEEEAAQ 982
Cdd:PTZ00121 1085 EDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEdARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDAR 1164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 983 KLQLEKVTAEAKikKMEEdilvledqNSKFLKEKKLLEERIAESTSQlAEEEEKAKNLAKLKNKQEMMISDLEERLKKEE 1062
Cdd:PTZ00121 1165 KAEEARKAEDAK--KAEA--------ARKAEEVRKAEELRKAEDARK-AEAARKAEEERKAEEARKAEDAKKAEAVKKAE 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1063 KTRQELEKAKR----KLDGETTDFQD-QIAELQAQIEELKLQLAKKEEELQAALARGDEEVLQKNNTLKLVRELQAQIAE 1137
Cdd:PTZ00121 1234 EAKKDAEEAKKaeeeRNNEEIRKFEEaRMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE 1313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1138 lqedlesekasRNKAEKQKRDlSEELEALKTELEDTLDTTAAQQELRTKREQEVAELRKSIEEETRNHEAQIQEMRqRQA 1217
Cdd:PTZ00121 1314 -----------AKKADEAKKK-AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK-KKA 1380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1218 TALEELSEQLEQAKRFKVNLEKNKQSLES------------DNKELATEVKSLQQMKAESEYKRKKLEGQVQELHAKVLE 1285
Cdd:PTZ00121 1381 DAAKKKAEEKKKADEAKKKAEEDKKKADElkkaaaakkkadEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAE 1460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1286 GDRLRADMVEKSSKLQNELENVSSlLEEAEKK---GIKLAKDVASMESQLQDTQELLQEETRQK---LNQSSRIRQLEEE 1359
Cdd:PTZ00121 1461 EAKKKAEEAKKADEAKKKAEEAKK-ADEAKKKaeeAKKKADEAKKAAEAKKKADEAKKAEEAKKadeAKKAEEAKKADEA 1539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1360 KNnlQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVKK-KLLKDTEGLGQRLEEKIIAYEKLEKTKN 1438
Cdd:PTZ00121 1540 KK--AEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1439 RLQ--QELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARHAEERDRAEADAREKE--TKALSLARALDEALEAQ 1514
Cdd:PTZ00121 1618 AKIkaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEeaKKAEEDEKKAAEALKKE 1697
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1515 DEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDElqgtEDAKLRLevnmqamkAQFERD 1594
Cdd:PTZ00121 1698 AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD----EEEKKKI--------AHLKKE 1765
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1595 LQTRDEQNEEKKRALVKQvreleaELEDERKQRAMAVAIKKKlemDMKD-FESQIEAANKG-------REDAIKQLRKLq 1666
Cdd:PTZ00121 1766 EEKKAEEIRKEKEAVIEE------ELDEEDEKRRMEVDKKIK---DIFDnFANIIEGGKEGnlvindsKEMEDSAIKEV- 1835
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148223878 1667 AQTKDYQRelEEARASRDDIFAQSKENEK---KLKGLEAEILQLQEELAASERSRRHAEQERDELADEISNS 1735
Cdd:PTZ00121 1836 ADSKNMQL--EEADAFEKHKFNKNNENGEdgnKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNN 1905
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1014-1888 |
2.85e-19 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 95.42 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1014 KEKKLLEERIAEStSQLAEEEEKAKNLAKLKNKQEMMISDLEE------RLKKEEKTRQE---------LEKAKRKLDGE 1078
Cdd:pfam02463 153 ERRLEIEEEAAGS-RLKRKKKEALKKLIEETENLAELIIDLEElklqelKLKEQAKKALEyyqlkekleLEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1079 TTDFQDQIAELQAQIEELKLQLAKKEEELQAALARGDEEVLQKNNTLKLVRELQAQIAELQEDLESEKASRNKAEKQKRD 1158
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVD 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1159 LSEELEALKTELEDTLDTTAAQQELRTKREQEVAELRKSIEEEtrnhEAQIQEMRQRQATALEELSEQLEQAKRFKVNLE 1238
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAE----EEEEEELEKLQEKLEQLEEELLAKKKLESERLS 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1239 KnKQSLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELHAKVLEGDRLRADMVEKSSKLQNELENVSSLLEEAEKKG 1318
Cdd:pfam02463 388 S-AAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELE 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1319 IKLAKDVASMESQLQDTQELLQEETRQKLNQSSRIRQLEEEKNNLQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDDE 1398
Cdd:pfam02463 467 LKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIS 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1399 vgTIEGLEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQIvsNLEKKQKKFDQLLAEEKNI 1478
Cdd:pfam02463 547 --TAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPIL--NLAQLDKATLEADEDDKRA 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1479 SARHAEERDRAEADAREKETKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKSK---RALDQQ 1555
Cdd:pfam02463 623 KVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEilrRQLEIK 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1556 VEEMRTQLEELEDELQGTEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRALVKQVRELEAELEDERKQRAMAVAIKK 1635
Cdd:pfam02463 703 KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREK 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1636 KLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEA-----RASRDDIFAQSKENEKKLKGLEAEILQLQEE 1710
Cdd:pfam02463 783 TEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQeekikEEELEELALELKEEQKLEKLAEEELERLEEE 862
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1711 LAASERSRRHAEQERDELADEISNSTSGKSALLDEKRRLEARIAHLEEELEEEQSNMELLNDRFRKTTLQVDTLNSELAA 1790
Cdd:pfam02463 863 ITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLL 942
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1791 ERSSGQKSENARQQLERQNKELKAKLQELEGSVKSKFKATIATLESKIAQLEEQLEQEAKERVASNKLVRRTEKKLKEVF 1870
Cdd:pfam02463 943 EEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEF 1022
|
890
....*....|....*...
gi 148223878 1871 MQVEDERRHADQYKEQME 1888
Cdd:pfam02463 1023 LELFVSINKGWNKVFFYL 1040
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
992-1581 |
6.79e-19 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 93.55 E-value: 6.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 992 EAKIKKMEEDILVLEDQ----NSKFLKEKKLLEERIAESTsqLAEEEEKAKNLAKLKNKQEmmISDLEERLKKEEKTRQE 1067
Cdd:TIGR04523 67 EEKINNSNNKIKILEQQikdlNDKLKKNKDKINKLNSDLS--KINSEIKNDKEQKNKLEVE--LNKLEKQKKENKKNIDK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1068 LEKAKRKLDGETTDFQDQIAELQAQIEELKLQLAKKEEEL---QAALARGDEEVLQKNNTLKLVRELQAQIAELQEDLES 1144
Cdd:TIGR04523 143 FLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKlniQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1145 EKASRNKAEKQKRDLSEELEALKTELEDTldttaaqqelrtkrEQEVAELRKSIEEETRNHEAQIQEMRQrQATALEELS 1224
Cdd:TIGR04523 223 LKKQNNQLKDNIEKKQQEINEKTTEISNT--------------QTQLNQLKDEQNKIKKQLSEKQKELEQ-NNKKIKELE 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1225 EQLEQAKRFKVNLEKNKQslESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELHAKVLEGDRLRADMVEKSSKLQNEL 1304
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1305 ENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQEETRQKLNQSSRIRQLEEEKNnlqeqqeeeeearkSLEKQILSL 1384
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE--------------LLEKEIERL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1385 QSQLIEAKKKVDDEVGTIEGLEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK 1464
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1465 QKKFDQLLAEEKNISARHAEERDRAEADAREKETKALSLARALD-EALEAQ-DEFERLNKQLRAEMEDLMSSKDDVGKNV 1542
Cdd:TIGR04523 512 VKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKkENLEKEiDEKNKEIEELKQTQKSLKKKQEEKQELI 591
|
570 580 590
....*....|....*....|....*....|....*....
gi 148223878 1543 HELEKSKRALDQQVEEMRTQLEELEDELQGTEDAKLRLE 1581
Cdd:TIGR04523 592 DQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
917-1731 |
9.40e-19 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 93.50 E-value: 9.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 917 ELFAEAEEMRARLAIKKQEMEEILRDLEIRMEEEEERNQVLQ----------NEKKKMQTHVQDLEEQLDEEEAAQKLQL 986
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKlkeqakkaleYYQLKEKLELEEEYLLYLDYLKLNEERI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 987 EKVTAEAKIKKMEEDILVLEDQNSKFLKEKKLLEerIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKKEEKTRQ 1066
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKE--NKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1067 ELEKAKRKLDGETTDFQDQIAELQAQIEELKLQLAKKEEELQAALARGDEEVLQKNNTLKLVRELQAQIAELQEDLESEK 1146
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEEL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1147 ASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKR---EQEVAELRKSIEEETRNHEAQIQEMRQRQATALEEL 1223
Cdd:pfam02463 398 ELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESielKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKET 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1224 SEQLEQAKRFKVNLEKNKQ---SLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELHAKVLEGDRLRADMVEKSSKL 1300
Cdd:pfam02463 478 QLVKLQEQLELLLSRQKLEersQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1301 QNELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQEETRQKLNQSSRIRQLEEEKNNLQEQQEEEEEARKSLEKQ 1380
Cdd:pfam02463 558 DEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKL 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1381 ILSLQSQLIEAKKKVDDEVGTIEGLeEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQELDDLMvDLDHQRQIVSN 1460
Cdd:pfam02463 638 KESAKAKESGLRKGVSLEEGLAEKS-EVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKK-EQREKEELKKL 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1461 LEKKQKKFDQLLAEEKNISARHAEERDRAEADAREKETK---------ALSLARALDEALEAQDEFERLNKQLRAEMEDL 1531
Cdd:pfam02463 716 KLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKsrlkkeekeEEKSELSLKEKELAEEREKTEKLKVEEEKEEK 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1532 MSSKDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDELQGTEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRALVK 1611
Cdd:pfam02463 796 LKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLK 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1612 QVRELEAELEDERKQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDIFAQSK 1691
Cdd:pfam02463 876 EEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK 955
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 148223878 1692 ENEKKLKGLEAEILQLQEELAASERSRRHAEQERDELADE 1731
Cdd:pfam02463 956 EEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDEL 995
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
863-1749 |
1.52e-18 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 93.11 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 863 VTRQEEELVAKDEELLKVKEKQSKVEGELVDMEQKHQQLVEEKNILAEQLHAETELFAEAEEMRA--RLAIKKQEMEEIL 940
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYldYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 941 RDLEIRMEEEEERNQVLQNEKKKMQThvqdleeqldeeeaaqkLQLEKVTAEAKIKKMEEDILVLEDQNSKFLKEKKLLE 1020
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQ-----------------VLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1021 ERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKKEEKTRQELEKAKrkldgettDFQDQIAELQAQIEELKLQL 1100
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEE--------EELEKLQEKLEQLEEELLAK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1101 AKKEEELQAALARGDEEVLQKNNTLKLVRELQAQIAELQEDL---ESEKASRNKAEKQKRDLSEELEALKTELEDTLDTT 1177
Cdd:pfam02463 379 KKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLlkeEKKEELEILEEEEESIELKQGKLTEEKEELEKQEL 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1178 AAQQELRTKREQEVAELRKSIEEETRNHEAQIQEMRQRQATALEELSEQLEQAKR-FKVNLEKNKQSLESDNKELATEVK 1256
Cdd:pfam02463 459 KLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLaLIKDGVGGRIISAHGRLGDLGVAV 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1257 SLQQMKAESEYKRKKLEGQVQELHAKVLEGDRLRADMVEKSSKLQNELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQ 1336
Cdd:pfam02463 539 ENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADED 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1337 ELLQEETRQKLNQSSRIRQLEEEKNNLQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLKDT 1416
Cdd:pfam02463 619 DKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQ 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1417 EglgqRLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARHAEERDRAEADAREK 1496
Cdd:pfam02463 699 L----EIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEK 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1497 ETKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDELQGTEDA 1576
Cdd:pfam02463 775 ELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEE 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1577 KLRLEVNMQAMKAQFERDLQTRDEQNEEKKRALVKQVRELEAELEDERKQRamavaikkkLEMDMKDFESQIEAANKGRE 1656
Cdd:pfam02463 855 ELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEE---------SQKLNLLEEKENEIEERIKE 925
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1657 DAIKQLRKLQAQTKDYQRELEEARASRDDIFAQSKENEKKLKGLEAEILQLQEELAASERSRRHAEQERDELADEISNST 1736
Cdd:pfam02463 926 EAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKK 1005
|
890
....*....|...
gi 148223878 1737 SGKSALLDEKRRL 1749
Cdd:pfam02463 1006 KLIRAIIEETCQR 1018
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1329-1945 |
1.90e-18 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 92.55 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1329 ESQLQDTQELLQEETRQKLNQSSRIRQLEEEKNNLQEQQEEE-------EEARKSLEKQILSLQSQLIEAKKKVDDEVGT 1401
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAEtelcaeaEEMRARLAARKQELEEILHELESRLEEEEER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1402 IEGLEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEeknISAR 1481
Cdd:pfam01576 91 SQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE---FTSN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1482 HAEErdraeadarEKETKALSLARALDEALEAQDEfERLNKQlraemedlmsskddvGKNVHELEKSKRALDQQVEEMRT 1561
Cdd:pfam01576 168 LAEE---------EEKAKSLSKLKNKHEAMISDLE-ERLKKE---------------EKGRQELEKAKRKLEGESTDLQE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1562 QLEELEDELQGTEDAKLRLEVNMQAMKAQFErDLQTRDEQNEEKKRALVKQVRELEAELEDERKQRAMAVAIKKKLEMDM 1641
Cdd:pfam01576 223 QIAELQAQIAELRAQLAKKEEELQAALARLE-EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEEL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1642 KDFESQIEAAnKGREDAIKQLR-KLQAQTKDYQRELE-EARASRDDIFAQSKENEKKLKGLEAEILQLQEELAASERSRR 1719
Cdd:pfam01576 302 EALKTELEDT-LDTTAAQQELRsKREQEVTELKKALEeETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1720 HAEQERDELADEISNSTSGKSALLDEKRRLEARIAHLEEELEEEQSNMELLNDRFRKTTLQVDTLNSELAAERSSGQKSE 1799
Cdd:pfam01576 381 ALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1800 NARQQLERQNKELKAKLQElEGSVKSKFKATIATLESKIAQLEEQLEQEAKERVASNKLVRRTEKKLKEVFMQVEDERRH 1879
Cdd:pfam01576 461 KDVSSLESQLQDTQELLQE-ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGT 539
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148223878 1880 ADQYKEQMEKANTRMKQLKRQLEEAEEEATRANASARKLQRELDDATEANEVLSREVSTLKNRLRR 1945
Cdd:pfam01576 540 LEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKK 605
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
844-1541 |
2.45e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 92.51 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 844 KLRHWQWWRLFTKVKPLLQVTRQ---EEELVAKDEELLKVKEKQSKVEGELVDMEQKhqqlVEEKNILAEQLHAETELFA 920
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQaaiKAEEARKADELKKAEEKKKADEAKKAEEKKK----ADEAKKKAEEAKKADEAKK 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 921 EAEEMRARLAIKKQEMEEILRDLEIRMEEEEERNQVLQNEKKKMQTHVQDLEEQLDEEEAAQKLQLEKVTA-EAKI---- 995
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAdEAKKkaee 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 996 -KKMEEDILVLEDQNSKFLKEKKLLEE-RIAESTSQLAEEEEKAKnlaKLKNKQEMMISDLEERLKKEEKTRQELEKAKR 1073
Cdd:PTZ00121 1403 dKKKADELKKAAAAKKKADEAKKKAEEkKKADEAKKKAEEAKKAD---EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKA 1479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1074 KLDGETTDFQDQIAELQAQIEELKlqlAKKEEELQAALARGDEEVLQKNNTLKLVRELQAQIAELQEDLESEKASRNKAE 1153
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAK---KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1154 KQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELRKSIEEETRNHEAQIQEMRQRQATAlEELSEQLEQAKRF 1233
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA-EELKKAEEEKKKV 1635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1234 ----KVNLEKNKQSLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQElhakvlEGDRLRADMVEKSSKLQNELENVSS 1309
Cdd:PTZ00121 1636 eqlkKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE------EDEKKAAEALKKEAEEAKKAEELKK 1709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1310 LLEEAEKKgiklAKDVASMESQLQDTQELLQEETRQKLNQSSRIRQLEEEKNNLQEQQEEEEEARKSLEKQilslQSQLI 1389
Cdd:PTZ00121 1710 KEAEEKKK----AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE----KEAVI 1781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1390 EAKKKVDDEVGTIEglEEVKKKLLKDTEGLGQRLEEKIIAYekLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFD 1469
Cdd:PTZ00121 1782 EEELDEEDEKRRME--VDKKIKDIFDNFANIIEGGKEGNLV--INDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKN 1857
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148223878 1470 QLLAEEKNISARHAEERDRAEADareketkalslaralDEALEAQDEFERLNKQlraEMEDLMSSKDDVGKN 1541
Cdd:PTZ00121 1858 NENGEDGNKEADFNKEKDLKEDD---------------EEEIEEADEIEKIDKD---DIEREIPNNNMAGKN 1911
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
985-1582 |
2.92e-17 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 88.64 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 985 QLEKVTAEAKiKKMEEDILVLEDQNSKFLKEKKL----LEERIAESTSQLAEEEEKAKNLA-KLKNKQEMMISDLEERLK 1059
Cdd:pfam15921 246 QLEALKSESQ-NKIELLLQQHQDRIEQLISEHEVeitgLTEKASSARSQANSIQSQLEIIQeQARNQNSMYMRQLSDLES 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1060 KEEKTRQELEKAKRKldgettdFQDQIaelqaqiEELKLQLAKKEEELQAALARGDEEVLQKNNTLKLVRELQAQIAELQ 1139
Cdd:pfam15921 325 TVSQLRSELREAKRM-------YEDKI-------EELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKRE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1140 EDLESEKASRNKAEKQKRDLSEELEALKTELED------TLDT--TAAQQELRTKREQEVAELRKSIE--EETRNHEAQI 1209
Cdd:pfam15921 391 KELSLEKEQNKRLWDRDTGNSITIDHLRRELDDrnmevqRLEAllKAMKSECQGQMERQMAAIQGKNEslEKVSSLTAQL 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1210 QEMRQRQATALEELSEQ---LEQAKR----FKVNLEKNKQSLESDNKELaTEVKSLQQMKAESEYKRKKLEGQVQELHAk 1282
Cdd:pfam15921 471 ESTKEMLRKVVEELTAKkmtLESSERtvsdLTASLQEKERAIEATNAEI-TKLRSRVDLKLQELQHLKNEGDHLRNVQT- 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1283 vlEGDRLRADMVEKSSK---LQNELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQEETRQKLNQSSRIRQLEEE 1359
Cdd:pfam15921 549 --ECEALKLQMAEKDKVieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEAR 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1360 KNNLQEQQEEEEEA---RKSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLKDTEglgqrleekiiayEKLEKT 1436
Cdd:pfam15921 627 VSDLELEKVKLVNAgseRLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKS-------------EEMETT 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1437 KNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQL-LAEEKNISARhaeerdRAEADARekETKALSLARALDEALEAQD 1515
Cdd:pfam15921 694 TNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVaMGMQKQITAK------RGQIDAL--QSKIQFLEEAMTNANKEKH 765
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148223878 1516 EFERLNKQLRAEMEDLMSSKDDVGKNVHELEKSKRALDQQVEEMRT-------QLEELEDELQGTEDAKLRLEV 1582
Cdd:pfam15921 766 FLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEValdkaslQFAECQDIIQRQEQESVRLKL 839
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
993-1820 |
3.89e-17 |
|
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: 88.57 E-value: 3.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 993 AKIKKMEEDILVLEDQNSKFLKEKKLLEERIAESTSQLAEEeekaknLAKLKNKQEMMISDLEERLKKEEKTRQELEKAK 1072
Cdd:TIGR00606 262 SKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQ------LNDLYHNHQRTVREKERELVDCQRELEKLNKER 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1073 RKLDGETTDFQDQIAELQAQIEELKLQLAKKEEELQA--------ALARGDEEVLQKNNTLKLVRELQAQIAELQEDLES 1144
Cdd:TIGR00606 336 RLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSlatrleldGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCA 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1145 EKASRNK-AEKQKRDLSEELEALKTELE-DTLDTTAAQQELRTKR---EQEVAELRKSIEEETRNHEAQIQEMRQRQATA 1219
Cdd:TIGR00606 416 DLQSKERlKQEQADEIRDEKKGLGRTIElKKEILEKKQEELKFVIkelQQLEGSSDRILELDQELRKAERELSKAEKNSL 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1220 LEELSEQLEQAKRFKVNLEKNKQSLESDNKELATEVKSLQQMKAESEYKRKKLEgQVQELHAKVLEGDRLRADMVEKSSK 1299
Cdd:TIGR00606 496 TETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDE-QIRKIKSRHSDELTSLLGYFPNKKQ 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1300 LQNELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQEETRQKLNQSSRIRQL---EEEKNNLQEQQEEEEEARKS 1376
Cdd:TIGR00606 575 LEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsQDEESDLERLKEEIEKSSKQ 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1377 LE--KQILSLQSQLIEAKKK--------VDDEVGTIEGLEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQELDD 1446
Cdd:TIGR00606 655 RAmlAGATAVYSQFITQLTDenqsccpvCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPG 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1447 LMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARhaEERDRAEADAREKETKALSLARALDEALEAQ-DEFERLNKQLR 1525
Cdd:TIGR00606 735 RQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE--QETLLGTIMPEEESAKVCLTDVTIMERFQMElKDVERKIAQQA 812
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1526 AEME--DLMSSKDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDELQGTEDAKLRLevnmQAMKAQFERDLQTRdEQNE 1603
Cdd:TIGR00606 813 AKLQgsDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNEL----KSEKLQIGTNLQRR-QQFE 887
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1604 EKKRALVKQVRELEAELEDERKQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIKQLRKlqaqtkdyqrELEEARASR 1683
Cdd:TIGR00606 888 EQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKE----------KVKNIHGYM 957
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1684 DDIFAQSKEN-EKKLKGLEAEILQLQEELAASERSRRHAEQERDELADEISNSTSGKSALLDEKRRLEARIAHLEEELEE 1762
Cdd:TIGR00606 958 KDIENKIQDGkDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEEL 1037
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 148223878 1763 EQSNMELLNDRFRKTTLQVDTLNSELAAERSSGQKSENARQQLERQNKELKAKLQELE 1820
Cdd:TIGR00606 1038 KQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1145-1890 |
6.39e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 87.72 E-value: 6.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1145 EKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELRKSIEEETRNHEAQIQEMRQRQATALEELS 1224
Cdd:pfam02463 170 KKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1225 EQLEQAKRFKVNLEKNKQSLESDNKELATEVKSLQQMKAE--SEYKRKKLEGQVQELHAKVLEGDRLRADMvEKSSKLQN 1302
Cdd:pfam02463 250 QEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKllAKEEEELKSELLKLERRKVDDEEKLKESE-KEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1303 ELENVSSLLEEAEKKGIKLAKDVASMESQLQDtQELLQEETRQKLNQSSRIRQLEEEKNNLQEQQEEEEEARKSLEKQIL 1382
Cdd:pfam02463 329 ELKKEKEEIEELEKELKELEIKREAEEEEEEE-LEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1383 SLQSQLieAKKKVDDEVGTIEGLEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLE 1462
Cdd:pfam02463 408 QLLLEL--ARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1463 KKQKKFDQLLAEEKNISARHAEERDRAEADAREKETKALSLARALDEALEAQDEferlnKQLRAEMEDLMSSKDDVGKNV 1542
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVE-----NYKVAISTAVIVEVSATADEV 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1543 HELEKSKRALDQQVEEMRTQLEELEDELqgteDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRALVKQVRELEAELED 1622
Cdd:pfam02463 561 EERQKLVRALTELPLGARKLRLLIPKLK----LPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTK 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1623 ERKQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDIFAQS----KENEKKLK 1698
Cdd:pfam02463 637 LKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKeqreKEELKKLK 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1699 GLEAEILQ--LQEELAASERSRRHAEQERDELADEISNSTSGKSALLDEKRRLEARIAHLEEELEEEQSNMELLNDRfRK 1776
Cdd:pfam02463 717 LEAEELLAdrVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKE-EK 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1777 TTLQVDTLNSELAAERSSGQKSENARQQLERQNKELKAKLQELEGSVKSKFKATIATLESKIAQLEEQLEQEAKERVASn 1856
Cdd:pfam02463 796 LKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLL- 874
|
730 740 750
....*....|....*....|....*....|....
gi 148223878 1857 KLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKA 1890
Cdd:pfam02463 875 KEEELEEQKLKDELESKEEKEKEEKKELEEESQK 908
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
875-1549 |
1.59e-16 |
|
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: 85.93 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 875 EELLKVKEKQSKVEGELvdmEQKHQQLVEEKNILAEQLHAETELFAEAEEMRARLAIKKQEMEEI-------------LR 941
Cdd:pfam05483 85 KEAEKIKKWKVSIEAEL---KQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLikennatrhlcnlLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 942 DLEIRMEEEEERNQVLQNEKKKMQTHVQDLEEQLDEEEAAQKLQLEKVTAEAKIKkMEEDILVLEDQNSKFLKEKKLLEE 1021
Cdd:pfam05483 162 ETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFK-LKEDHEKIQHLEEEYKKEINDKEK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1022 RIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKKEEKTRQELEKAKRKLDGETTD----FQDQIAELQAQIEELK 1097
Cdd:pfam05483 241 QVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDikmsLQRSMSTQKALEEDLQ 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1098 LQLAKKEEELQAALARGDEEVLQKNNTLKLVRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTT 1177
Cdd:pfam05483 321 IATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFK 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1178 AAQQ----ELRT-----------------------KREQEVAELRKSIEEETRNHEAQIQEMR---QRQATALEELSEQL 1227
Cdd:pfam05483 401 NNKEveleELKKilaedeklldekkqfekiaeelkGKEQELIFLLQAREKEIHDLEIQLTAIKtseEHYLKEVEDLKTEL 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1228 EQAKRFKVNLEKNKQSLESDNKELATE----VKSLQQMKAESEYKRKKLEGQVQELHAKVLEGDRLRADMVEKSSKLQNE 1303
Cdd:pfam05483 481 EKEKLKNIELTAHCDKLLLENKELTQEasdmTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQK 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1304 LENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQEETRQKLNQSSRIRQLEEEKNNLQEQQEEEEEARKSLEKQILS 1383
Cdd:pfam05483 561 GDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNK 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1384 LQSQLIEAKKKVDDEVGTIEglEEVKKKLLKDTEGLGQRLEEKIIAYEKLektknRLQQELDdlmVDLDHQ-RQIVSNLE 1462
Cdd:pfam05483 641 LELELASAKQKFEEIIDNYQ--KEIEDKKISEEKLLEEVEKAKAIADEAV-----KLQKEID---KRCQHKiAEMVALME 710
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1463 KKQKKFDQLLaeeknisarhaEERDRAEADAREKETKALSLARALDEALE-AQDEFERLNKQLRAEMEDLMSSKDDVGKN 1541
Cdd:pfam05483 711 KHKHQYDKII-----------EERDSELGLYKNKEQEQSSAKAALEIELSnIKAELLSLKKQLEIEKEEKEKLKMEAKEN 779
|
....*...
gi 148223878 1542 VHELEKSK 1549
Cdd:pfam05483 780 TAILKDKK 787
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1604-1925 |
4.36e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.60 E-value: 4.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1604 EKKRALVKQVRELEAELEdeRKQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIKQLRKLQAqtkdyqrELEEARASR 1683
Cdd:COG1196 206 ERQAEKAERYRELKEELK--ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA-------ELEELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1684 DDIFAQSKENEKKLKGLEAEILQLQEELAASERSRRHAEQERDELADEISnstsgksALLDEKRRLEARIAHLEEELEEE 1763
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA-------ELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1764 QSNMELLNDRFRKTTLQVDTLNSELAAERSSGQKSENARQQLERQNKELKAKLQELEgsvkskfkATIATLESKIAQLEE 1843
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE--------EAEEALLERLERLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1844 QLEQEAKERVASNKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANTRMKQLKRQLEEAEEEATRANASARKLQRELD 1923
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
..
gi 148223878 1924 DA 1925
Cdd:COG1196 502 DY 503
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
983-1711 |
1.14e-15 |
|
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: 83.48 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 983 KLQLEKVTAEAKIKKMEEDILVLEDQNSKFLKEKKLLEERIAESTSQLAEEEEKAKnLAKLKNKQEMMISDLEERLKKEE 1062
Cdd:TIGR00618 202 RSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK-KQQLLKQLRARIEELRAQEAVLE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1063 KTRQELEKAKRKLdgettdfqdQIAELQAQIEELKLQLAKKEEELQAALARGDEEVLQKNNTLKLVRELQAQIAELQEDL 1142
Cdd:TIGR00618 281 ETQERINRARKAA---------PLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLH 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1143 ESEKASRNKAEKQKRDLSEELEAlkTELEDTLDTTAAQQELRTKREQEVAELRKSIEEETRNHEAQIQE---MRQRQATA 1219
Cdd:TIGR00618 352 SQEIHIRDAHEVATSIREISCQQ--HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAfrdLQGQLAHA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1220 LEELSEQLEQAKRFKVNLEKNKQSLESDNKELateVKSLQQMKAeseykRKKLEGQVQELHAKVLEGDRLRADMVEKSSK 1299
Cdd:TIGR00618 430 KKQQELQQRYAELCAAAITCTAQCEKLEKIHL---QESAQSLKE-----REQQLQTKEQIHLQETRKKAVVLARLLELQE 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1300 LQNELENVSSLLEEAEKKGIKLAKDVASMESQLQdtqellqeetrqklnqssRIRQLEEEKNNLQEQQEEEEEARKSLEK 1379
Cdd:TIGR00618 502 EPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQ------------------TYAQLETSEEDVYHQLTSERKQRASLKE 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1380 QILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLKDTEGLgqrLEEKIIAYEKLEKTKNRLQQELDDLMVDLdHQRQIVs 1459
Cdd:TIGR00618 564 QMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKL---SEAEDMLACEQHALLRKLQPEQDLQDVRL-HLQQCS- 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1460 nlEKKQKKFDQLLAEEKNIsarhAEERDRaEADAREKETKALSLARALDEALEAQDEFERLN------KQLRAEMEDLMS 1533
Cdd:TIGR00618 639 --QELALKLTALHALQLTL----TQERVR-EHALSIRVLPKELLASRQLALQKMQSEKEQLTywkemlAQCQTLLRELET 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1534 SKDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDELQGTEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRALVKQV 1613
Cdd:TIGR00618 712 HIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFN 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1614 RELEaelEDERKQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEarasrddiFAQSKEN 1693
Cdd:TIGR00618 792 RLRE---EDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLK--------YEECSKQ 860
|
730
....*....|....*...
gi 148223878 1694 EKKLKGLEAEILQLQEEL 1711
Cdd:TIGR00618 861 LAQLTQEQAKIIQLSDKL 878
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1153-1898 |
1.59e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 83.27 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1153 EKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELRKSIEEETRNHEA-QIQEMRQRQATALEELSEQLEQAK 1231
Cdd:PTZ00121 1085 EDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDArKAEEARKAEDAKRVEIARKAEDAR 1164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1232 RFKVNlEKNKQSLESDNKELATEVKSLQQMKAESEYKR----KKLEGQVQELHAKVLEGDRlRADMVEKSSKLQNELENV 1307
Cdd:PTZ00121 1165 KAEEA-RKAEDAKKAEAARKAEEVRKAEELRKAEDARKaeaaRKAEEERKAEEARKAEDAK-KAEAVKKAEEAKKDAEEA 1242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1308 SSLLEEAEKKGIKLAKDvASMESQLQDTQELLQEETRQ--KLNQSSRIRQLEEEKNNLQEQQEEEEEARKSLEKQILSLQ 1385
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEE-ARMAHFARRQAAIKAEEARKadELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAK 1321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1386 SQLIEAKKKVDDEVGTIE---GLEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLE 1462
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEeakKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE 1401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1463 KKQKKFDQL--LAEEKNIS---ARHAEERDRAEaDAREKETKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDD 1537
Cdd:PTZ00121 1402 EDKKKADELkkAAAAKKKAdeaKKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE 1480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1538 VGKNVHELEKSKRALDQQVEEMRTQLEELE--DELQGTEDAKlrlevnmqamKAQFERDLQTRDEQNEEKKRALVKQVRE 1615
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKAAEAKKkaDEAKKAEEAK----------KADEAKKAEEAKKADEAKKAEEKKKADE 1550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1616 LEAELEDERKQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKdyQRELEEARasrddifaqsKENEK 1695
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK--KMKAEEAK----------KAEEA 1618
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1696 KLKGleaeilqlqEELAASERSRRHAEQERDELADEISNSTSGKSALLDEKRRLEariahleeeleeeqsnmellndrfr 1775
Cdd:PTZ00121 1619 KIKA---------EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAA------------------------- 1664
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1776 kttlqvdtlnSELAAERSSGQKSENARQQLERQNKELKAKLQELEGSVKSKFKATIATLESKIAQLEEQLEQEAKERVAS 1855
Cdd:PTZ00121 1665 ----------EEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE 1734
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 148223878 1856 NKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANTRMKQLK 1898
Cdd:PTZ00121 1735 AKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1410-1945 |
1.94e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.40 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1410 KKLLKDTEGLGQRLEEKIIAYEK--LEKTKNRLQQELDDLMVDLDHqrqivsnLEKKQKKFDQLLAEEKNISARHAEERD 1487
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIEEKEEkdLHERLNGLESELAELDEEIER-------YEEQREQARETRDEADEVLEEHEERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1488 RAE----------ADAREKETKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKSKRALDQQVE 1557
Cdd:PRK02224 252 ELEtleaeiedlrETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1558 EMRTQLEELEDELQGTEDAKLRLEvnMQAMKAQFE-RDLQTRDEQNEEKKRALVKQVRELEAELEDERKQRAMAvaikkk 1636
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLE--ERAEELREEaAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA------ 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1637 lEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDD--------------IFAQSKENEKKLKGLEA 1702
Cdd:PRK02224 404 -PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1703 EILQLQEELAASErsrrhaeqERDELADEISNSTSGKSALLDEKRRLEARIAHLEEELEEEQSNMELLNDRfrkttlqVD 1782
Cdd:PRK02224 483 ELEDLEEEVEEVE--------ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER-------AA 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1783 TLNSELAAERSSGQKSENARQQLERQNKELKAKLQELEGSVKSKfkATIATLESKIAQLEEQLEqeakervasnklvRRT 1862
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL--ERIRTLLAAIADAEDEIE-------------RLR 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1863 EKKlkEVFMQVEDERRhadqykEQMEKANTRMKQLKRQ-----LEEAEEEATRANASARKLQRELDDATEANEVLSREVS 1937
Cdd:PRK02224 613 EKR--EALAELNDERR------ERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIG 684
|
....*...
gi 148223878 1938 TLKNRLRR 1945
Cdd:PRK02224 685 AVENELEE 692
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1185-1900 |
2.07e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 82.88 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1185 TKREQEVAELRKSIEEETRNHEAQIQEMRQRQATALEELSEQLEQAKRFKVNLEKNKQSLESDNKELATEVKSLQQMKAE 1264
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRV 1154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1265 SEYKR----KKLEGQVQELHAKVLEGDRlRADMVEKSSKLQnELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQ 1340
Cdd:PTZ00121 1155 EIARKaedaRKAEEARKAEDAKKAEAAR-KAEEVRKAEELR-KAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1341 EETRQKLNQSsriRQLEEEKNNLQEQQEEEEEARKSLEKQilslQSQLIEAKKKVDD--EVGTIEGLEEVKK-KLLKDTE 1417
Cdd:PTZ00121 1233 EEAKKDAEEA---KKAEEERNNEEIRKFEEARMAHFARRQ----AAIKAEEARKADElkKAEEKKKADEAKKaEEKKKAD 1305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1418 GLGQRLEEKIIAyEKLEKTKNRLQQELDDLMvdldhqrqivSNLEKKQKKFDQLLAEEKNISARHAEERDRAEADAREKE 1497
Cdd:PTZ00121 1306 EAKKKAEEAKKA-DEAKKKAEEAKKKADAAK----------KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1498 TkalslARALDEALEAQDEFERLNKQLRAEMEDLMSSKDDVgknvheleKSKRALDQQVEEMRTQLEELEDELQGTEDAK 1577
Cdd:PTZ00121 1375 E-----AKKKADAAKKKAEEKKKADEAKKKAEEDKKKADEL--------KKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1578 LRLEVNMQAMKAQFERDLQTRDEQNEEKKRAlvkqvRELEAELEDERKqramAVAIKKKLEMDMKdfesQIEAANKGRED 1657
Cdd:PTZ00121 1442 EAKKADEAKKKAEEAKKAEEAKKKAEEAKKA-----DEAKKKAEEAKK----ADEAKKKAEEAKK----KADEAKKAAEA 1508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1658 AIKQLRKLQAQTKDYQRELEEARASRDDIFAQSKENEKKlkgleAEILQLQEELAASERSRRHAEQERDELADEISNSTS 1737
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK-----ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA 1583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1738 GKSALLDEKRRLEARIAHLEEELEEEQSNMELLNDRFRKTTLQvdtlnselAAERSSGQKSENARQQLERQNKELKAKLQ 1817
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK--------KAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1818 ELEGSVKSKFKATIATLESKIAqlEEQLEQEAKERVASNKLVRRTE--KKLKEVFMQVEDERRHADQYKEQMEKANTRMK 1895
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEEDKKKA--EEAKKAEEDEKKAAEALKKEAEeaKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
....*
gi 148223878 1896 QLKRQ 1900
Cdd:PTZ00121 1734 EAKKE 1738
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1235-1940 |
2.83e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 82.50 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1235 VNLEKNKQSLESDNKELATEVKSLQQMKAES-EYKRKKLEGQVQELHAKVLEGDRLRADMVEKSSKLQNeLENVSSLLEE 1313
Cdd:PTZ00121 1024 FNIEKIEELTEYGNNDDVLKEKDIIDEDIDGnHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEA-TEEAFGKAEE 1102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1314 AEKKGIKLAKDVASMESQLQDTQELLQEETRQKLNQSSRIRQLEEEKNNLQEQQEEEEEARKSLEKQILSLQSQLIEAKK 1393
Cdd:PTZ00121 1103 AKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAAR 1182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1394 KVDD--EVGTIEGLEEVKK--------KLLKDTEGLGQRLEEKIIAYEKLEKTKNRlqQELDDLMVDLDHQRQIVSNLEK 1463
Cdd:PTZ00121 1183 KAEEvrKAEELRKAEDARKaeaarkaeEERKAEEARKAEDAKKAEAVKKAEEAKKD--AEEAKKAEEERNNEEIRKFEEA 1260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1464 KQKKFDQLLAEEKNISARHAEERDRAEADAREKETKALSLARALDEALEAQDEFERlnkqlraemedlmssKDDVGKNVH 1543
Cdd:PTZ00121 1261 RMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKK---------------ADEAKKKAE 1325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1544 ELEKSKRALDQQVEEMRTQLEELEDElqgTEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRAL-VKQVRELEAELED 1622
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEAAKAE---AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEeKKKADEAKKKAEE 1402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1623 ERKQramAVAIKKKLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDdifaQSKENEKKLKGLEA 1702
Cdd:PTZ00121 1403 DKKK---ADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEE----AKKKAEEAKKADEA 1475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1703 EilQLQEELAASERSRRHAEQERDElADEISNSTSGKSALLDEKRRLEARIAHLEEELEEEQSNMELLNDRFRKTTLQVD 1782
Cdd:PTZ00121 1476 K--KKAEEAKKADEAKKKAEEAKKK-ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1783 TLNSELAAERSsgQKSENARQQLERQNKELKaKLQELEGSVKSKFKATIATLESKIAQLEEQLEQEAKERVASNKLVRRT 1862
Cdd:PTZ00121 1553 KAEELKKAEEK--KKAEEAKKAEEDKNMALR-KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1863 E--KKLKEVFMQVEDERRHADQYKEQMEKANTRMKQL-------KRQLEEAEEEATRANASARKLQRELDDATEANEVLS 1933
Cdd:PTZ00121 1630 EekKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEakkaeedKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709
|
....*..
gi 148223878 1934 REVSTLK 1940
Cdd:PTZ00121 1710 KEAEEKK 1716
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1305-1884 |
2.90e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.03 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1305 ENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQEETRQKLnqssRIRQLEEEKNNLQEQQEEEEEARKSLEKQILSL 1384
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK----ELEELKEEIEELEKELESLEGSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1385 QSQLIEAKKKvddevgtIEGLEEVKKKLlkdteglgQRLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK 1464
Cdd:PRK03918 265 EERIEELKKE-------IEELEEKVKEL--------KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1465 QKKFDQLLAEEKNISARHAEERDRAEadarEKETKAlslaRALDEALEAQDEFERLNKQLRAEmedlmsSKDDVGKNVHE 1544
Cdd:PRK03918 330 IKELEEKEERLEELKKKLKELEKRLE----ELEERH----ELYEEAKAKKEELERLKKRLTGL------TPEKLEKELEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1545 LEKSKRALDQQVEEMRTQLEELEDELQGTEDAKLRLEvnmqamKAQFERDLQTRDEQNEEKKRALvkqvRELEAELEDER 1624
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK------KAKGKCPVCGRELTEEHRKELL----EEYTAELKRIE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1625 KQRAMAVAIKKKLEMDMKDFESQIEAANKGR--EDAIKQLRKLQAQTKDYQRE-LEEARASRDDIFAQSKENEKKLKGLE 1701
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKESELIklKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1702 AEILQLQE---ELAASERSRRHAEQERDELADEISNSTSGKSALLDEK---------------------RRLEARIAHLE 1757
Cdd:PRK03918 546 KELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEERlkelepfyneylelkdaekelEREEKELKKLE 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1758 EELEEEQSNMELLNDRFRKTTLQVDTLNSELAAErssgqKSENARQQLERQNKELKAKLQELEGsvkskfkatiatLESK 1837
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKYSEE-----EYEELREEYLELSRELAGLRAELEE------------LEKR 688
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 148223878 1838 IAQLEEQLEqEAKERVASNKLVRRTEKKLKEVFMQVEDERRHADQYK 1884
Cdd:PRK03918 689 REEIKKTLE-KLKEELEEREKAKKELEKLEKALERVEELREKVKKYK 734
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
888-1265 |
3.37e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 82.04 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 888 EGELVDMEQKHQQLVEEKNILAEQLhaeTELFAEAEEMRARLAIKKQEMEEILRDLEIRMEEEEERNQVLQNEKKKMQth 967
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSEL---RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS-- 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 968 vqdleeqldeeeaaqKLQLEKVTAEAKIKKMEEDILVLEDQNSKFLKEKKLLEERIAEStsQLAEEEEKAKNLAKLKNKQ 1047
Cdd:TIGR02169 748 ---------------SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS--RIPEIQAELSKLEEEVSRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1048 EMMISDLEERLKKEEKTRQELEKAKRKLDGETTDFQDQIAELQAQIEELKLQLAKKEEELQaalargdeevlqknntlkl 1127
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE------------------- 871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1128 vrELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELRKSIEEETRNHEA 1207
Cdd:TIGR02169 872 --ELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE 949
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1208 -----QIQEMRQRQATALEELS-------EQLEQAKRFKVNLEKNKQSLESDNKELATEVKSLQQMKAES 1265
Cdd:TIGR02169 950 elsleDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1116-1735 |
4.26e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 81.50 E-value: 4.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1116 EEVLQKNNTLKLVRELQAQIAELQEdleSEKASRnKAEKQKRDLsEELEALKTELEDTLDTTAAQQELRTKREQEVAELR 1195
Cdd:COG4913 215 EYMLEEPDTFEAADALVEHFDDLER---AHEALE-DAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1196 KsieEETRNHEAQIQEMRQRQATALEELSEQLEQAKRFKVNLEKNKQSLESDNKE-LATEVKSLQQMKAESEYKRKKLEG 1274
Cdd:COG4913 290 L---ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1275 QVQELHAKVLEGdrlRADMVEKSSKLQNELENVSSLLEEAEKkgiklakDVASMESQLQDtqelLQEETRQKlnqSSRIR 1354
Cdd:COG4913 367 LLAALGLPLPAS---AEEFAALRAEAAALLEALEEELEALEE-------ALAEAEAALRD----LRRELREL---EAEIA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1355 QLEEEKNNLQEQQEEeeeARKSLEKQILSLQSQ------LIEAKKKVDDEVGTIEGL----------------------E 1406
Cdd:COG4913 430 SLERRKSNIPARLLA---LRDALAEALGLDEAElpfvgeLIEVRPEEERWRGAIERVlggfaltllvppehyaaalrwvN 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1407 EVKKKLLKDTEGLGQRLEEKIIA-------YEKLEKTKNRLQQELDDLMV------------DLDHQR-------QIVSN 1460
Cdd:COG4913 507 RLHLRGRLVYERVRTGLPDPERPrldpdslAGKLDFKPHPFRAWLEAELGrrfdyvcvdspeELRRHPraitragQVKGN 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1461 LEKKQKKFDQLLAEE-----KNISARHAEERDRAEADAREKE-TKALSLARALDEALEAQDE---------FERLN-KQL 1524
Cdd:COG4913 587 GTRHEKDDRRRIRSRyvlgfDNRAKLAALEAELAELEEELAEaEERLEALEAELDALQERREalqrlaeysWDEIDvASA 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1525 RAEMEDLMSSKDDVGKNVHELekskRALDQQVEEMRTQLEELEDELQGTEDAKLRLEVNMQamkaqferDLQTRDEQNEE 1604
Cdd:COG4913 667 EREIAELEAELERLDASSDDL----AALEEQLEELEAELEELEEELDELKGEIGRLEKELE--------QAEEELDELQD 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1605 KKRALVKQVRELEAELEDERKQRAMAVAIKKKLemdMKDFESQIEAANKGREDAIKQLRKLQAQ-TKDYQRELEEARASR 1683
Cdd:COG4913 735 RLEAAEDLARLELRALLEERFAAALGDAVEREL---RENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADL 811
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 148223878 1684 DDIFaqskENEKKLKGLEAEIL-QLQEELAasERSRRHAEQERDELADEISNS 1735
Cdd:COG4913 812 ESLP----EYLALLDRLEEDGLpEYEERFK--ELLNENSIEFVADLLSKLRRA 858
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1292-1898 |
7.43e-15 |
|
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: 80.45 E-value: 7.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1292 DMVEKSSKLQNELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQEETRQKLNQSSRIRQLEEEKNNLQEQQEEEE 1371
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1372 EARKSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQELDDLMVDL 1451
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1452 DHQRQIVSNLEKKQKKFDQLLAEEKNISARHAEERDRAEADAREKETKALSLARALDEALEAQDEFERLNKQLRAEMEDL 1531
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1532 MSSK---DDVGKNVHELEKSKRALDQQVE-----EMRTQLEELEDELQGTEDAKLRLEVNMQAMK---AQFERDLQTRDE 1600
Cdd:TIGR04523 277 EQNNkkiKELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNeqiSQLKKELTNSES 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1601 QNEEKKRalvkQVRELEAELEDERKQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEAR 1680
Cdd:TIGR04523 357 ENSEKQR----ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1681 ASR-------DDIFAQSKENEKKLKGLEAEILQLQEELAASERSRRHAEQERDELADEISNSTSGKSALLDEKRRLEARI 1753
Cdd:TIGR04523 433 ETIiknnseiKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1754 AHLEEELEEEQSNMELLNDRFRKTTLQVDTLNSELAAERSSGQKS----------------ENARQQLERQNKELKAKLQ 1817
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEnlekeideknkeieelKQTQKSLKKKQEEKQELID 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1818 ELEgSVKSKFKATIATLESKIAQLEEQLEQEAKERVASNKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANTRMKQL 1897
Cdd:TIGR04523 593 QKE-KEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKES 671
|
.
gi 148223878 1898 K 1898
Cdd:TIGR04523 672 K 672
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
860-1640 |
1.01e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 80.40 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 860 LLQVTRQEEELVAKDEELLKVKEKQSKVEGELVDMEQKHQQLVEEknilaeqlhaETELFAEAEEMRARLAIKKQEMEEI 939
Cdd:pfam02463 288 LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKK----------EKEEIEELEKELKELEIKREAEEEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 940 LRDLEIRMEEEEERNQVLQNEKKKMQTHVQDLEEQLDEEEAAQKLQLEKVTAEAKIKKMEEDIL-VLEDQNSKFLKEKKL 1018
Cdd:pfam02463 358 EEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLkEEKKEELEILEEEEE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1019 LEERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKKEEKTRQELEKAKRKLDgettdfqdqiaelqaqiEELKL 1098
Cdd:pfam02463 438 SIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKL-----------------EERSQ 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1099 QLAKKEEELQAALARGDEEVLQKNNTLKLVRELQAQIAELqEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTA 1178
Cdd:pfam02463 501 KESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVEN-YKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARK 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1179 AQQELRTKREQEVAELRKSIEEETRNHEAQIQEMRQRQATALEELSEQLEQAKRFKVNLEKNKQSLESDNK----ELATE 1254
Cdd:pfam02463 580 LRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKgvslEEGLA 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1255 VKSLQQMKAESEYKRKKLEGQVQELHAKVLEGDRLRADMVEKSSKLQNELENVSSLLEEAEKkgIKLAKDVASMESQLQD 1334
Cdd:pfam02463 660 EKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEE--LLADRVQEAQDKINEE 737
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1335 TQELLQEETRQKLNQSSRIRQLEEEKNNLQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDDEvgtiegLEEVKKKLLK 1414
Cdd:pfam02463 738 LKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEE------ELRALEEELK 811
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1415 DTEGLGQRLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARHAEERDRaeadaR 1494
Cdd:pfam02463 812 EEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLK-----D 886
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1495 EKETKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDELQGTE 1574
Cdd:pfam02463 887 ELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLL 966
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1575 DAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRALVKQVRELEAELEDERKQR----AMAVAIKKKLEMD 1640
Cdd:pfam02463 967 LAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLkeflELFVSINKGWNKV 1036
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1014-1232 |
1.44e-14 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 77.88 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1014 KEKKLLEERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKKEEKTRQELEKAKRKLDGETTDFQDQIAELQAQI 1093
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1094 EEL--KLQLAKKEEELQAALARGDEEVLQKNNTL--KLVRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTE 1169
Cdd:COG4942 107 AELlrALYRLGRQPPLALLLSPEDFLDAVRRLQYlkYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148223878 1170 LedtldttAAQQELRTKREQEVAELRKSIEEEtrnhEAQIQEMrQRQATALEELSEQLEQAKR 1232
Cdd:COG4942 187 R-------AALEALKAERQKLLARLEKELAEL----AAELAEL-QQEAEELEALIARLEAEAA 237
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
985-1630 |
1.68e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.57 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 985 QLEKVTAEA-KIKKMEEDILVLEDQNSKF-----LKEKKLLEERIAESTSQLAEEEEKaknlaklknkqemmISDLEERL 1058
Cdd:COG4913 253 LLEPIRELAeRYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAE--------------LERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1059 KKEEKTRQELEKAKRKLDGettdfqDQIAELQAQIEELKLQLAKKEEELQAALARGDEEVLQKNNTLKLVRELQAQIAEL 1138
Cdd:COG4913 319 DALREELDELEAQIRGNGG------DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1139 QEDLESEKAsrnKAEKQKRDLSEELEALKTELEDTldttaaqqelrtkrEQEVAELRKSIeeetRNHEAQIQEMRQRQAT 1218
Cdd:COG4913 393 LEALEEELE---ALEEALAEAEAALRDLRRELREL--------------EAEIASLERRK----SNIPARLLALRDALAE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1219 ALE----------EL----------------------------SEQLEQAKRFkVNLEKNKQSLESDnkELATEVKSLQQ 1260
Cdd:COG4913 452 ALGldeaelpfvgELievrpeeerwrgaiervlggfaltllvpPEHYAAALRW-VNRLHLRGRLVYE--RVRTGLPDPER 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1261 MKAES-------EYKRKKLEGQVQEL------HAKVLEGDRLR---------------ADMVEKSSKLQNELENV----- 1307
Cdd:COG4913 529 PRLDPdslagklDFKPHPFRAWLEAElgrrfdYVCVDSPEELRrhpraitragqvkgnGTRHEKDDRRRIRSRYVlgfdn 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1308 SSLLEEAEKKGIKLAKDVASMESQLQDTQELLQeETRQKLNQSSRIRQLEEEKNNLqeqqeeeeearKSLEKQILSLQSQ 1387
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELD-ALQERREALQRLAEYSWDEIDV-----------ASAEREIAELEAE 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1388 LieakKKVDDEVGTIEGLEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK--Q 1465
Cdd:COG4913 677 L----ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAllE 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1466 KKFDQLLAE--EKNISARHAEERDRAEADAREKETKALSLARA-----------LDEALEAQDEFERLNKQLRAemEDLM 1532
Cdd:COG4913 753 ERFAAALGDavERELRENLEERIDALRARLNRAEEELERAMRAfnrewpaetadLDADLESLPEYLALLDRLEE--DGLP 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1533 SSKDDVGKNVHELEKSK-----RALDQQVEEMRTQLEELEDELQGTE---DAKLRLEVNMQ--AMKAQFERDLQ------ 1596
Cdd:COG4913 831 EYEERFKELLNENSIEFvadllSKLRRAIREIKERIDPLNDSLKRIPfgpGRYLRLEARPRpdPEVREFRQELRavtsga 910
|
730 740 750
....*....|....*....|....*....|....*
gi 148223878 1597 -TRDEQNEEKKRALVKQVRELEAELEDERKQRAMA 1630
Cdd:COG4913 911 sLFDEELSEARFAALKRLIERLRSEEEESDRRWRA 945
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1298-1878 |
2.17e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 79.31 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1298 SKLQNELENVSSLLEEAEKKGikLAKDVASMESQLQDTQELLQEETRQKlnqsSRIRQLEEEKNNLQEQQEEEEEARKSL 1377
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEKEEKD--LHERLNGLESELAELDEEIERYEEQR----EQARETRDEADEVLEEHEERREELETL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1378 EKQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQI 1457
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1458 VSNLEKKQKkfdqllaeeknisaRHAEERDRAEADAREKETKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDD 1537
Cdd:PRK02224 337 AQAHNEEAE--------------SLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1538 VGKNVHELEKSKRALDQQVEEMRTQLEELEDELQGTEDAKLRLEVNMQAMKA-------QFERDLQTRDEQNEekkralv 1610
Cdd:PRK02224 403 APVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCpecgqpvEGSPHVETIEEDRE------- 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1611 kQVRELEAELEDERKQRAmavAIKKKLEM--DMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDIFA 1688
Cdd:PRK02224 476 -RVEELEAELEDLEEEVE---EVEERLERaeDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEA 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1689 QSKENEKKLKGLEAEILQLQEELAASERSRRHAEQERDELADeISNSTSGKSALLDEKRRLEARIAHLEEELEEEQSNME 1768
Cdd:PRK02224 552 EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIERLREKREALAELNDERRERLA 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1769 LLNDRfrkttlqVDTLNSELAAERSSGQKSEnaRQQLERQNKELKAKLQELEGSvKSKFKATIATLESKIAQLEEQLEQ- 1847
Cdd:PRK02224 631 EKRER-------KRELEAEFDEARIEEARED--KERAEEYLEQVEEKLDELREE-RDDLQAEIGAVENELEELEELRERr 700
|
570 580 590
....*....|....*....|....*....|..
gi 148223878 1848 -EAKERVASNKLVRRTEKKLKEVFMQVEDERR 1878
Cdd:PRK02224 701 eALENRVEALEALYDEAEELESMYGDLRAELR 732
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1150-1891 |
2.25e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 79.24 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1150 NKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELrKSIEEETRNHEAQIQEMRQRQATALEELSEQLEQ 1229
Cdd:TIGR00618 159 KAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRS-QLLTLCTPCMPDTYHERKQVLEKELKHLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1230 AK------RFKVNLEKNKQSLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQElhAKVLEGDRLRADMVEKSSKLQNE 1303
Cdd:TIGR00618 238 TQqshaylTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKA--APLAAHIKAVTQIEQQAQRIHTE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1304 LENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQEETRQklnqssrirqleEEKNNLQEQQEEEEEARKSLEKQILS 1383
Cdd:TIGR00618 316 LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHI------------RDAHEVATSIREISCQQHTLTQHIHT 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1384 LQSQLIEAKKKVDDEVGTIEGLEEVKKKLlkDTEGLGQRLEEKIIAyeKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEK 1463
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELDILQREQATI--DTRTSAFRDLQGQLA--HAKKQQELQQRYAELCAAAITCTAQCEKLEKI 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1464 KQKKFDQLLAEEKNisarhaEERDRAEADAREKETKALSLARALDEAlEAQDEFERLNKQLRAEMEDLMSSKDDVGK--- 1540
Cdd:TIGR00618 460 HLQESAQSLKEREQ------QLQTKEQIHLQETRKKAVVLARLLELQ-EEPCPLCGSCIHPNPARQDIDNPGPLTRRmqr 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1541 ---NVHELEKSKRALDQQVEEMRTQLEELEDELQGTEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEkkralvkqvreLE 1617
Cdd:TIGR00618 533 geqTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDL-----------TE 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1618 AELEDERKQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTK-DYQRELEEARASRDDIFAQSKENEKK 1696
Cdd:TIGR00618 602 KLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTlTQERVREHALSIRVLPKELLASRQLA 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1697 LKGLEAEILQL---QEELAASE---RSRRHAEQERDELADEISNSTSGKSALLDekrrleariAHLEEELEEEQSNMELL 1770
Cdd:TIGR00618 682 LQKMQSEKEQLtywKEMLAQCQtllRELETHIEEYDREFNEIENASSSLGSDLA---------AREDALNQSLKELMHQA 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1771 NDRFRKTTLQVDTLNSELAAERSSGQKSENARQQLERQNK-------ELKAKLQELEGSVKSKFKATIATLEsKIAQLEE 1843
Cdd:TIGR00618 753 RTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRlreedthLLKTLEAEIGQEIPSDEDILNLQCE-TLVQEEE 831
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 148223878 1844 QLEQEAKERVASNKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKAN 1891
Cdd:TIGR00618 832 QFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1001-1444 |
1.29e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 76.62 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1001 DILVLEDQNSKFLKEKKLLEERIAESTSQLAEEEEKAKNLAKlknkqemMISDLEERLKKEEKTRQELEKAKRKLDGETT 1080
Cdd:PRK02224 308 DAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRE-------DADDLEERAEELREEAAELESELEEAREAVE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1081 DFQDQIAELQAQIEELKLQLAKKEEELQAALARGDEEVLQKNntlklvrELQAQIAELQEDLESEKASRNKAEkqkrdls 1160
Cdd:PRK02224 381 DRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERD-------ELREREAELEATLRTARERVEEAE------- 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1161 EELEALK-----TELEDTLDTTAAqQELRTKREqEVAELRKSIEEETRNHEAQIQEMRQRQATAlEELSEQLEQAKRFKV 1235
Cdd:PRK02224 447 ALLEAGKcpecgQPVEGSPHVETI-EEDRERVE-ELEAELEDLEEEVEEVEERLERAEDLVEAE-DRIERLEERREDLEE 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1236 NLEKNKQSLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELHAKVLEGDRLRADMVEKSSKLQNeLENVSSLLEEAE 1315
Cdd:PRK02224 524 LIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES-LERIRTLLAAIA 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1316 KKGiklaKDVASMESQLQDTQElLQEETRQKLNQ-SSRIRQLEEE--KNNLQEQQEEEEEARKSLEKQILSLQsQLIEAK 1392
Cdd:PRK02224 603 DAE----DEIERLREKREALAE-LNDERRERLAEkRERKRELEAEfdEARIEEAREDKERAEEYLEQVEEKLD-ELREER 676
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 148223878 1393 KKVDDEVGTIEG----LEEVKKKlLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQEL 1444
Cdd:PRK02224 677 DDLQAEIGAVENeleeLEELRER-REALENRVEALEALYDEAEELESMYGDLRAEL 731
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
991-1501 |
2.41e-13 |
|
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: 75.63 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 991 AEAKIKKMEediLVLEDQNSKFLKEKKLLEERiaestSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKKEEktrQELEK 1070
Cdd:pfam10174 190 AEMQLGHLE---VLLDQKEKENIHLREELHRR-----NQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLE---DEVQM 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1071 AKRKLDGETTDFQDQIAELQA----------QIEELKLQLAKKEEELQAALARGDE------------EVLQKNNTLKLV 1128
Cdd:pfam10174 259 LKTNGLLHTEDREEEIKQMEVykshskfmknKIDQLKQELSKKESELLALQTKLETltnqnsdckqhiEVLKESLTAKEQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1129 RE--LQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAqqelrtkREQEVAELRKSIE---EETR 1203
Cdd:pfam10174 339 RAaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDV-------KERKINVLQKKIEnlqEQLR 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1204 NHEAQIQEMRQRQA----------TALEELSEQLEQAKRFKVNLEKNKqslESDNKELATEVKSLQQmkaeseykrkkle 1273
Cdd:pfam10174 412 DKDKQLAGLKERVKslqtdssntdTALTTLEEALSEKERIIERLKEQR---EREDRERLEELESLKK------------- 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1274 gQVQELHAKVlegDRLRADMVEKSSKLQNELENVSSLLEEAEKKGIKLAK----------DVASMESQLQDTQElLQEET 1343
Cdd:pfam10174 476 -ENKDLKEKV---SALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSleiaveqkkeECSKLENQLKKAHN-AEEAV 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1344 RQKLNQSSRIRQLEEEKN--------------NLQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVK 1409
Cdd:pfam10174 551 RTNPEINDRIRLLEQEVArykeesgkaqaeveRLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEM 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1410 KKllkdteGLGQRLEEKIiaYEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARHAEERDRA 1489
Cdd:pfam10174 631 KK------KGAQLLEEAR--RREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQ 702
|
570
....*....|..
gi 148223878 1490 EADAREKETKAL 1501
Cdd:pfam10174 703 LEEILEMKQEAL 714
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1220-1943 |
3.55e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 75.39 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1220 LEELSEQLEQAKRFKVNLEKnKQSLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELHAKVLEGDRLRADMVEKSSK 1299
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKL-IEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1300 LQNELENVSSLLEEAEKKGIKLAKDVASMesqLQDTQELLQEETRQKLNQSSRIRQLEEEKNNLQEQQEEEEEARKSLEK 1379
Cdd:pfam02463 238 RIDLLQELLRDEQEEIESSKQEIEKEEEK---LAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1380 QILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLKDTEglgqRLEEKIIAYEKLEKTKNRLQQELDDLMVDLdhqrqivS 1459
Cdd:pfam02463 315 KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKRE----AEEEEEEELEKLQEKLEQLEEELLAKKKLE-------S 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1460 NLEKKQKKFDQLLAEEKNISARHAEERDRAEADAREKETKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDDVG 1539
Cdd:pfam02463 384 ERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKD 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1540 KNVHELEKSKRALDQQVEEMRTQLEELEDELQGTEDAKLRLEVNMQAMKAQFERDLQTRD---EQNEEKKRALVKQVREL 1616
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRiisAHGRLGDLGVAVENYKV 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1617 EAELEDERKQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDI---FAQSKEN 1693
Cdd:pfam02463 544 AISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLeadEDDKRAK 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1694 EKKLKGLEAEILQLQEELAASERSRRHAEQERDELADEISNSTSGKSALLDEKRRLEARIAHLEEELEEEQSNMELLNDR 1773
Cdd:pfam02463 624 VVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1774 FRKTTLQVDTLNSELAAERSSGQKSENARQQLERQNKELKAKLQELEGSVKSKFKATiaTLESKIAQLEEQLEQEAKERV 1853
Cdd:pfam02463 704 KEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKE--EKEEEKSELSLKEKELAEERE 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1854 ASNKLVRRTEKKLKEVFMQVEDERrhadQYKEQMEKANTRMKQLKRQLEEAEEEATRANASARKLQRELDDATEANEVLS 1933
Cdd:pfam02463 782 KTEKLKVEEEKEEKLKAQEEELRA----LEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELE 857
|
730
....*....|
gi 148223878 1934 REVSTLKNRL 1943
Cdd:pfam02463 858 RLEEEITKEE 867
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1331-1934 |
4.00e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.95 E-value: 4.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1331 QLQDTQELLqEETRQKLNQSSRIRQLEEEKNNLQEQQEEEEEARKSLEKQILSLQSQLIEAK-KKVDDEVGTIEGLEEVK 1409
Cdd:COG4913 236 DLERAHEAL-EDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAElEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1410 KKLLKDTEGLGQRLEEKI--IAYEKLEktknRLQQELDDLMVDLDHQRQIVSNLEKKQKKFD-QLLAEEKNISARHAEER 1486
Cdd:COG4913 315 EARLDALREELDELEAQIrgNGGDRLE----QLEREIERLERELEERERRRARLEALLAALGlPLPASAEEFAALRAEAA 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1487 DRAEADAREKETKALSLARALDEALEAQDEFERLNKQLRAemedlmsskddvgknvheLEKSKRALDQQVEEMRtqlEEL 1566
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS------------------LERRKSNIPARLLALR---DAL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1567 EDELQGTEDAkLR-----LEVNMQAMKAQ--FERDLQTR------DEQNEEKKRALVKQVR--------ELEAELEDERK 1625
Cdd:COG4913 450 AEALGLDEAE-LPfvgelIEVRPEEERWRgaIERVLGGFaltllvPPEHYAAALRWVNRLHlrgrlvyeRVRTGLPDPER 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1626 QRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIK-----QLRKLQ-AQTKDYQRELEEARASRDDIFAQSKE------N 1693
Cdd:COG4913 529 PRLDPDSLAGKLDFKPHPFRAWLEAELGRRFDYVCvdspeELRRHPrAITRAGQVKGNGTRHEKDDRRRIRSRyvlgfdN 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1694 EKKLKGLEAEILQLQEELAASERSRRHAEQERDEladeisnstsgksalLDEKRRLEARIAhleeeleeeQSNMELLNdr 1773
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDA---------------LQERREALQRLA---------EYSWDEID-- 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1774 FRKTTLQVDTLNSELAAERSSGQKSENARQQLERQNKELKAKLQELEgsvksKFKATIATLESKIAQLEEQLEQ-----E 1848
Cdd:COG4913 663 VASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELD-----ELKGEIGRLEKELEQAEEELDElqdrlE 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1849 AKERVASNKLVRRTEKKLKEVfMQVEDERRHADQYKEQMEKANTRMKQLKRQLEEAEEEATRA-NASARKLQRELDDATE 1927
Cdd:COG4913 738 AAEDLARLELRALLEERFAAA-LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREwPAETADLDADLESLPE 816
|
....*..
gi 148223878 1928 ANEVLSR 1934
Cdd:COG4913 817 YLALLDR 823
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
819-1362 |
4.33e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.18 E-value: 4.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 819 RKAFAKKQQQLIALKVLQRNCAAYLKLRHWQWWRLFTKVKPLLQVTRQEEELVAKDEELLKVKEKQSKVEgelvdmEQKH 898
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE------EAKK 1445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 899 QQLVEEKnilAEQLHAETELFAEAEEMRARLAIKKQemeeilrdleirmeeeeernqvlQNEKKKMQTHVQDLEEQLDEE 978
Cdd:PTZ00121 1446 ADEAKKK---AEEAKKAEEAKKKAEEAKKADEAKKK-----------------------AEEAKKADEAKKKAEEAKKKA 1499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 979 EAAQKLQLEKVTAEaKIKKMEEDILVleDQNSKFLKEKKLLEERIAESTSQlAEEEEKAKNLAKLKNKQEMmisdlEERL 1058
Cdd:PTZ00121 1500 DEAKKAAEAKKKAD-EAKKAEEAKKA--DEAKKAEEAKKADEAKKAEEKKK-ADELKKAEELKKAEEKKKA-----EEAK 1570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1059 KKEEKTRQELEKAKRKLDGETTDFQdQIAELQAQIEELKLQLAKKEEE--LQAALARGDEEVLQKNNTLKLVRELQAQIA 1136
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIE-EVMKLYEEEKKMKAEEAKKAEEakIKAEELKKAEEEKKKVEQLKKKEAEEKKKA 1649
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1137 ElqEDLESEKASRNKAEKQKRDLSEE---LEALKTELEDtlDTTAAQQELRTKRE-QEVAELRKSIEEETRNHEaQIQEM 1212
Cdd:PTZ00121 1650 E--ELKKAEEENKIKAAEEAKKAEEDkkkAEEAKKAEED--EKKAAEALKKEAEEaKKAEELKKKEAEEKKKAE-ELKKA 1724
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1213 RQRQATALEELSEQLEQAKRFKVNLEKNKQslesdnkelatEVKSLQQMKAESEYKRKKLEGQVQE-LHAKVLEGDRLRA 1291
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEEDKKKAEEAKKDEE-----------EKKKIAHLKKEEEKKAEEIRKEKEAvIEEELDEEDEKRR 1793
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148223878 1292 DMVEKSSKlqnELENVSSLLEEAEKKGIKLAKDvaSMESQLQDTQELLQEETRQkLNQSSRIRQLEEEKNN 1362
Cdd:PTZ00121 1794 MEVDKKIK---DIFDNFANIIEGGKEGNLVIND--SKEMEDSAIKEVADSKNMQ-LEEADAFEKHKFNKNN 1858
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
982-1747 |
8.55e-13 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 73.99 E-value: 8.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 982 QKLQLEKVTAEAKIK----KMEEDILVLEDQNsKFLKEKKLLEERIaesTSQLAEEEEKAKNLAKLKNKQEMMISDLEER 1057
Cdd:pfam05483 88 EKIKKWKVSIEAELKqkenKLQENRKIIEAQR-KAIQELQFENEKV---SLKLEEEIQENKDLIKENNATRHLCNLLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1058 LKKEEKTRQELEKAKRKLDGETTDFQDQIAELQAQIEELKLQLAKKEEELQAALARGDEEVLQknntlkLVRELQAQIAE 1137
Cdd:pfam05483 164 CARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQH------LEEEYKKEIND 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1138 LQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELRKSIEEetrnheaqIQEMRQRQA 1217
Cdd:pfam05483 238 KEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELED--------IKMSLQRSM 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1218 TALEELSEQLEQAKRFKVNLEKNKQS-LESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELHAKvleGDRLRAdmvek 1296
Cdd:pfam05483 310 STQKALEEDLQIATKTICQLTEEKEAqMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKN---EDQLKI----- 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1297 sskLQNELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQEEtrqklnqssriRQLEEEKNNLQEQQEEEEEARKS 1376
Cdd:pfam05483 382 ---ITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEK-----------KQFEKIAEELKGKEQELIFLLQA 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1377 LEKQILSLQSQLIEAKKKVDDEVGTIEGLE-EVKKKLLKDTEGLGQRleekiiayEKLEKTKNRLQQELDDLMVDLDHQR 1455
Cdd:pfam05483 448 REKEIHDLEIQLTAIKTSEEHYLKEVEDLKtELEKEKLKNIELTAHC--------DKLLLENKELTQEASDMTLELKKHQ 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1456 QIVSNLEKKQKKfdqLLAEEKNISARHAEERDRAEADAREKETKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSSK 1535
Cdd:pfam05483 520 EDIINCKKQEER---MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKC 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1536 DDVGKNVHELEKSKRALDQQVEEMRTQLEELEDELQGTEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRALVKQVRE 1615
Cdd:pfam05483 597 NNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEE 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1616 LeaeledERKQRAMAVAIKKKLEMDMKdfesqieaankgREDAIKQLRKLQAQTKDYQRELEEARASRDDIFAQSKENEK 1695
Cdd:pfam05483 677 V------EKAKAIADEAVKLQKEIDKR------------CQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQS 738
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 148223878 1696 KLK-GLEAEILQLQEELAASERSRRHAEQERDELADEISNSTsgksALLDEKR 1747
Cdd:pfam05483 739 SAKaALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT----AILKDKK 787
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1379-1924 |
1.10e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.80 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1379 KQILSLQSQLIEAKKKVDdevgTIEGLEEVKKKLLKDTEGLG-QRLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQi 1457
Cdd:COG4913 235 DDLERAHEALEDAREQIE----LLEPIRELAERYAAARERLAeLEYLRAALRLWFAQRRLELLEAELEELRAELARLEA- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1458 vsNLEKKQKKFDQLLAEEKNISARHAE-----------ERDRAEADAREKETKALSLARALD----EALEAQDEFERLNK 1522
Cdd:COG4913 310 --ELERLEARLDALREELDELEAQIRGnggdrleqlerEIERLERELEERERRRARLEALLAalglPLPASAEEFAALRA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1523 QLRAEMEDLMSSKDDVGKNVHELEKSKRALdqqveemRTQLEELEDELQGTEDAKLRLEVNMQAMKAQFERDLQTRDEQ- 1601
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDL-------RRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAEl 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1602 ---------------------------------------------NEEKKRALVkQVRELEAELEDERKQRAMAVAIKKK 1636
Cdd:COG4913 461 pfvgelievrpeeerwrgaiervlggfaltllvppehyaaalrwvNRLHLRGRL-VYERVRTGLPDPERPRLDPDSLAGK 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1637 LEMDMKDFESQIEAANKGREDAIK-----QLRKLQ-AQTKDYQRELEEARASRDDIFAQSKE------NEKKLKGLEAEI 1704
Cdd:COG4913 540 LDFKPHPFRAWLEAELGRRFDYVCvdspeELRRHPrAITRAGQVKGNGTRHEKDDRRRIRSRyvlgfdNRAKLAALEAEL 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1705 LQLQEELAASERSRRHAEQERDELAD---------EISNSTSGKSALLDEKRRLEARIAHleeeleeeqsnMELLNDRFR 1775
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQErrealqrlaEYSWDEIDVASAEREIAELEAELER-----------LDASSDDLA 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1776 KTTLQVDTLNSELAAERSSGQKSENARQQLERQNKELKAKLQELEGSVKSKFKATIATLEskiAQLEEQLEQEAKERVas 1855
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR---ALLEERFAAALGDAV-- 763
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148223878 1856 nklVRRTEKKLKEvfmQVEDERRHADQYKEQMEKAntrMKQLKRQLEEAEEEATRANASARKLQRELDD 1924
Cdd:COG4913 764 ---ERELRENLEE---RIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESLPEYLALLDR 823
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1544-1933 |
1.26e-12 |
|
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: 73.56 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1544 ELEKSKRALD---QQVEEMRTQLEELEDELQgtedaKLRLEvnmqamKAQFERDLQTRDEQNEEKKRALVKQVRELEAEL 1620
Cdd:TIGR02169 171 KKEKALEELEeveENIERLDLIIDEKRQQLE-----RLRRE------REKAERYQALLKEKREYEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1621 EDERKQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIKQLRKLqaqTKDYQRELEEarasrddifaqskenekKLKGL 1700
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL---GEEEQLRVKE-----------------KIGEL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1701 EAEILQLQEELAASERSRRHAEQERDELADEISNSTSGKSALLDEKRRLEARIAHLEEELEEEQSNMELLNDRFRKTTLQ 1780
Cdd:TIGR02169 300 EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1781 VDTLNSELAAERSSGQKSENARQQLERQNKELKAKLQELEGSVkSKFKATIATLESKIAQLEEQLEQEAKErvasnklVR 1860
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL-ADLNAAIAGIEAKINELEEEKEDKALE-------IK 451
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148223878 1861 RTEKKLKEVFMQVEDERRHADQYKEQMEKANTRMKQLKRQLEeaeeeatRANASARKLQRELDDATEANEVLS 1933
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA-------EAEAQARASEERVRGGRAVEEVLK 517
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1055-1885 |
2.04e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 73.06 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1055 EERLKKEEKT---RQELEKAKRKLDGEttdfQDQIAELQAQIEELKLQLAKKEEELQAAlargdeevlqkNNTLKLVRE- 1130
Cdd:COG3096 278 NERRELSERAlelRRELFGARRQLAEE----QYRLVEMARELEELSARESDLEQDYQAA-----------SDHLNLVQTa 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1131 --LQAQIAELQEDLEsekasrnkaekqkrDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELRKSIEEETRNHEAQ 1208
Cdd:COG3096 343 lrQQEKIERYQEDLE--------------ELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1209 IQEMRQ-RQA-TALEELSEQLEQAKRFKVNLEKNKQSLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELHAKVLEG 1286
Cdd:COG3096 409 QTRAIQyQQAvQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEV 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1287 DRLRADMVEKS-----SKLQNELENVSSL---LEEAEKKgiklakdvasmESQLQDTQELLQEETRQKLNQSSRIRQLEE 1358
Cdd:COG3096 489 ERSQAWQTAREllrryRSQQALAQRLQQLraqLAELEQR-----------LRQQQNAERLLEEFCQRIGQQLDAAEELEE 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1359 EKNnlqeqqeeeeearkSLEKQILSLQSQLIEAkkkVDDEVGTIEGLEEVKKKLlkdtEGLGQRLEEKIIAYEKLEKTKN 1438
Cdd:COG3096 558 LLA--------------ELEAQLEELEEQAAEA---VEQRSELRQQLEQLRARI----KELAARAPAWLAAQDALERLRE 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1439 RLQQELDDLmVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARHAEERDRAEADArekETKALSLARAL----------D 1508
Cdd:COG3096 617 QSGEALADS-QEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPGGAE---DPRLLALAERLggvllseiydD 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1509 EALEAQDEFERLNKQLR---------------AEMEDLMS----------SKDDVGKNVHELEK------SKRAL----- 1552
Cdd:COG3096 693 VTLEDAPYFSALYGPARhaivvpdlsavkeqlAGLEDCPEdlyliegdpdSFDDSVFDAEELEDavvvklSDRQWrysrf 772
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1553 -----------DQQVEEMRTQLEELEDELqgtedAKLRLEVN-MQAMKAQFERDLQTR-----DEQNEEKKRALVKQVRE 1615
Cdd:COG3096 773 pevplfgraarEKRLEELRAERDELAEQY-----AKASFDVQkLQRLHQAFSQFVGGHlavafAPDPEAELAALRQRRSE 847
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1616 LEAELEDERKQramavaikkklemdMKDFESQIEAAnkgREdAIKQLRKLQAQT-----KDYQRELEEARASRDDifAQS 1690
Cdd:COG3096 848 LERELAQHRAQ--------------EQQLRQQLDQL---KE-QLQLLNKLLPQAnlladETLADRLEELREELDA--AQE 907
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1691 KENEKKLKGLEAEIL---------------QLQEELAASERSRRHAEQERDELADEISNST----SGKSALLDEKR---- 1747
Cdd:COG3096 908 AQAFIQQHGKALAQLeplvavlqsdpeqfeQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGLLGENSdlne 987
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1748 RLEARIAHleeeleeEQSNMELLNDRFRKTTLQVDTLNSELAAERSSgqkSENARQQLerqnKELKAKLQELEGSVKSkf 1827
Cdd:COG3096 988 KLRARLEQ-------AEEARREAREQLRQAQAQYSQYNQVLASLKSS---RDAKQQTL----QELEQELEELGVQADA-- 1051
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148223878 1828 kATIATLESKIAQLEEQLEQEAKERVASNKLVRRTE-------KKLKEVFMQVEDERRHADQYKE 1885
Cdd:COG3096 1052 -EAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEaemdslqKRLRKAERDYKQEREQVVQAKA 1115
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
31-76 |
2.15e-12 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 63.22 E-value: 2.15e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 148223878 31 TAKKLVWVPSERHGFEAASIKEERGDEVVVELaENGKKAIVNKDDI 76
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
866-1447 |
2.50e-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: 72.69 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 866 QEEELVAKDEELLKVKEKQSKV--EGELVDMEQKHQQLVEEKNILAEQLHAETELFAEAEEMR------ARLAIKKQEME 937
Cdd:TIGR00618 224 LEKELKHLREALQQTQQSHAYLtqKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERInrarkaAPLAAHIKAVT 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 938 EILRDLEIRMEEEEERNQVLQNEKKKMQTHVQDLEEQLDEEEAAQKLQLE--------------------KVTAEAKIKK 997
Cdd:TIGR00618 304 QIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQeihirdahevatsireiscqQHTLTQHIHT 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 998 MEEDILVLEDQNSKFLKEKKLLEERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKKEEKTRQ-------ELEK 1070
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQceklekiHLQE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1071 AKRKLDGETTDFQDQ-----------------IAELQAQIEELKLQLAKKEEELQAA---------LARGDEEVLQKNNT 1124
Cdd:TIGR00618 464 SAQSLKEREQQLQTKeqihlqetrkkavvlarLLELQEEPCPLCGSCIHPNPARQDIdnpgpltrrMQRGEQTYAQLETS 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1125 LKLVR----ELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELRKSIEE 1200
Cdd:TIGR00618 544 EEDVYhqltSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQP 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1201 ETRN-----HEAQIQEMRQRQATALEELSEQL------EQAKRFKVNLEKNKQSLESDNKELATEVKSLQQMKAESEYKR 1269
Cdd:TIGR00618 624 EQDLqdvrlHLQQCSQELALKLTALHALQLTLtqervrEHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQ 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1270 KKLegqvQELHAKVLEGDRLRADMVEKSSKLQNELENVSSLLEEAEKKGIKLAKDV--ASMESQLQDTQELL------QE 1341
Cdd:TIGR00618 704 TLL----RELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVlkARTEAHFNNNEEVTaalqtgAE 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1342 ETRQKLNQSSRIRQLEEEKNNLQEQQEEEEEARKSLEkQILSLQSQLIeakkkVDDEVGTIEGLEEVKKKLLKDTEGLGQ 1421
Cdd:TIGR00618 780 LSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDE-DILNLQCETL-----VQEEEQFLSRLEEKSATLGEITHQLLK 853
|
650 660
....*....|....*....|....*.
gi 148223878 1422 rLEEKIIAYEKLEKTKNRLQQELDDL 1447
Cdd:TIGR00618 854 -YEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
864-1478 |
3.54e-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: 71.59 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 864 TRQEEELVAKDEELLKVKEKQSKVEGELVDMEQKHQQLVEEKNILAEQLHAETELFAEAEEMRARLAIKKQEMEEILRDL 943
Cdd:TIGR04523 64 NKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 944 EIRMEEEEERNQVLQNEKKKMQTHVQDLeeqldeeeaaqklqlekvtaeakikkmeedilvlEDQNSKFLKEKKLLEERI 1023
Cdd:TIGR04523 144 LTEIKKKEKELEKLNNKYNDLKKQKEEL----------------------------------ENELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1024 AESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERlkkeEKTRQELEKAKRKLDGETTDFQDQIAELQAQIEELKLQLAKK 1103
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQKNKSLESQISEL----KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1104 EEELQaalargdEEVLQKNNTLKLVRELQAQIAELQEDLESEKasRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQEL 1183
Cdd:TIGR04523 266 KKQLS-------EKQKELEQNNKKIKELEKQLNQLKSEISDLN--NQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1184 RTKREQEVAELRKSIEEETRNHEAQIQEMRQRQaTALEELSEQLEQAKRFKVNLEKNKQSLESDNKELATEVKSLQQMKA 1263
Cdd:TIGR04523 337 ISQLNEQISQLKKELTNSESENSEKQRELEEKQ-NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1264 ESEYKRKKLEGQVQELHAKVLEGDRLRADMVEKSSKLQNELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQEET 1343
Cdd:TIGR04523 416 KLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1344 RQKLNQSSRIRQLEEEKNNLQEQQEEEEEARKSLEKQILSLQSQL--IEAKKKVDDEVGTIEGLEEVKKKLLKDTEGLGQ 1421
Cdd:TIGR04523 496 KELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKIsdLEDELNKDDFELKKENLEKEIDEKNKEIEELKQ 575
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148223878 1422 RLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK----QKKFDQLLAEEKNI 1478
Cdd:TIGR04523 576 TQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKElekaKKENEKLSSIIKNI 636
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
915-1630 |
7.18e-12 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 71.02 E-value: 7.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 915 ETELFAEAEEMRARLAIKKQEMEEILRDLEIRMEEEEERNQVLQNEKKKmqthvQDLEEQLDEEEAAQKLQLEKVTAEAK 994
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQ-----LLRTLDDQWKEKRDELNGELSAADAA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 995 IKKMEEDILVLEDQNSKFLKEkklleeriaestsqlaeeeekakNLAKLKNKQEMmisdleerlkkEEKTRQELEKAKRK 1074
Cdd:pfam12128 317 VAKDRSELEALEDQHGAFLDA-----------------------DIETAAADQEQ-----------LPSWQSELENLEER 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1075 LDGETTDFQDQIAELQAQIEELKLQLAKKEEELQAALARGDEEVLQKNNTLKLVreLQAQIAELQEDLESEKASRNKAEK 1154
Cdd:pfam12128 363 LKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDD--LQALESELREQLEAGKLEFNEEEY 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1155 QkrdLSEELEALKTEledtLDTTAAQQELRTKREQEVAELRKSIEEETRNHEAQ--IQEMRQRQATALEELSEQLEQAKR 1232
Cdd:pfam12128 441 R---LKSRLGELKLR----LNQATATPELLLQLENFDERIERAREEQEAANAEVerLQSELRQARKRRDQASEALRQASR 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1233 FkvnLEKNKQSLESDNKELATEVKSLQqmkaesEYKRKKLEGQVQELhAKVLEGDRL-RADMVEKSsklqneleNVSSLL 1311
Cdd:pfam12128 514 R---LEERQSALDELELQLFPQAGTLL------HFLRKEAPDWEQSI-GKVISPELLhRTDLDPEV--------WDGSVG 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1312 EEAEKKGIKLAKDVASMESQLQDTQELlqeetRQKLNQSSRIRQLEEEKnnlqeqqeeeeeaRKSLEKQILSLQSQLIEA 1391
Cdd:pfam12128 576 GELNLYGVKLDLKRIDVPEWAASEEEL-----RERLDKAEEALQSAREK-------------QAAAEEQLVQANGELEKA 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1392 KKKVDDEVGTIEGLEEVKKKLLKDTEGLGQRLEEKIIAYEKL-EKTKNRLQQELDDLmvDLDHQ-------RQIVSNLEK 1463
Cdd:pfam12128 638 SREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSaNERLNSLEAQLKQL--DKKHQawleeqkEQKREARTE 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1464 KQKKFDQLLAEEKNISARHAEERDRAEAdAREKETKALSLARALDEALEAQDEfERLNKqLRAEMEDLMSSKDDVGKNVH 1543
Cdd:pfam12128 716 KQAYWQVVEGALDAQLALLKAAIAARRS-GAKAELKALETWYKRDLASLGVDP-DVIAK-LKREIRTLERKIERIAVRRQ 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1544 ELEK-----------SKRALDQQVEEMRTQLEELEDEL-QGTEDAKLRLEVNMQAMKAQfeRDLQTRDEQNEEKKRALVK 1611
Cdd:pfam12128 793 EVLRyfdwyqetwlqRRPRLATQLSNIERAISELQQQLaRLIADTKLRRAKLEMERKAS--EKQQVRLSENLRGLRCEMS 870
|
730
....*....|....*....
gi 148223878 1612 QVRELEAELEDERKQRAMA 1630
Cdd:pfam12128 871 KLATLKEDANSEQAQGSIG 889
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1047-1282 |
8.14e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.41 E-value: 8.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1047 QEMMISDLEERLKKEEKTRQELEKAKRKLDGETTDFQDQIAELQAQIEELKLQLAKKEEELQAALARgdeevlqknntlk 1126
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1127 lVRELQAQIAELQEDLesekasrnkaEKQKRDLSEELEAL-KTELEDTLD-----TTAAQQELRTKREQEVAELRKSIEE 1200
Cdd:COG4942 85 -LAELEKEIAELRAEL----------EAQKEELAELLRALyRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1201 ETRNHEAQIQEMRQRQATALEELSEQLEQAKRFKVNLEKNKQSLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELH 1280
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
..
gi 148223878 1281 AK 1282
Cdd:COG4942 234 AE 235
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
863-1272 |
1.29e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.09 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 863 VTRQEEELVAKDEELLKVKEKQSKVEGELVDMEQKHQQLVEEKNILAEQLHAETEL----FAEAEEMRARLAIKKQEMEE 938
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLtgltPEKLEKELEELEKAKEEIEE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 939 ILRDLEIRMEEeeernqvLQNEKKKMQTHVQDLEEQLDE--------EEAAQKLQLEKVTAEakIKKMEEDILVLEDQNS 1010
Cdd:PRK03918 406 EISKITARIGE-------LKKEIKELKKAIEELKKAKGKcpvcgrelTEEHRKELLEEYTAE--LKRIEKELKEIEEKER 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1011 KFLKEKKLLEERIAEStSQLAEEEEKAKNLAKLKNK-QEMMISDLEERLKKEEKTRQELEKAKRKLDGETTDFQdQIAEL 1089
Cdd:PRK03918 477 KLRKELRELEKVLKKE-SELIKLKELAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEEL 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1090 QAQIEELKLQLAKKEEELQAALARGDEEvlqknnTLKLVRELQAQIAELqEDLESEKASRNKAEKQKRDLSEELEALKTE 1169
Cdd:PRK03918 555 KKKLAELEKKLDELEEELAELLKELEEL------GFESVEELEERLKEL-EPFYNEYLELKDAEKELEREEKELKKLEEE 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1170 LEDTLDTTAAQQELRTKREQEVAELRKSI-EEETRNHEAQIQEMRQRQATALEELSEQLEQAKRFKVNLEKNKQSLEsDN 1248
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKKYsEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE-ER 706
|
410 420
....*....|....*....|....
gi 148223878 1249 KELATEVKSLQQMKAESEYKRKKL 1272
Cdd:PRK03918 707 EKAKKELEKLEKALERVEELREKV 730
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1051-1227 |
2.92e-11 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 65.72 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1051 ISDLEERLKKEEKTRQELEKAKRKLDGETTDFQDQIAELQAQIEELKLQLAKKEEELQAALARGdEEVLQKNNTLKLVRE 1130
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI-KKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1131 LQAqiaeLQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTldttaaqQELRTKREQEVAELRKSIEEETRNHEAQIQ 1210
Cdd:COG1579 91 YEA----LQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELE 159
|
170
....*....|....*..
gi 148223878 1211 EMRQRQATALEELSEQL 1227
Cdd:COG1579 160 ELEAEREELAAKIPPEL 176
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1180-1922 |
3.76e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 68.71 E-value: 3.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1180 QQELRTKREQEVAELRKsieeetRNHEAQIQEMRQRqATALEELSEQLEQAKrfkVNLEKNKQSLESDNKELATEVKSLQ 1259
Cdd:pfam12128 213 PPKSRLNRQQVEHWIRD------IQAIAGIMKIRPE-FTKLQQEFNTLESAE---LRLSHLHFGYKSDETLIASRQEERQ 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1260 QMKAESEYKRKKLEGQVQELHAKvLEGDRLRADmvEKSSKLQNELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELL 1339
Cdd:pfam12128 283 ETSAELNQLLRTLDDQWKEKRDE-LNGELSAAD--AAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENL 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1340 QEETRQklnQSSRIRQLEEEKNnlqeqqeeeeeARKSLEKQilslqsqlieakkkvdDEVGTIEGLEEvkkKLLKDTEGL 1419
Cdd:pfam12128 360 EERLKA---LTGKHQDVTAKYN-----------RRRSKIKE----------------QNNRDIAGIKD---KLAKIREAR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1420 GQRLEEKIIAYEKLEktkNRLQQELDDLMVDL-DHQRQIVSNLEKKQKKFDQLLAEEKNISarHAEERDRAEADAREKET 1498
Cdd:pfam12128 407 DRQLAVAEDDLQALE---SELREQLEAGKLEFnEEEYRLKSRLGELKLRLNQATATPELLL--QLENFDERIERAREEQE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1499 KAL-SLARALDEALEAQDEFERLNKQLRAEmedlmsskddvgknvhelekskralDQQVEEMRTQLEELEDEL---QGTE 1574
Cdd:pfam12128 482 AANaEVERLQSELRQARKRRDQASEALRQA-------------------------SRRLEERQSALDELELQLfpqAGTL 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1575 DAKLRLEVNM--QAMKAQFERDLQTRDEQNEEKKRALVKQVRELEA-ELEDERKQRAMAVAIKKKLEMDMKDFESQIEAA 1651
Cdd:pfam12128 537 LHFLRKEAPDweQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGvKLDLKRIDVPEWAASEEELRERLDKAEEALQSA 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1652 NKGREDAIKQLRKLQAQTKDYQRELEEARASrddiFAQSKENEKKLKG-LEAEILQLQEELAASERSrrhAEQERDELAD 1730
Cdd:pfam12128 617 REKQAAAEEQLVQANGELEKASREETFARTA----LKNARLDLRRLFDeKQSEKDKKNKALAERKDS---ANERLNSLEA 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1731 EISNSTSGKSALLDEKRR--LEARIAhleeeleEEQSNMELLNDRfrktTLQVDTLNSELAAERSSGQKSENArqqLERQ 1808
Cdd:pfam12128 690 QLKQLDKKHQAWLEEQKEqkREARTE-------KQAYWQVVEGAL----DAQLALLKAAIAARRSGAKAELKA---LETW 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1809 NK-ELKAKlqELEGSVKSKFKATIATLESKIAQLEEQLEQEAKERVASNKLVRRTEKKLKEVFMQVEDE-RRHADQYKEQ 1886
Cdd:pfam12128 756 YKrDLASL--GVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAiSELQQQLARL 833
|
730 740 750
....*....|....*....|....*....|....*.
gi 148223878 1887 MEKANTRMKQLKRQLEEAEEEATRANASARKLQREL 1922
Cdd:pfam12128 834 IADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEM 869
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1650-1868 |
1.84e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.17 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1650 AANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDIFAQSKENEKKLKGLEAEILQLQEELAASERSRRHAEQERDELA 1729
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1730 DEISNSTSGKSALLDE----KRRLEARIAHLEEELEEEQSNMELLNDRFRKTTLQVDTLNSELAAERSSGQKSENARQQL 1805
Cdd:COG4942 97 AELEAQKEELAELLRAlyrlGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148223878 1806 ERQNKELKAKLQELEgSVKSKFKATIATLESKIAQLEEQLEQEAKERVASNKLVRRTEKKLKE 1868
Cdd:COG4942 177 EALLAELEEERAALE-ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1163-1627 |
1.99e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.94 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1163 LEALKTELEDTLDTTAAQQELRTKREQEVAELRKSIEEETRNHEAQIQEmrqrqataLEELSEQLEQAKRFKVNLEKNKQ 1242
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEE--------LEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1243 SLE--SDNKELATEVKSLQQMKAESEYKRKKLEGQVQELHAKVLEGDRLRADMVEKSSKLQNELENVSsllEEAEKKGIK 1320
Cdd:COG4717 120 KLEklLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS---LATEEELQD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1321 LAKDVASMESQLQDTQELLQEETRQKLNQSSRIRQLEEEKNNLQEQQEEEEEARKSLekqILSLQSQLIEAKKKVDDEVG 1400
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL---IAAALLALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1401 TIEG--------LEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLL 1472
Cdd:COG4717 274 TIAGvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1473 AEEKNISARHAEERDRAEADAREKETKA------LSLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDDVGKnvHELE 1546
Cdd:COG4717 354 REAEELEEELQLEELEQEIAALLAEAGVedeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELE 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1547 KSKRALDQQVEEMRTQLEELEDELQGTEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRALVKQVRE-LEAELEDERK 1625
Cdd:COG4717 432 EELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALElLEEAREEYRE 511
|
..
gi 148223878 1626 QR 1627
Cdd:COG4717 512 ER 513
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1019-1755 |
2.38e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 66.13 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1019 LEERIAESTSQLAEEEEK----AKNLAKLKNKQEMMISDLE---ERLKKEEKTRQELEKAKRkldgettdFQDQIAELQA 1091
Cdd:COG3096 290 LRRELFGARRQLAEEQYRlvemARELEELSARESDLEQDYQaasDHLNLVQTALRQQEKIER--------YQEDLEELTE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1092 QIEELKLQLAKKEEEL---QAALARGDEEVlqknntlklvRELQAQIAELQEDLEsEKASRNKAEKQKRDLSEELEALKT 1168
Cdd:COG3096 362 RLEEQEEVVEEAAEQLaeaEARLEAAEEEV----------DSLKSQLADYQQALD-VQQTRAIQYQQAVQALEKARALCG 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1169 ELEDTLDTTAAQQELRTKREQEV------AELRKSIEEETRN-HEAQIQEMRQ------------------RQATALEEL 1223
Cdd:COG3096 431 LPDLTPENAEDYLAAFRAKEQQAteevleLEQKLSVADAARRqFEKAYELVCKiageversqawqtarellRRYRSQQAL 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1224 SEQLEQAKRFKVNLEKNKQSLEsDNKELATEvksLQQMKAESEYKRKKLEGQVQELHAKVLEGDRLRADMVEKSSKLQNE 1303
Cdd:COG3096 511 AQRLQQLRAQLAELEQRLRQQQ-NAERLLEE---FCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1304 LENVSSLLEEAEKKG---IKLAKDVASMESQLQDTQELLQEETRQKLNQSSRIRQLEEEKNNLQEqqeeeeeARKSLEKQ 1380
Cdd:COG3096 587 LEQLRARIKELAARApawLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAA-------RKQALESQ 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1381 ILSLQ-------SQLIEAKKKVD--------DEVgTIE-------------------GLEEVKKKL--LKDT-------E 1417
Cdd:COG3096 660 IERLSqpggaedPRLLALAERLGgvllseiyDDV-TLEdapyfsalygparhaivvpDLSAVKEQLagLEDCpedlyliE 738
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1418 GLGQRLEEKIIAYEklektknrlqqELDDLMVDLDHQRQI-VSNLEK--------KQKKFDQLLAEEKNISARHAEER-- 1486
Cdd:COG3096 739 GDPDSFDDSVFDAE-----------ELEDAVVVKLSDRQWrYSRFPEvplfgraaREKRLEELRAERDELAEQYAKASfd 807
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1487 ----DRAEADAREKETKALSLA------RALDEALEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHELekskRALDQQV 1556
Cdd:COG3096 808 vqklQRLHQAFSQFVGGHLAVAfapdpeAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLL----NKLLPQA 883
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1557 -----EEMRTQLEELEDELQGTEDAKLRLEVNMQAMkAQFERDLQT--RDEQNEEKKRALVKQVRELEAELE------DE 1623
Cdd:COG3096 884 nlladETLADRLEELREELDAAQEAQAFIQQHGKAL-AQLEPLVAVlqSDPEQFEQLQADYLQAKEQQRRLKqqifalSE 962
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1624 RKQRAMAVAIKKKLEM-----DMKD-FESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDIFAQSKENEKKL 1697
Cdd:COG3096 963 VVQRRPHFSYEDAVGLlgensDLNEkLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQEL 1042
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 148223878 1698 KGLEaeilqLQEELAASERSRrhaeQERDELADEISNSTSGKSALLDEKRRLEARIAH 1755
Cdd:COG3096 1043 EELG-----VQADAEAEERAR----IRRDELHEELSQNRSRRSQLEKQLTRCEAEMDS 1091
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1013-1278 |
4.33e-10 |
|
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: 64.76 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1013 LKEKKLLEERIAEStsQLAEEEEKAKNLAKLKnkqemmisdlEERLKKEEKTRQELEKAkRKLDGETTDFQDQIAELQAQ 1092
Cdd:pfam17380 355 QEERKRELERIRQE--EIAMEISRMRELERLQ----------MERQQKNERVRQELEAA-RKVKILEEERQRKIQQQKVE 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1093 IEELKlqlAKKEEELQAALARGDEEVLQKNNTLKLVR-ELQAQIAELQEDLESEKASRNKAEKQKRDLSEelealktele 1171
Cdd:pfam17380 422 MEQIR---AEQEEARQREVRRLEEERAREMERVRLEEqERQQQVERLRQQEEERKRKKLELEKEKRDRKR---------- 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1172 dtldttaAQQELRTKREQEVAELRKSIEEETRNHEAQIQEMRQRQ-ATALEELSEQLEQAKRFKVNLEKNKQSLESDNKe 1250
Cdd:pfam17380 489 -------AEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQkAIYEEERRREAEEERRKQQEMEERRRIQEQMRK- 560
|
250 260
....*....|....*....|....*....
gi 148223878 1251 lATEVKS-LQQMKAESEYKRKKLEGQVQE 1278
Cdd:pfam17380 561 -ATEERSrLEAMEREREMMRQIVESEKAR 588
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
865-1447 |
1.12e-09 |
|
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: 63.70 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 865 RQEEELVAKDEEllkVKEKQSKVEGELVDMEQKHQQLVEEKNILAEQ----LHAETELFAEAEEMRARLAIKKQEMEEIL 940
Cdd:pfam12128 287 ELNQLLRTLDDQ---WKEKRDELNGELSAADAAVAKDRSELEALEDQhgafLDADIETAAADQEQLPSWQSELENLEERL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 941 RDLEIRMEEEEERNQVL-QNEKKKMQTHVQDLEEQLDEEEAAQKLQLEkvTAEAKIKKMEEDI-LVLEDQNSKFLKEKKL 1018
Cdd:pfam12128 364 KALTGKHQDVTAKYNRRrSKIKEQNNRDIAGIKDKLAKIREARDRQLA--VAEDDLQALESELrEQLEAGKLEFNEEEYR 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1019 LEERIAESTSQLAE---EEEKAKNLAKLKNKQEMMISDLEERLKKEEKTRQELEKAKRKLDGETTDFQD---QIAELQAQ 1092
Cdd:pfam12128 442 LKSRLGELKLRLNQataTPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQasrRLEERQSA 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1093 IEELKLQLAKKEEELQAALA------------------------------------------RGDEEVLQKNNTLKLVRE 1130
Cdd:pfam12128 522 LDELELQLFPQAGTLLHFLRkeapdweqsigkvispellhrtdldpevwdgsvggelnlygvKLDLKRIDVPEWAASEEE 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1131 LQAQIAELQEDLESEKAS-----------RNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELRKSIE 1199
Cdd:pfam12128 602 LRERLDKAEEALQSAREKqaaaeeqlvqaNGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSAN 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1200 EETRNHEAQIQEMRQRQATALEELSEQL------EQAKRFKVNLEKNKQSLESDNKELATEVKSLQQMKA-ESEYKRkkl 1272
Cdd:pfam12128 682 ERLNSLEAQLKQLDKKHQAWLEEQKEQKrearteKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKAlETWYKR--- 758
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1273 egqvqELHAKVLEGDRLradmveksSKLQNELENVSSLLEEAEKKGiklaKDVASMESQLQDTqeLLQEETRQKLNQSSR 1352
Cdd:pfam12128 759 -----DLASLGVDPDVI--------AKLKREIRTLERKIERIAVRR----QEVLRYFDWYQET--WLQRRPRLATQLSNI 819
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1353 IRQLEEEKNNLQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVkkKLLKDTEGLGQRLEEKIIAYEK 1432
Cdd:pfam12128 820 ERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATL--KEDANSEQAQGSIGERLAQLED 897
|
650
....*....|....*....
gi 148223878 1433 LEKTKNRL----QQELDDL 1447
Cdd:pfam12128 898 LKLKRDYLsesvKKYVEHF 916
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
982-1232 |
2.37e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.63 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 982 QKLQLEKVTAEAKIKKMEEDILVLEDQNSKFLKEKKLLEERI--AESTSQLAEEEEKAKNLAKLKNKqemmISDLEERLK 1059
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSDD----LAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1060 KEEKTRQELEKAKRKLDGETTDFQDQIAELQAQIEELKLQLAKKEEELQAALARGDEEVLQKNNTLKLVRELQAQIAELQ 1139
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERI 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1140 EDLESEKA-SRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTK-REQEVAElrksieeetrnHEAQIQEMRQRQA 1217
Cdd:COG4913 776 DALRARLNrAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRlEEDGLPE-----------YEERFKELLNENS 844
|
250
....*....|....*.
gi 148223878 1218 TA-LEELSEQLEQAKR 1232
Cdd:COG4913 845 IEfVADLLSKLRRAIR 860
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1099-1852 |
2.73e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 62.43 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1099 QLAKKEEELQAALARGDEEVLQKNNTLKLVREL-QAQIAELQE-DLESEKASRNKAE--KQKRDLSEELEALKTELEDTL 1174
Cdd:pfam05483 82 KLYKEAEKIKKWKVSIEAELKQKENKLQENRKIiEAQRKAIQElQFENEKVSLKLEEeiQENKDLIKENNATRHLCNLLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1175 DTTAAQQELRTKREQEvaelrksiEEETRNHEAQIQEMRQRQATALEELSEQLEQAK-----RFKVNLEKNKQSLESDNK 1249
Cdd:pfam05483 162 ETCARSAEKTKKYEYE--------REETRQVYMDLNNNIEKMILAFEELRVQAENARlemhfKLKEDHEKIQHLEEEYKK 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1250 ELATEVKSLQQMKAESEYKRKKLEGQVqelhaKVLEGDRLRADMVEKSSKLQNEleNVSSLLEEAEKKGIKLAKDVASME 1329
Cdd:pfam05483 234 EINDKEKQVSLLLIQITEKENKMKDLT-----FLLEESRDKANQLEEKTKLQDE--NLKELIEKKDHLTKELEDIKMSLQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1330 SQLQdTQELLQEETRQKlnqSSRIRQLEEEKnnlQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVK 1409
Cdd:pfam05483 307 RSMS-TQKALEEDLQIA---TKTICQLTEEK---EAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1410 KKLLKDteglgqrLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARhaeerdra 1489
Cdd:pfam05483 380 KIITME-------LQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFL-------- 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1490 eADAREKETKALSLAraLDEALEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDE 1569
Cdd:pfam05483 445 -LQAREKEIHDLEIQ--LTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQED 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1570 LQGTEDAKLRLEVNMQAMKaqfERDLQTRDEQnEEKKRALVKQVRELEAELEDERKQRAMAVAIKKKLEMDMKDFESQIE 1649
Cdd:pfam05483 522 IINCKKQEERMLKQIENLE---EKEMNLRDEL-ESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCN 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1650 AANKGREDAIKQLRKLQAQTKDYQReleearasrddifaQSKENEKKLKGLEAEILQLQEELAASersRRHAEQERDELA 1729
Cdd:pfam05483 598 NLKKQIENKNKNIEELHQENKALKK--------------KGSAENKQLNAYEIKVNKLELELASA---KQKFEEIIDNYQ 660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1730 DEISNSTSGKSALLDEKRRLEARIahleeeleeeqsnmellnDRFRKTTLQVDTLNSELAAERSSGQKSENAR--QQLER 1807
Cdd:pfam05483 661 KEIEDKKISEEKLLEEVEKAKAIA------------------DEAVKLQKEIDKRCQHKIAEMVALMEKHKHQydKIIEE 722
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 148223878 1808 QNKEL---KAKLQElEGSVKSKFKATIATLESKIAQLEEQLEQEAKER 1852
Cdd:pfam05483 723 RDSELglyKNKEQE-QSSAKAALEIELSNIKAELLSLKKQLEIEKEEK 769
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1040-1519 |
3.30e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1040 LAKLKNKQEMMISDLEERLKKEEKTRQELEKAKRKLDGETTDF---QDQIAELQAQIEELKLQLAKKEEELQAAlargdE 1116
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYaelQEELEELEEELEELEAELEELREELEKL-----E 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1117 EVLQKNNTLKLVRELQAQIAELQEDLESEKAsrnkAEKQKRDLSEELEALKTELEdtldttaaqqELRTKREQEVAELRK 1196
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERLEELEE----RLEELRELEEELEELEAELA----------ELQEELEELLEQLSL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1197 SIEEETRNHEAQIQEMRQRQATALEELSEQLEQAKRFKVNLEKNKQSLESDNKE-----------LATEVKSLQQMKAES 1265
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearllllIAAALLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1266 EYKRKKLEG-------------QVQELHAKVLEGDRLRADMVEKSSKLQNelENVSSLLEEAEKKGIKLAKDVASMESQL 1332
Cdd:COG4717 269 LSLILTIAGvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEE--EELEELLAALGLPPDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1333 QDTQELLQEetRQKLNQSSRIRQLEEEKNNLqeQQEEEEEARKSLEkQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKL 1412
Cdd:COG4717 347 EELQELLRE--AEELEEELQLEELEQEIAAL--LAEAGVEDEEELR-AALEQAEEYQELKEELEELEEQLEELLGELEEL 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1413 LKDTEglGQRLEEKIiayEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKkqkkfDQLLAEeknisARHAEERDRAEAD 1492
Cdd:COG4717 422 LEALD--EEELEEEL---EELEEELEELEEELEELREELAELEAELEQLEE-----DGELAE-----LLQELEELKAELR 486
|
490 500
....*....|....*....|....*..
gi 148223878 1493 AREKETKALSLARALDEalEAQDEFER 1519
Cdd:COG4717 487 ELAEEWAALKLALELLE--EAREEYRE 511
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1373-1925 |
4.47e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1373 ARKSLEKQILSLQsQLIEAKKKVDDEVGTIEGLEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQELDDLMVDLD 1452
Cdd:PRK03918 146 SREKVVRQILGLD-DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1453 HQRQIVSNLEKKQKKFDQLLAEEKNI--SARHAEERDRAEADAREKETKALSLARALDEALEAQDEFERLNKQLRAEMED 1530
Cdd:PRK03918 225 KLEKEVKELEELKEEIEELEKELESLegSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1531 LMSSKDDVGKNVHELEKSKRALDQQV---EEMRTQLEELEDELQGTEDAKLRLEVNMQAmkaqFERDLQTRDEQNEEKKR 1607
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEINGIEERIkelEEKEERLEELKKKLKELEKRLEELEERHEL----YEEAKAKKEELERLKKR 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1608 ALVKQVRELEAELEDERKQramavaiKKKLEMDMKDFESQI---EAANKGREDAIKQLRKLQAQTKDYQRELEEARasRD 1684
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKA-------KEEIEEEISKITARIgelKKEIKELKKAIEELKKAKGKCPVCGRELTEEH--RK 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1685 DIFAqskENEKKLKGLEAEILQLQEELAASERSRRHAEQERDELADEISNSTsgksaLLDEKRRLEARI-AHLEEELEEE 1763
Cdd:PRK03918 452 ELLE---EYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKE-----LAEQLKELEEKLkKYNLEELEKK 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1764 QSNMELLNDRFRKTTLQVDTLNSELaaerSSGQKSENARQQLERQNKELKAKLQELEGSVKSKFKATIATLESKIAQLEE 1843
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKEL----EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEP 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1844 qLEQEAKERVASNKLVRRTEKKLKevfmqvederrhadqykeqmekantrmkQLKRQLEEAEEEATRANASARKLQRELD 1923
Cdd:PRK03918 600 -FYNEYLELKDAEKELEREEKELK----------------------------KLEEELDKAFEELAETEKRLEELRKELE 650
|
..
gi 148223878 1924 DA 1925
Cdd:PRK03918 651 EL 652
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
982-1195 |
4.91e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 61.57 E-value: 4.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 982 QKLQLEKVTAEAKIK--KMEEDILVLEDQNSKFLKEKKLLEERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEErLK 1059
Cdd:COG3206 185 PELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ-SP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1060 KEEKTRQELEKAKRKLDGETTDFQD---QIAELQAQIEELKLQLAKKEEELQAALaRGDEEVLQKNntlklVRELQAQIA 1136
Cdd:COG3206 264 VIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQIAALRAQLQQEAQRILASL-EAELEALQAR-----EASLQAQLA 337
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 148223878 1137 ELQEDLESEkasrNKAEKQKRDLSEELEALKTELEDTLdttAAQQELRTKREQEVAELR 1195
Cdd:COG3206 338 QLEARLAEL----PELEAELRRLEREVEVARELYESLL---QRLEEARLAEALTVGNVR 389
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
873-1297 |
5.29e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.70 E-value: 5.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 873 KDEELLKVKEKQSKVEGELVDMEQKHQQLveeknilaeqlhaetelfAEAEEMRArlAIKKQEMEEILRDLEIRMEEEEE 952
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADEL------------------KKAEELKK--AEEKKKAEEAKKAEEDKNMALRK 1582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 953 RNQVLQNEKKKMQTHVQDLEEQLDEEEAAQKLQLEKVTAEAKIKKMEEDILVLEDQNSKFLKEKKLLEE-RIAESTSQLA 1031
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElKKAEEENKIK 1662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1032 EEEEKAKNLAKLKNKQEMMISDLEERLKKEEKTRQELEKAK----RKLDGETTDFQDQIAElQAQIEELKLQLAKKEEEL 1107
Cdd:PTZ00121 1663 AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKaeelKKKEAEEKKKAEELKK-AEEENKIKAEEAKKEAEE 1741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1108 QaalARGDEEVLQKNNTLKLVRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTeLEDTLDTTAAQQELRTKR 1187
Cdd:PTZ00121 1742 D---KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK-IKDIFDNFANIIEGGKEG 1817
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1188 EQEVAELRKSIEEETR----NHEAQIQEMRQRQATALEELSEQLEQAKRfKVNLEKNKQSLESDNKEL--ATEVKSLQQM 1261
Cdd:PTZ00121 1818 NLVINDSKEMEDSAIKevadSKNMQLEEADAFEKHKFNKNNENGEDGNK-EADFNKEKDLKEDDEEEIeeADEIEKIDKD 1896
|
410 420 430
....*....|....*....|....*....|....*.
gi 148223878 1262 KAESEYKRKKLEGQVQELHAKVLEGDRLRADMVEKS 1297
Cdd:PTZ00121 1897 DIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEET 1932
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
987-1525 |
5.56e-09 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 61.30 E-value: 5.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 987 EKVTAEAKIKKMEEDILVLEDQNSKFLKEKKLLEERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKKEEKT-- 1064
Cdd:pfam05557 28 ARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVis 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1065 --RQELEKAKRKLDGETTDFQDQIAELQAQIEELKLQLAKKE--EELQAALARGDEEVLQKNNTLK-LVREL--QAQIAE 1137
Cdd:pfam05557 108 clKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASeaEQLRQNLEKQQSSLAEAEQRIKeLEFEIqsQEQDSE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1138 LQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTK--REQEVAELRKSIEEETRNHEAQIQE-MRQ 1214
Cdd:pfam05557 188 IVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKleREEKYREEAATLELEKEKLEQELQSwVKL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1215 RQATAL-----EELSEQLEQAKRFKVNLEKNKQSLESDNKELATEVKSLQQMKA-------ESEYKRKKLEGQVQELHAK 1282
Cdd:pfam05557 268 AQDTGLnlrspEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAqylkkieDLNKKLKRHKALVRRLQRR 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1283 VL----EGDRLRADmvekssklqneLENVSSLLEEAEkKGIKLAKDVASMESQLQDTQELLQEetrqklnQSSRIRQLEE 1358
Cdd:pfam05557 348 VLlltkERDGYRAI-----------LESYDKELTMSN-YSPQLLERIEEAEDMTQKMQAHNEE-------MEAQLSVAEE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1359 EKNNLQEQQEeeeearkSLEKQILSLQSQlieakKKVDDEVGTIEGLEEVKKKlLKDTEGLGQRLEEKIIAYEkLEKTKN 1438
Cdd:pfam05557 409 ELGGYKQQAQ-------TLERELQALRQQ-----ESLADPSYSKEEVDSLRRK-LETLELERQRLREQKNELE-MELERR 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1439 RLQQELDDLMVDLDHQRQIVSNLEKKQKK--FDQLLAEEKNISARHAEERDRAEADAREKETkalSLARALDEALEAQDE 1516
Cdd:pfam05557 475 CLQGDYDPKKTKVLHLSMNPAAEAYQQRKnqLEKLQAEIERLKRLLKKLEDDLEQVLRLPET---TSTMNFKEVLDLRKE 551
|
....*....
gi 148223878 1517 FERLNKQLR 1525
Cdd:pfam05557 552 LESAELKNQ 560
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1492-1947 |
6.22e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 6.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1492 DAREKETKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDELQ 1571
Cdd:PRK03918 145 ESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1572 GTEDAKLRLE--VNMQAMKAQFERDLQTRDEQNEEKKRALVKQVRELEAELEDERKQRAMAVAIKKKLEmdmkdfesQIE 1649
Cdd:PRK03918 225 KLEKEVKELEelKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE--------EYI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1650 AANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDIfaqsKENEKKLKGLEAEILQLQEELAASERSRRHAEQERdela 1729
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL----EEKEERLEELKKKLKELEKRLEELEERHELYEEAK---- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1730 deisnstsgksALLDEKRRLEARIAHLEEELEEEQsnMELLNDRFRKTTLQVDTLNSELAAERSSGQKSENARQQLERQN 1809
Cdd:PRK03918 369 -----------AKKEELERLKKRLTGLTPEKLEKE--LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAK 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1810 KELKAKLQEL----EGSVKSKFKATIATLESKIAQLEEQLEQEAKERVASNKLVRRTEK--KLKEVFMQVEDERRHADQY 1883
Cdd:PRK03918 436 GKCPVCGRELteehRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKY 515
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148223878 1884 -KEQMEKANTRMKQLKRQLEEAEEEATRANASARKLQ---RELDDATEANEVLSREVSTLKNRLRRGG 1947
Cdd:PRK03918 516 nLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEelkKKLAELEKKLDELEEELAELLKELEELG 583
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
875-1614 |
6.54e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 875 EELLKVKEKQSKVEGELVDMEQKHQQLVEEKNILAEQLHAetelfAEAEEMRARLAIKKQEMEEILRDLEirmeEEEERN 954
Cdd:COG4913 241 HEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAA-----LRLWFAQRRLELLEAELEELRAELA----RLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 955 QVLQNEKKKMQTHVQDLEEQLDEEEAAQKLQLEK--VTAEAKIKKMEEDILVLEDQ----NSKFLKEKKLLEERIAESTS 1028
Cdd:COG4913 312 ERLEARLDALREELDELEAQIRGNGGDRLEQLEReiERLERELEERERRRARLEALlaalGLPLPASAEEFAALRAEAAA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1029 QLAEEEEKAKNLAKLKNKQEMMISDLEERLKKEEKTRQELEKAKRKLDGETTDFQDQIAE-LQAQIEELK-----LQLAK 1102
Cdd:COG4913 392 LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEaLGLDEAELPfvgelIEVRP 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1103 KEEELQAALAR--GD------------EEVLQKNNTLKLVRELQAQ-IAELQEDLESEKASRNkaekqkrDLSEELEALK 1167
Cdd:COG4913 472 EEERWRGAIERvlGGfaltllvppehyAAALRWVNRLHLRGRLVYErVRTGLPDPERPRLDPD-------SLAGKLDFKP 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1168 TELEDTLDTTAAQQELRTK--REQEVAELRKSIeeeTRN---------HEAQIQEMRQRQ-------ATALEELSEQLEQ 1229
Cdd:COG4913 545 HPFRAWLEAELGRRFDYVCvdSPEELRRHPRAI---TRAgqvkgngtrHEKDDRRRIRSRyvlgfdnRAKLAALEAELAE 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1230 akrfkvnLEKNKQSLESDNKELATEVKSLQqmkaeseykrkklegQVQELHAKVLEGDRLRADMVEksskLQNELENVSS 1309
Cdd:COG4913 622 -------LEEELAEAEERLEALEAELDALQ---------------ERREALQRLAEYSWDEIDVAS----AEREIAELEA 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1310 LLEEAEKKGiklaKDVASMESQLQDTQELLQEETRQKLNQSSRIRQLEEEKNNLQEQQEEEEEARKSLEKQILSLQSQLI 1389
Cdd:COG4913 676 ELERLDASS----DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1390 EAKKkvdDEVGTIEGLEEVKKKLLKDTEGLGQRLEEkiiAYEKLEKTKNRLQQELDDLMVDLD------------HQRQI 1457
Cdd:COG4913 752 EERF---AAALGDAVERELRENLEERIDALRARLNR---AEEELERAMRAFNREWPAETADLDadleslpeylalLDRLE 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1458 VSNLEKKQKKFDQLLAEeknisarhAEERDRAEadareketkalsLARALDEALE-AQDEFERLNKQLRAEmedlmsskd 1536
Cdd:COG4913 826 EDGLPEYEERFKELLNE--------NSIEFVAD------------LLSKLRRAIReIKERIDPLNDSLKRI--------- 876
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148223878 1537 DVGKNVH-ELEKSKRaLDQQVEEMRTQLEELEDELQGTEDAKlrLEVNMQAMKAQFERdLQTRDEQNEEKKRALVKQVR 1614
Cdd:COG4913 877 PFGPGRYlRLEARPR-PDPEVREFRQELRAVTSGASLFDEEL--SEARFAALKRLIER-LRSEEEESDRRWRARVLDVR 951
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1209-1944 |
8.39e-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: 8.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1209 IQEMRQRQATALEELSEQLEQAKRFKVNLEKNKQSLESDNKELATEVKSLQQMKAESEYKRKKLEgQVQELHAKVLEGDr 1288
Cdd:TIGR00606 191 LRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLK-EIEHNLSKIMKLD- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1289 lraDMVEKSSKLQNELENVSSLLEEaekkgiKLAKDVASMESQLQDTQELLQEETRQKLNQSSRIrQLEEEKNNLQEQQE 1368
Cdd:TIGR00606 269 ---NEIKALKSRKKQMEKDNSELEL------KMEKVFQGTDEQLNDLYHNHQRTVREKERELVDC-QRELEKLNKERRLL 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1369 EEEEARKSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQELDDLM 1448
Cdd:TIGR00606 339 NQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1449 VDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARHAEERDRAEADAREKETKALSLARALDEALEAQDEFERLNKQlrAEM 1528
Cdd:TIGR00606 419 SKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKN--SLT 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1529 EDLMSSKDDVGKNVHELEKSKRALDQQVEEM------RTQLEELE----DELQGTEDAKLRLEVNMQAMKAQFERDLQTR 1598
Cdd:TIGR00606 497 ETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhhtttRTQMEMLTkdkmDKDEQIRKIKSRHSDELTSLLGYFPNKKQLE 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1599 D---------EQNEEKKRALVKQVRELEAELEDERKQRAMAVAIKKKLEMDM------KDFESQIEAANKGREDAIKQLR 1663
Cdd:TIGR00606 577 DwlhskskeiNQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEIEKSSKQRA 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1664 KLQAQTKDYQRELEEARASR-------DDIFAQSKENEKKLKGLEAEILQLQEELAASERSRRHAEQERDELADEISNST 1736
Cdd:TIGR00606 657 MLAGATAVYSQFITQLTDENqsccpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQ 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1737 SGKSALLDEKRRLEARIAHLEEELEEEQSNMELlNDRFRKTTLQVDTLNSELAAERSSGQKSENARQQLERQNKELKAKL 1816
Cdd:TIGR00606 737 SIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE-QETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKL 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1817 QELEGSVK----SKFKATIATLESKIAQLEEQLEQEAKERVASNKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANT 1892
Cdd:TIGR00606 816 QGSDLDRTvqqvNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELST 895
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 148223878 1893 RMKQLKRQLEEAEEEATRANASARKLQRE----LDDATEANEVLSREVSTLKNRLR 1944
Cdd:TIGR00606 896 EVQSLIREIKDAKEQDSPLETFLEKDQQEkeelISSKETSNKKAQDKVNDIKEKVK 951
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1645-1868 |
8.68e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.84 E-value: 8.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1645 ESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDIFAQSKENEKKLKGLEAEILQLQEELaasersrrhaEQE 1724
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI----------EER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1725 RDELADEI------SNSTSGKSALLDEK------RRLEAriahleeeleeeqsnMELLNDRFRKTTLQVDTLNSELAAER 1792
Cdd:COG3883 85 REELGERAralyrsGGSVSYLDVLLGSEsfsdflDRLSA---------------LSKIADADADLLEELKADKAELEAKK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148223878 1793 SsgqKSENARQQLERQNKELKAKLQELEgSVKSKFKATIATLESKIAQLEEQLEQEAKERVASNKLVRRTEKKLKE 1868
Cdd:COG3883 150 A---ELEAKLAELEALKAELEAAKAELE-AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1667-1945 |
9.79e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 9.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1667 AQTKDYQRELEEARASRDdifaQSKENEKKLKGLEAEILQLQEELaasERSRRHAEQERDeladeisnstsgksaLLDEK 1746
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELE----EVEENIERLDLIIDEKRQQLERL---RREREKAERYQA---------------LLKEK 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1747 RRLEARI-AHLEEELEEEQSNMELLNDRFRKTTLQVDTLNSELAAErssgqkSENARQQLERQNKELKAKLQELEGSVKS 1825
Cdd:TIGR02169 221 REYEGYElLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR------LEEIEQLLEELNKKIKDLGEEEQLRVKE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1826 K---FKATIATLESKIAQLEEQLEQEAKERVASNKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANTRMKQLKRQLE 1902
Cdd:TIGR02169 295 KigeLEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE 374
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 148223878 1903 EAEEEATRANASARKLQRELDDATEANEVLSREVSTLKNRLRR 1945
Cdd:TIGR02169 375 EVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR 417
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1511-1755 |
1.02e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1511 LEAQDEFERLNkQLRAEMEDLMSSKDDVGKnvheLEKSKRALdQQVEEMRTQLEELEDELQGTEDAKLRLEVnmqAMKAQ 1590
Cdd:COG4913 218 LEEPDTFEAAD-ALVEHFDDLERAHEALED----AREQIELL-EPIRELAERYAAARERLAELEYLRAALRL---WFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1591 FERDLQTRDEQNEEKKRALVKQVRELEAELEDERKQRAMAVAIKKKLEMD-MKDFESQIEAANKGREDAIKQLRKLQAQT 1669
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1670 KDYQRELEEARASRDDIFAQSKENEKKLKGLEAEilqLQEELAASERSRRHAEQERDELADEISNSTSGKSALLDEKRRL 1749
Cdd:COG4913 369 AALGLPLPASAEEFAALRAEAAALLEALEEELEA---LEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
....*.
gi 148223878 1750 EARIAH 1755
Cdd:COG4913 446 RDALAE 451
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1503-1945 |
1.21e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1503 LARALDEALEAQDEFERLnKQLRAEMEDLMSSKDDVGKNVHELEKSKRALDQQ-VEEMRTQLEELEDELQGTEDAKLRLE 1581
Cdd:COG4913 237 LERAHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQRrLELLEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1582 VNMQAMKAQFERDLQTRDEQNEEKKRALVKQVRELEAELeDERKQRAmavaikkklemdmKDFESQIEAANKGREDAIKQ 1661
Cdd:COG4913 316 ARLDALREELDELEAQIRGNGGDRLEQLEREIERLEREL-EERERRR-------------ARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1662 LRKLQAQTKDYQRELEEARASRDDIFAqskENEKKLKGLEAEILQLQEELAASERSR----RHAEQERDELADEISNSTS 1737
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALA---EAEAALRDLRRELRELEAEIASLERRKsnipARLLALRDALAEALGLDEA 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1738 -----------------------------GKSALLDEKR--------------------RLEARIAHLEEELEEEQS--- 1765
Cdd:COG4913 459 elpfvgelievrpeeerwrgaiervlggfALTLLVPPEHyaaalrwvnrlhlrgrlvyeRVRTGLPDPERPRLDPDSlag 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1766 -------------NMELLN----------DRFRKTTLQVdTLNSELAAERSSGQKseNARQQLERQN----------KEL 1812
Cdd:COG4913 539 kldfkphpfrawlEAELGRrfdyvcvdspEELRRHPRAI-TRAGQVKGNGTRHEK--DDRRRIRSRYvlgfdnraklAAL 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1813 KAKLQELEgsvkskfkATIATLESKIAQLEEQLEQEAKERVASNKLVRRTEKKLKevFMQVEDERRHADQYKEQMEKANT 1892
Cdd:COG4913 616 EAELAELE--------EELAEAEERLEALEAELDALQERREALQRLAEYSWDEID--VASAEREIAELEAELERLDASSD 685
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 148223878 1893 RMKQLKRQLeeaeeeatranasaRKLQRELDDATEANEVLSREVSTLKNRLRR 1945
Cdd:COG4913 686 DLAALEEQL--------------EELEAELEELEEELDELKGEIGRLEKELEQ 724
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1239-1923 |
1.26e-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: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1239 KNKQSLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQElHAKVLEGDRlradmvEKSSKLQNELENVSSLLEEaekkG 1318
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQE-NRKIIEAQR------KAIQELQFENEKVSLKLEE----E 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1319 IKLAKDVASMESQLQDTQELLQEETRQKLNQSSRIRQLEEEKNNLQEQQeeeeeaRKSLEKQILSLQSQLIEAKK----- 1393
Cdd:pfam05483 140 IQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDL------NNNIEKMILAFEELRVQAENarlem 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1394 --KVDDEVGTIEGLEEVKKKLLKDTEGlgqrlEEKIIAYEKLEKtknrlQQELDDLMVDLDHQRQIVSNLEKKQKKFDQL 1471
Cdd:pfam05483 214 hfKLKEDHEKIQHLEEEYKKEINDKEK-----QVSLLLIQITEK-----ENKMKDLTFLLEESRDKANQLEEKTKLQDEN 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1472 LAEEKNISARHAEERDraeaDAREKETKALSLARALDEALE-AQDEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKSKR 1550
Cdd:pfam05483 284 LKELIEKKDHLTKELE----DIKMSLQRSMSTQKALEEDLQiATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTC 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1551 ALDQQVEEMRTQLEELEDELQgtedaklrlEVNMQAMKAQFERDLQTRDEQNEEKKRALVKQVRELEAELEDERKQrama 1630
Cdd:pfam05483 360 SLEELLRTEQQRLEKNEDQLK---------IITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQ---- 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1631 vaikkklemdmkdFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDIFAQSKENEKKLKGLEAEILQLQEE 1710
Cdd:pfam05483 427 -------------FEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAH 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1711 LAASERSRRHAEQERDELADEISNSTSGKSALLDEKRRLEARIAHLEEELEEEQSNMELLNDRFRKttlQVDTLNSELAA 1790
Cdd:pfam05483 494 CDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQ---KGDEVKCKLDK 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1791 ERSSGQKSENARQQLERQNKELKAKLQELEGSVKSKFKatiatlesKIAQLEEQLEQEAKERVASNKLVRRTEKKLKEVF 1870
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNK--------NIEELHQENKALKKKGSAENKQLNAYEIKVNKLE 642
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 148223878 1871 MQVEDERRHADQYKEQMEKANTRMKQLKRQLEEAEEEATRANASARKLQRELD 1923
Cdd:pfam05483 643 LELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEID 695
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1054-1535 |
1.42e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1054 LEERLKKEektRQELEKAKRKLDgetTDFQDQIAELQAQIEELKlqlaKKEEELQAALARgdeevlqknntlklVRELQA 1133
Cdd:COG4717 47 LLERLEKE---ADELFKPQGRKP---ELNLKELKELEEELKEAE----EKEEEYAELQEE--------------LEELEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1134 QIAELQEDLESEKASRNKAEKQKR--DLSEELEALKTELEDT---LDTTAAQQELRTKREQEVAELRKSIEEETRNHEAQ 1208
Cdd:COG4717 103 ELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELperLEELEERLEELRELEEELEELEAELAELQEELEEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1209 IQEMRQRQATALEELSEQLEQAKRFKVNLEKNKQSLESDNKELATEVKSLQ-QMKAESEYKRKKLEGQVQELHAKVLEgd 1287
Cdd:COG4717 183 LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEnELEAAALEERLKEARLLLLIAAALLA-- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1288 rLRADMVEKSSKLQNELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELlqeETRQKLNQSSRIRQLEEEKNNLQEQQ 1367
Cdd:COG4717 261 -LLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQAL---PALEELEEEELEELLAALGLPPDLSP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1368 EEEEEARKSLEkQILSLQSQLIEAKKKVDdevgtIEGLEEVKKKLLK-----DTEGLGQRLEEKiIAYEKLEKTKNRLQQ 1442
Cdd:COG4717 337 EELLELLDRIE-ELQELLREAEELEEELQ-----LEELEQEIAALLAeagveDEEELRAALEQA-EEYQELKEELEELEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1443 ELDDLMVDLDHQRQIVsNLEKKQKKFDQLLAEEKNISARHaeERDRAEADAREKETKALSLARALDEALEaqdEFERLNK 1522
Cdd:COG4717 410 QLEELLGELEELLEAL-DEEELEEELEELEEELEELEEEL--EELREELAELEAELEQLEEDGELAELLQ---ELEELKA 483
|
490
....*....|...
gi 148223878 1523 QLRAEMEDLMSSK 1535
Cdd:COG4717 484 ELRELAEEWAALK 496
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1032-1231 |
1.55e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.07 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1032 EEEEKAKNLAKLKNKQEMMISDLEERLKKEEKTRQELEKAKRKLDgettDFQDQIAELQAQIEELKLQLAKKEEELQAAL 1111
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE----ALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1112 AR--------GDEEVL---------------------QKNNTLKLVRELQAQIAELQEDLESEKASRNKAEKQKRDLSEE 1162
Cdd:COG3883 93 RAlyrsggsvSYLDVLlgsesfsdfldrlsalskiadADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148223878 1163 LEALKTELEDTLDTTAAQQELRTKREQEVAELRKSIEEETRNHEAQIQEMRQRQATALEELSEQLEQAK 1231
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
855-1313 |
1.70e-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: 59.74 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 855 TKVKPLLQVTRQEEELVAKDEELLKV-----KEKQSKVEGELVDMEQKHQQLVEEKNILAEQ---LHAETELFAEAEEMR 926
Cdd:pfam05483 356 ATTCSLEELLRTEQQRLEKNEDQLKIitmelQKKSSELEEMTKFKNNKEVELEELKKILAEDeklLDEKKQFEKIAEELK 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 927 AR---LAIKKQEMEEILRDLEIRMEEEEERNQVLQNEKKKMQThvqdleeqldeeeaaqklQLEKvtaeAKIKKMEedil 1003
Cdd:pfam05483 436 GKeqeLIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKT------------------ELEK----EKLKNIE---- 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1004 vLEDQNSKFLKEKKLLEERIAESTSQLAEEEEKAKNLaklKNKQEMMISDLEERLKKEEKTRQELEKAKRKLDGETTDFQ 1083
Cdd:pfam05483 490 -LTAHCDKLLLENKELTQEASDMTLELKKHQEDIINC---KKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVK 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1084 DQIAELQAQIEELKLQLAKKEEELQAALARGDEEVLQKNNTLKLVRELQAQIAELQEDLESEKASRNKAEKQKRDLSEEL 1163
Cdd:pfam05483 566 CKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELEL 645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1164 EALKTELEDTLDTtaaqqelrtkreqevaeLRKSIEEETRNHEAQIQEMRQRQATALEELSEQLEQAKRFKVN------- 1236
Cdd:pfam05483 646 ASAKQKFEEIIDN-----------------YQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKiaemval 708
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148223878 1237 LEKNKQSLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELHAKVLEGDRLRADMVEKSSKLQNELENVSSLLEE 1313
Cdd:pfam05483 709 MEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
862-1177 |
1.70e-08 |
|
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: 59.65 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 862 QVTRQEEELVAKDEELlkvKEKQSKVEGELVDMEQKHQ---QLVEEKNILAEQLHAETELFAEAEEmraRLAIKKQEMEE 938
Cdd:TIGR04523 350 ELTNSESENSEKQREL---EEKQNEIEKLKKENQSYKQeikNLESQINDLESKIQNQEKLNQQKDE---QIKKLQQEKEL 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 939 ILRDLEIRMEEEEERNQVLQNEKKKmQTHVQDLEEQLDEEEAAQKLQLEKVTAEAKIKKMEEDILVLE-----DQNSKFL 1013
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQ-DSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKElkskeKELKKLN 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1014 KEKKLLEERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKK--EEKTRQELEKAKRKLDGETTDFQDQIAELQA 1091
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQKSLKK 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1092 QIEELKLQLAKKEEElqaalargdeevlqKNNTLKLVRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELE 1171
Cdd:TIGR04523 583 KQEEKQELIDQKEKE--------------KKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVK 648
|
....*....
gi 148223878 1172 ---DTLDTT 1177
Cdd:TIGR04523 649 qikETIKEI 657
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1500-1724 |
1.87e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1500 ALSLARALDEALEAQDEFERLNKQL---RAEMEDLMSSKDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDELQGTEDA 1576
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIaelEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1577 KLRLEVNMQAMKAQFERDLQTRDEQNEEKKRALVKQVRELEAELEDERKQRAMAVAIKKKLEmDMKDFESQIEAANKGRE 1656
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAE-ELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148223878 1657 DAIKQLRKLQAQTKDYQRELEEARASRDDIFAQSKENEKK----LKGLEAEILQLQEELAASERSRRHAEQE 1724
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAElaaeLAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1089-1516 |
2.43e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 58.75 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1089 LQAQIEELKLQLAKKEEELQAAlARGDEEVLQKNNTLKL-----VRELQAQIAELQEDLESEKASRNKAEKQKRDLSEEL 1163
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAA-NRQREKEKERYKRDREqwerqRRELESRVAELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1164 EALKTELedtlDTTAAQQELRTKREQEVAELRKSIEEETRNHEAQIQEMRQRQATALEELSEQLEQAKRFKVNLeknkQS 1243
Cdd:pfam07888 111 EELSEEK----DALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKL----QQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1244 LESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELHAKVLEGDRLRADMveksSKLQNELENVSSLLEEAEKKGIKLAK 1323
Cdd:pfam07888 183 TEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEN----EALLEELRSLQERLNASERKVEGLGE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1324 DVASMESQLQDTQELLQEetrqklnqsSRIrQLEEEKNNLQEQQEEEEEARKSLEKQILSLQsQLIEAKKkvddevgtiE 1403
Cdd:pfam07888 259 ELSSMAAQRDRTQAELHQ---------ARL-QAAQLTLQLADASLALREGRARWAQERETLQ-QSAEADK---------D 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1404 GLEEVKKKLLKDTEGLGQRLEEKIIAYEKL--EKTKNRLQqeLDDLMVDLDHQRqivSNLEKKQKKFDQLLAEEKNI--S 1479
Cdd:pfam07888 319 RIEKLSAELQRLEERLQEERMEREKLEVELgrEKDCNRVQ--LSESRRELQELK---ASLRVAQKEKEQLQAEKQELleY 393
|
410 420 430
....*....|....*....|....*....|....*..
gi 148223878 1480 ARHAEERDRAEADAREKETKALSLARALDEALEAQDE 1516
Cdd:pfam07888 394 IRQLEQRLETVADAKWSEAALTSTERPDSPLSDSEDE 430
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1236-1860 |
2.53e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 59.14 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1236 NLEKNKQSLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELHAKVLEGDRLRAdmvekssklqnELENVSSLLEEAE 1315
Cdd:PRK01156 184 NIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKS-----------ALNELSSLEDMKN 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1316 KkgikLAKDVASMESQLQDTQEllqeetrqklnQSSRIRQLEEEKNNLQEQQEEeeeARKSLEKQILSLQSQLIEAKKKV 1395
Cdd:PRK01156 253 R----YESEIKTAESDLSMELE-----------KNNYYKELEERHMKIINDPVY---KNRNYINDYFKYKNDIENKKQIL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1396 DDEVGTIEGLEEVKKKLlkdteglgQRLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEE 1475
Cdd:PRK01156 315 SNIDAEINKYHAIIKKL--------SVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNI 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1476 KNISARHAEERDRAEADAREketkalslaraldealeaqdeferlnkqLRAEMEDLMSSKDDVGKNVHELEKSKRALDQQ 1555
Cdd:PRK01156 387 ERMSAFISEILKIQEIDPDA----------------------------IKKELNEINVKLQDISSKVSSLNQRIRALREN 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1556 VEEMRTQLEELEDE----LQGT---EDAKLRLEVNMQAMKAQFERDLqtRDEQNEEKK-RALVKQVRELEAELEDERKQR 1627
Cdd:PRK01156 439 LDELSRNMEMLNGQsvcpVCGTtlgEEKSNHIINHYNEKKSRLEEKI--REIEIEVKDiDEKIVDLKKRKEYLESEEINK 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1628 AMAVAIK-KKLEMDMKDFE---SQIEAANKGREDAIKQLRKLQAQTKDYQR-ELEEARASRD--DIFAQSKENEKKLKGL 1700
Cdd:PRK01156 517 SINEYNKiESARADLEDIKikiNELKDKHDKYEEIKNRYKSLKLEDLDSKRtSWLNALAVISliDIETNRSRSNEIKKQL 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1701 EAEILQLQEELAASERSRRHAEQERDELADEISNSTSGKSALLDEKRRLEariahleeeleeeqsNMELLNDRFRKTTLQ 1780
Cdd:PRK01156 597 NDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIE---------------KLRGKIDNYKKQIAE 661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1781 VDTLNSELAAERSSGQKSENARQQLERQNKELKAKLQELEGSVKSkFKATIATLESKIAQLEEQLEQEAKERVASNKLVR 1860
Cdd:PRK01156 662 IDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEI-LRTRINELSDRINDINETLESMKKIKKAIGDLKR 740
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1176-1407 |
3.01e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1176 TTAAQQELRTKREQEVAELRKSIEEetrnHEAQIQEMRQRQATALEELSEQLEQAKRfkvnLEKNKQSLESDNKELATEV 1255
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAE----LEKELAALKKEEKALLKQLAALERRIAA----LARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1256 KSLQQMKAESEYKRKKLEGQVQELHAKVLEGDRLRADMVEKSSKLQNELENVSSLLEEAEKKgikLAKDVASMESQLQDT 1335
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA---RREQAEELRADLAEL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148223878 1336 QELLQEETRQKLNQSSRIRQLEEEKNNLQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEE 1407
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1129-1395 |
3.47e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.85 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1129 RELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEdtldttAAQQELRtKREQEVAELRKSIEEetrnHEAQ 1208
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA------ALARRIR-ALEQELAALEAELAE----LEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1209 IQEMRQRQATALEELSEQLEQAKRfkvNLEKNKQSLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELhakvlegdr 1288
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYR---LGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL--------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1289 lrADMVEKSSKLQNELENVSSLLEEAEKKgiklakdVASMESQLQDTQELLQEETRQKLNQSSRIRQLEEEknnlqeqqe 1368
Cdd:COG4942 160 --AELAALRAELEAERAELEALLAELEEE-------RAALEALKAERQKLLARLEKELAELAAELAELQQE--------- 221
|
250 260
....*....|....*....|....*..
gi 148223878 1369 eeeeaRKSLEKQILSLQSQLIEAKKKV 1395
Cdd:COG4942 222 -----AEELEALIARLEAEAAAAAERT 243
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1083-1729 |
3.92e-08 |
|
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: 58.68 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1083 QDQIAELQAQIEELKLQLAKKEEELQAALargdeevlqknNTLKLVrelqaqiaeLQEDLESEKASRNKAEKQKRDLSEE 1162
Cdd:pfam10174 2 QAQLRDLQRENELLRRELDIKESKLGSSM-----------NSIKTF---------WSPELKKERALRKEEAARISVLKEQ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1163 LEALKTELED-TLDTTAAQQELRTKRE------------QEVAELRKSIEEETRNHEAQIQEMRQRQATALEELSEQLEQ 1229
Cdd:pfam10174 62 YRVTQEENQHlQLTIQALQDELRAQRDlnqllqqdfttsPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1230 akrFKVNLEKNKQSL----ESDNKELAT-EVKSLQQMKAESEYKRKK----LEGQVQE----LHAKVLEGDRLRADMVEK 1296
Cdd:pfam10174 142 ---MELRIETQKQTLgardESIKKLLEMlQSKGLPKKSGEEDWERTRriaeAEMQLGHlevlLDQKEKENIHLREELHRR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1297 SSkLQNELENVSSLLEEAEKKGIKlakdVASMESQLQDTQELLQE-ETRQKLNQSSR---IRQLEEEKNNLQEQQEEEEE 1372
Cdd:pfam10174 219 NQ-LQPDPAKTKALQTVIEMKDTK----ISSLERNIRDLEDEVQMlKTNGLLHTEDReeeIKQMEVYKSHSKFMKNKIDQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1373 ARKSLEK---QILSLQSQLIEAKKKVDDEVGTIEGLEE---VKKK----LLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQ 1442
Cdd:pfam10174 294 LKQELSKkesELLALQTKLETLTNQNSDCKQHIEVLKEsltAKEQraaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1443 ELDDLMVDLDHQRQIVSNLEKK----QKKFDQLLAEEKNISARHAEERDRAEADAREKETKALSLArALDEALEAQDE-F 1517
Cdd:pfam10174 374 EKSTLAGEIRDLKDMLDVKERKinvlQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALT-TLEEALSEKERiI 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1518 ERLNKQLRAEMEDLMSSKDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDELQG------TEDAKLR-LEVNMQAMKAQ 1590
Cdd:pfam10174 453 ERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSlassglKKDSKLKsLEIAVEQKKEE 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1591 F---ERDLQTRDEQ--NEEKKRALVKQVRELEAELEDERKQRAMAVA-------IKKKLEMDMKDFESQIEAANKGREDA 1658
Cdd:pfam10174 533 CsklENQLKKAHNAeeAVRTNPEINDRIRLLEQEVARYKEESGKAQAeverllgILREVENEKNDKDKKIAELESLTLRQ 612
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148223878 1659 IKQLRKLQAQTKDYQRELEEARASRDDIFAQSKENEKKlkglEAEILQLQEELAASERSRRHAEQERDELA 1729
Cdd:pfam10174 613 MKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLAD----NSQQLQLEELMGALEKTRQELDATKARLS 679
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1544-1754 |
4.13e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1544 ELEKSKRALDQQVEEMRTQLEELEDELQGTEDAKLRLEVNMQAMKAQfERDLQTRDEQNEEKKRALVKQVRELEAELEDE 1623
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-IRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1624 RKQRAMAVAikkKLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDIFAQSKENEKKLKGLEAE 1703
Cdd:COG4942 103 KEELAELLR---ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 148223878 1704 ILQLQEELAASERSRRHAEQERDELADEISNSTSGKSALLDEKRRLEARIA 1754
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1489-1714 |
4.24e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 4.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1489 AEADAREKETKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKSKRALDQQVEEMRTQLEELED 1568
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1569 ELQGTEDAKLRLEVNMQAMKAQFE----------RDLQTRDEQNEEKKRALVKQVRELEAELEDERKQRAMAVAIKKKLE 1638
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPlalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148223878 1639 MDMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDIfaqskenEKKLKGLEAEILQLQEELAAS 1714
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL-------EALIARLEAEAAAAAERTPAA 246
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
862-1392 |
4.86e-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: 58.19 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 862 QVTRQEEELVAKDEELLKVKEKQSKVEGELVDMEQKHQQLVEEKNILAEQLHAET----ELFAEAEEMRARLAIKKQEME 937
Cdd:pfam05483 269 KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATkticQLTEEKEAQMEELNKAKAAHS 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 938 EILRDLEIRMEEEEernQVLQNEKKKMQTHvQDLEEQLDEEEAAQKLQLEKVTAEAKIKKME-EDILVLEDQNSKFLKEK 1016
Cdd:pfam05483 349 FVVTEFEATTCSLE---ELLRTEQQRLEKN-EDQLKIITMELQKKSSELEEMTKFKNNKEVElEELKKILAEDEKLLDEK 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1017 KLLeERIAEstsqlaEEEEKAKNLAKLKNKQEMMISDLEERLKKEEKTRQELEKAKRKLDGETTDFQDQIAELQAQIEEL 1096
Cdd:pfam05483 425 KQF-EKIAE------ELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKL 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1097 KLQLAKKEEELQAALARGDEEVLQKNNTLKLVRELQAQIAELQedlESEKASRNKAEKQKRDLSEELEALKTELEDTLDT 1176
Cdd:pfam05483 498 LLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDELESVREEFIQKGDEVKCKLDKSEEN 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1177 TAAQQELRTKREQEVAELRK---SIEEETRNHEAQIQEMRQRQATALEELSEQLEQAKRFKVNLEKNKQSLESDNKELAT 1253
Cdd:pfam05483 575 ARSIEYEVLKKEKQMKILENkcnNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEE 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1254 EVKSLQQMKAESEYKRKKLEGQVQELHAKVLEGDRLRADMvekSSKLQNELENVSSLLEEAEKKGIKLakdVASMESQLQ 1333
Cdd:pfam05483 655 IIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEI---DKRCQHKIAEMVALMEKHKHQYDKI---IEERDSELG 728
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 148223878 1334 DTQELLQEETRQKLNQSSRIRQLEEEKNNLQEQQEEEEEARKSLEKQILSLQSQLIEAK 1392
Cdd:pfam05483 729 LYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1066-1331 |
4.98e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.53 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1066 QELEKAKRKLDGETTDFQDQIAELQAQIEELKLQLAKKEEELQAAlargdEEVLQKNNtlKLVRELQAQIAELQEDLese 1145
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-----QAEIDKLQ--AEIAEAEAEIEERREEL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1146 kASRNKAEKQKRDLSEELEALK--TELEDTLDTTAAqqelrtkreqevaelrksieeetrnheaqIQEMRQRQATALEEL 1223
Cdd:COG3883 89 -GERARALYRSGGSVSYLDVLLgsESFSDFLDRLSA-----------------------------LSKIADADADLLEEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1224 SEQLEQAKRFKVNLEKNKQSLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELHAKVLEGDRLRADMVEKSSKLQNE 1303
Cdd:COG3883 139 KADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
250 260
....*....|....*....|....*...
gi 148223878 1304 LENVSSLLEEAEKKGIKLAKDVASMESQ 1331
Cdd:COG3883 219 AAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
865-1717 |
5.94e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.43 E-value: 5.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 865 RQEEELVAKDEELLKVKEKQSKVEGELVDMEQKHQQLVEEkniLAEQLHAETELFAEAEEMRARLAI---------KKQE 935
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARE---LAELNEAESDLEQDYQAASDHLNLvqtalrqqeKIER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 936 MEEILRDLEIR-----MEEEEERNQVLQNEKKKMQThvqdleeqldeeeaaqklQLEKVTAEAKIKKMEEDILVLEDQNS 1010
Cdd:PRK04863 353 YQADLEELEERleeqnEVVEEADEQQEENEARAEAA------------------EEEVDELKSQLADYQQALDVQQTRAI 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1011 KFLKEKKLLEEriAESTSQLAE-EEEKAKN-LAKLKNKQEMMIS---DLEERLKKEEKTRQELEKAK---RKLDGETT-- 1080
Cdd:PRK04863 415 QYQQAVQALER--AKQLCGLPDlTADNAEDwLEEFQAKEQEATEellSLEQKLSVAQAAHSQFEQAYqlvRKIAGEVSrs 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1081 DFQDQIAELQAQIEELKlQLAKKEEELQAALARGDEEVLQKNNTLKLVRELQaQIAELQEDLESEkasrnkaekqkrdLS 1160
Cdd:PRK04863 493 EAWDVARELLRRLREQR-HLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFC-KRLGKNLDDEDE-------------LE 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1161 EELEALKTELEDTLDTTAAQQELRTKREQEVAELRKSIEEetrnHEAQIQEMRQRQAtALEELSEQLEQAkrfkvnlEKN 1240
Cdd:PRK04863 558 QLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQR----LAARAPAWLAAQD-ALARLREQSGEE-------FED 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1241 KQSLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQEL----------------------------------------- 1279
Cdd:PRK04863 626 SQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLsqpggsedprlnalaerfggvllseiyddvsledapyfsal 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1280 -----HAKV-----------------------LEGD------------RLRADMVEKSSKLQ------------------ 1301
Cdd:PRK04863 706 ygparHAIVvpdlsdaaeqlagledcpedlylIEGDpdsfddsvfsveELEKAVVVKIADRQwrysrfpevplfgraare 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1302 NELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQ-----------EETRQKLNQssRIRQLEEEKNNlqeqqeee 1370
Cdd:PRK04863 786 KRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGshlavafeadpEAELRQLNR--RRVELERALAD-------- 855
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1371 eearksLEKQILSLQSQLIEAKKKVDdevgtieGLEEV--KKKLLKDtEGLGQRLEE---KIIAYEKLEKTKNRLQQELD 1445
Cdd:PRK04863 856 ------HESQEQQQRSQLEQAKEGLS-------ALNRLlpRLNLLAD-ETLADRVEEireQLDEAEEAKRFVQQHGNALA 921
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1446 DLmvdldhqRQIVSNLEKKQKKFDQLlaeeknisarhaeERDRAEADAREKETK----ALSLARALDEALEAQDEFERLN 1521
Cdd:PRK04863 922 QL-------EPIVSVLQSDPEQFEQL-------------KQDYQQAQQTQRDAKqqafALTEVVQRRAHFSYEDAAEMLA 981
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1522 KQlrAEMEDLMSSKddvgknvheLEKSKRALDQQVEEMRTQLEELEDELQGTEDAKLRLEVNMQaMKAQFERDLQ----T 1597
Cdd:PRK04863 982 KN--SDLNEKLRQR---------LEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQ-MLQELKQELQdlgvP 1049
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1598 RDEQNEEKKRAlvkQVRELEAELEDERKQRAmavaikkKLEMDMKDFESQIEAANkgredaiKQLRKLQAQTKDYQRELE 1677
Cdd:PRK04863 1050 ADSGAEERARA---RRDELHARLSANRSRRN-------QLEKQLTFCEAEMDNLT-------KKLRKLERDYHEMREQVV 1112
|
970 980 990 1000
....*....|....*....|....*....|....*....|..
gi 148223878 1678 EARASRDDIFAQSKEN--EKKLKGLEAEILQLQEELAASERS 1717
Cdd:PRK04863 1113 NAKAGWCAVLRLVKDNgvERRLHRRELAYLSADELRSMSDKA 1154
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1336-1579 |
6.08e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 6.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1336 QELLQEETRQKLNQ-SSRIRQLEEEKNNLQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLK 1414
Cdd:COG4942 18 QADAAAEAEAELEQlQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1415 DTEGLGQRLEEKIIAYEKLEktknrlQQELDDLMVDLDHQRQIVSNLEkkqkKFDQLLAEEKNISARHAEERDRAEADAR 1494
Cdd:COG4942 98 ELEAQKEELAELLRALYRLG------RQPPLALLLSPEDFLDAVRRLQ----YLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1495 EKETKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDELQGTE 1574
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
....*
gi 148223878 1575 DAKLR 1579
Cdd:COG4942 248 FAALK 252
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1337-1682 |
7.88e-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: 57.44 E-value: 7.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1337 ELLQEETRQKLNQSsRIRQLEEEKnnlqeqqEEEEEARKSLEKQILSLQSQL-IEAKKKVDDEVGTIEGLEEVKKKLLKD 1415
Cdd:pfam17380 286 ERQQQEKFEKMEQE-RLRQEKEEK-------AREVERRRKLEEAEKARQAEMdRQAAIYAEQERMAMERERELERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1416 TEGLGQRLEEKIIAYE-----KLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNIsaRHAEERDRAE 1490
Cdd:pfam17380 358 RKRELERIRQEEIAMEisrmrELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQI--RAEQEEARQR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1491 ADAREKETKALSLARALDEALEAQDEFERLNKQlraemedlmssKDDVGKNVHELEKSKRAlDQQVEEMRTQLEELEdel 1570
Cdd:pfam17380 436 EVRRLEEERAREMERVRLEEQERQQQVERLRQQ-----------EEERKRKKLELEKEKRD-RKRAEEQRRKILEKE--- 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1571 qgtedaklrLEVNMQAMKAQfERDLQTRDEQNEEKKRALVKQVRELEAElEDERKQRAMAVaiKKKLEMDMKdfesqIEA 1650
Cdd:pfam17380 501 ---------LEERKQAMIEE-ERKRKLLEKEMEERQKAIYEEERRREAE-EERRKQQEMEE--RRRIQEQMR-----KAT 562
|
330 340 350
....*....|....*....|....*....|..
gi 148223878 1651 ANKGREDAIKQLRKLQAQTKDYQRELEEARAS 1682
Cdd:pfam17380 563 EERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
982-1349 |
1.06e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 982 QKLQLEKVTAEAKIKKMEEDILVLED--QNSKFLKEKKLLEERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLK 1059
Cdd:COG4717 98 EELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1060 KEEKTRQELEKAKRKldgETTDFQDQIAELQAQIEELKLQLAKKEEELQAALARGDE-----EVLQKNNTLK-------- 1126
Cdd:COG4717 178 ELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQlenelEAAALEERLKearlllli 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1127 --------------------------------------LVRELQAQIAELQEDLESEKASRNKAEKQKRDLSE---ELEA 1165
Cdd:COG4717 255 aaallallglggsllsliltiagvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAAlglPPDL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1166 LKTELEDTLDTTAAQQELRTKREQEVAELRKSIEEETRNheaqiQEMRQRQATALEELSEQLEQAKRFkVNLEKNKQSLE 1245
Cdd:COG4717 335 SPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA-----ALLAEAGVEDEEELRAALEQAEEY-QELKEELEELE 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1246 SDNKELATEVKSLQQMKAESEykrkkLEGQVQELHAKVLEGDRLRADMVEKSSKLQNELEN------VSSLLEEAEKKGI 1319
Cdd:COG4717 409 EQLEELLGELEELLEALDEEE-----LEEELEELEEELEELEEELEELREELAELEAELEQleedgeLAELLQELEELKA 483
|
410 420 430
....*....|....*....|....*....|....*.
gi 148223878 1320 KL---AKDVASM---ESQLQDTQELLQEETRQKLNQ 1349
Cdd:COG4717 484 ELrelAEEWAALklaLELLEEAREEYREERLPPVLE 519
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1379-1630 |
1.14e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1379 KQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQiv 1458
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1459 sNLEKKQKKFDQLLAEeknisarhaeerdrAEADAREKETKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDDV 1538
Cdd:COG4942 98 -ELEAQKEELAELLRA--------------LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1539 GKNVHELEKSKRALDQQVEEMRTQLEELEDELQGTEDAKLRLEVNMQAmkaqferdLQTRDEQNEEKKRALVKQVRELEA 1618
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE--------LAAELAELQQEAEELEALIARLEA 234
|
250
....*....|..
gi 148223878 1619 ELEDERKQRAMA 1630
Cdd:COG4942 235 EAAAAAERTPAA 246
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1307-1898 |
1.18e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 57.06 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1307 VSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQEETRQKLNQSSRIRQLEEEKNNLQEQQEEEEEARKSLEKQILSLQS 1386
Cdd:pfam05557 11 LSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1387 QLIEAKKKVDDevgtiegLEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQK 1466
Cdd:pfam05557 91 KLNEKESQLAD-------AREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1467 kfdqlLAEEKNISARHAEERDRAEADAREketkalsLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHELE 1546
Cdd:pfam05557 164 -----SLAEAEQRIKELEFEIQSQEQDSE-------IVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1547 KSKRALDQQvEEMRTQLEELEDELQGTEdAKLRLEVNMQAMKAQFER---DLQTRDEQNEEKKRALVKQVRELEAELEDE 1623
Cdd:pfam05557 232 DLKRKLERE-EKYREEAATLELEKEKLE-QELQSWVKLAQDTGLNLRspeDLSRRIEQLQQREIVLKEENSSLTSSARQL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1624 RKQRamavaikKKLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARA---SRDDIFAQSKENEKKLKGL 1700
Cdd:pfam05557 310 EKAR-------RELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAileSYDKELTMSNYSPQLLERI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1701 EAEILQLQEELAASERSRRHAEQERDELadeisnsTSGKSALLDEKRRLEARiahleeeleeeqSNMELLNDRfRKTTLQ 1780
Cdd:pfam05557 383 EEAEDMTQKMQAHNEEMEAQLSVAEEEL-------GGYKQQAQTLERELQAL------------RQQESLADP-SYSKEE 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1781 VDTLNSELaaerssgQKSENARQQLERQNKELKAKL--QELEGSVKSKFKATIATLESKIAQLEEQLEQEAKERVASNKL 1858
Cdd:pfam05557 443 VDSLRRKL-------ETLELERQRLREQKNELEMELerRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIER 515
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 148223878 1859 VRRTEKKLKEVFMQV--------EDERRHADQYKEQMEKANTRMKQLK 1898
Cdd:pfam05557 516 LKRLLKKLEDDLEQVlrlpettsTMNFKEVLDLRKELESAELKNQRLK 563
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1132-1336 |
1.68e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.61 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1132 QAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELRKSIEEETRNHEAQIQE 1211
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1212 MRQ--RQATALEEL------SEQLEQAKRFKVNLEKNK---QSLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELH 1280
Cdd:COG3883 95 LYRsgGSVSYLDVLlgsesfSDFLDRLSALSKIADADAdllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 148223878 1281 AKVLEGDRLRADMVEKSSKLQNELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQ 1336
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
864-1223 |
1.75e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 864 TRQEEELVAKDEELLKVKEKQSKVEGELVDMEQKHQQLVEEKNILAEQLHAETELFAEAEEMRARLAIKKQEMEEILRDL 943
Cdd:PRK02224 359 EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 944 EIRMEEeeerNQVLQNEKK--------KMQTHVQDLEEQLDEEeaaQKLQLEKVTAEAKIKKMEEDI-----LV-LEDQN 1009
Cdd:PRK02224 439 RERVEE----AEALLEAGKcpecgqpvEGSPHVETIEEDRERV---EELEAELEDLEEEVEEVEERLeraedLVeAEDRI 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1010 SKFLKEKKLLEERIAESTSQLAEEEEKAKNLAKLKNKQEmmiSDLEERLKKEEKTRQELEKAKRKLD---------GETT 1080
Cdd:PRK02224 512 ERLEERREDLEELIAERRETIEEKRERAEELRERAAELE---AEAEEKREAAAEAEEEAEEAREEVAelnsklaelKERI 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1081 DFQDQIAELQAQIEELKLQLAKKEEELQAALARGDEEvlqkNNTLKLVRELQAQI-AELQED-LESEKASRNKAEKQKRD 1158
Cdd:PRK02224 589 ESLERIRTLLAAIADAEDEIERLREKREALAELNDER----RERLAEKRERKRELeAEFDEArIEEAREDKERAEEYLEQ 664
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148223878 1159 LSEELEALkTELEDTLDTTAAQQELRTKREQEVAELRKSIEE-----ETRNHEA-QIQ--------EMRQRQATALEEL 1223
Cdd:PRK02224 665 VEEKLDEL-REERDDLQAEIGAVENELEELEELRERREALENrvealEALYDEAeELEsmygdlraELRQRNVETLERM 742
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1520-1945 |
2.04e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1520 LNKQLRAEMEDLMSSKDDVGK-NVHELEKSKRALDQQVEEMRtQLEELEDELQGTEDAKLRLEVNMQAMKAQFER-DLQT 1597
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPElNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEKlEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1598 RDEQNEEKKRALVKQVRELEAELEDERKQRAmavaikkklemDMKDFESQIEAANKGREDAIKQLRKLQAQTK-DYQREL 1676
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLE-----------ELRELEEELEELEAELAELQEELEELLEQLSlATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1677 EEARASRDDIFAQSKENEKKLKGLEAEILQLQEELAASERS-RRHAEQERDELADEISNSTSGKSALLDEKRRLEARIAH 1755
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENElEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1756 LEEELEEEQSNMELLNDRFRKTTLQvdtLNSELAAERSSGQKSENARQQLERQNKELKAKLQELEGSVKSKFK--ATIAT 1833
Cdd:COG4717 275 IAGVLFLVLGLLALLFLLLAREKAS---LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDriEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1834 LESKIAQLEEQLEQEAkervasnkLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANTRMKQLKRQL---------EEA 1904
Cdd:COG4717 352 LLREAEELEEELQLEE--------LEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLeellgeleeLLE 423
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 148223878 1905 EEEATRANASARKLQRELDDATEANEVLSREVSTLKNRLRR 1945
Cdd:COG4717 424 ALDEEELEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1087-1363 |
2.31e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 56.07 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1087 AELQAQIEELKLQlakKEEELQAALARGDEEvlqknNTLKLVrelqAQIAELQEDLESEKASRNKAEKQKRDLSEELEAL 1166
Cdd:PRK11281 39 ADVQAQLDALNKQ---KLLEAEDKLVQQDLE-----QTLALL----DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1167 KTELEDTLDTTAAQQELRTkREQEVAELR---KSIEEETRNHEAQI---QEMRQRQATALEELSEQLEQAKRFKVNLEKN 1240
Cdd:PRK11281 107 KDDNDEETRETLSTLSLRQ-LESRLAQTLdqlQNAQNDLAEYNSQLvslQTQPERAQAALYANSQRLQQIRNLLKGGKVG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1241 KQSLESDNK-ELATEVKSLQqmkAESEYKRKKLEG--QVQELhakvleGDRLRADMVEKSSKLQNELENVSSL-----LE 1312
Cdd:PRK11281 186 GKALRPSQRvLLQAEQALLN---AQNDLQRKSLEGntQLQDL------LQKQRDYLTARIQRLEHQLQLLQEAinskrLT 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 148223878 1313 EAEKkgiKLAKDVASMESQLQDTQELLQEETRQKLNQSSRIRQLEEEKNNL 1363
Cdd:PRK11281 257 LSEK---TVQEAQSQDEAARIQANPLVAQELEINLQLSQRLLKATEKLNTL 304
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1075-1232 |
2.42e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1075 LDGETTDFQDQIAELQAQIEELKLQLAKKEEELQAALARGDEEVL--QKNNTLKLVRELQAQIAELQEDLESEKASRNKA 1152
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLseEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1153 EKQKRDLSEELEALKT-----ELEDTLDTTAAQ-QELRTKR----------EQEVAELRKSIEEETRNHEAQIQEMRQRQ 1216
Cdd:COG3206 246 RAQLGSGPDALPELLQspviqQLRAQLAELEAElAELSARYtpnhpdvialRAQIAALRAQLQQEAQRILASLEAELEAL 325
|
170
....*....|....*.
gi 148223878 1217 ATALEELSEQLEQAKR 1232
Cdd:COG3206 326 QAREASLQAQLAQLEA 341
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
861-1232 |
2.84e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 861 LQVTRQEEELVAKDEELLKVKEKQSKVEGELVDMEQKHQQLVEEKNILAEQLHAETELFAEAEEMRARLAIKKQ----EM 936
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqlslAT 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 937 EEILRDLEIRMEEEEERNQVLQNEKKKMQTHVQDLEEQLDE-EEAAQKLQLEKVTAEAKIKKMEEDILVLEDQNSKFLKE 1015
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQlENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1016 KK---------------LLEERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLK-KEEKTRQELEKAKRKLDget 1079
Cdd:COG4717 271 LIltiagvlflvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIE--- 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1080 tDFQDQIAELQAQIEELKLQLAKKEEE--LQAALARGDEEVLQKNNTLKLVRELQAQIAELQEDLESEKASRNKAEKQkr 1157
Cdd:COG4717 348 -ELQELLREAEELEEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA-- 424
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148223878 1158 dlsEELEALKTELEDTLDTTAAQQELRTKREQEVAELRKSIEEETRNHEaqIQEMRQRQATALEELSEQLEQAKR 1232
Cdd:COG4717 425 ---LDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE--LAELLQELEELKAELRELAEEWAA 494
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1708-1944 |
3.79e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1708 QEELAASERSRRHAEQERDELADEISNSTSGKSALLDEKRRLEARIAHLEEELEEEQSNMELLNDRFRKTTLQVDTLNSE 1787
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1788 LAAERSSGQKSENARQQLERQNK-ELKAKLQELEGSVKSKfkATIATLESKIAQLEEQLEQEAKERVASNKLVRRTEKKL 1866
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRRL--QYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1867 KEVFMQVEDERRhadQYKEQMEKANTRMKQLKRQLEEAEEEATRANASARKLQRELDD-----ATEANEVLSREVSTLKN 1941
Cdd:COG4942 177 EALLAELEEERA---ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARleaeaAAAAERTPAAGFAALKG 253
|
...
gi 148223878 1942 RLR 1944
Cdd:COG4942 254 KLP 256
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
982-1180 |
4.14e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 982 QKLQLEKVTAEAKIKKMEEDILVLEDQNSKFLKEKKLLEERIAESTSQLAE----EEEKAKNLAKLKNKQEMMISDLEER 1057
Cdd:COG4942 44 AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAElraeLEAQKEELAELLRALYRLGRQPPLA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1058 LKKEEKTRQELEKAKRKLDGETTDFQDQIAELQAQIEELKLQLAKKEEELQAALARGDEEVLQKNNTLKLVRELQAQIAE 1137
Cdd:COG4942 124 LLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR 203
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 148223878 1138 LQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQ 1180
Cdd:COG4942 204 LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1673-1896 |
4.20e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1673 QRELEEARASRDDIFAQSKENEKKLKGLEAEILQLQEE--LAASERSRRHAEQERDELADEISNSTSGKSALLDEKRRLE 1750
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1751 ARIAHLEEELEEEQSNMELLNDRfrkttLQVDTLNSELAAERSSGQKSENARQQLERQNKELKAKLQELEGSVKSKFKAT 1830
Cdd:COG3206 247 AQLGSGPDALPELLQSPVIQQLR-----AQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAE 321
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148223878 1831 IATLESKIAQLEEQLEQeAKERVASnklVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANTRMKQ 1896
Cdd:COG3206 322 LEALQAREASLQAQLAQ-LEARLAE---LPELEAELRRLEREVEVARELYESLLQRLEEARLAEAL 383
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1032-1899 |
4.75e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 55.44 E-value: 4.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1032 EEEEKAKNLAKLKNKQEMMISDLEERLKKEEKtrqelekAKRKLDGETTDFQDQIAELQAQIEELKLQLAKKE----EEL 1107
Cdd:TIGR01612 826 KEDEIFKIINEMKFMKDDFLNKVDKFINFENN-------CKEKIDSEHEQFAELTNKIKAEISDDKLNDYEKKfndsKSL 898
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1108 QAALARGDEEVLQKNNTLKLVRELqaqIAELQEDLESEKASRNKAEKQKRDLSEELEALKtelEDTLDTTAAQQELRTKR 1187
Cdd:TIGR01612 899 INEINKSIEEEYQNINTLKKVDEY---IKICENTKESIEKFHNKQNILKEILNKNIDTIK---ESNLIEKSYKDKFDNTL 972
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1188 EQEVAELRKSIEEETRN-HEAQIQEMRQRQATALEELS--------EQLEQAKRFKVNLEknkQSLESDNKELAT-EVKS 1257
Cdd:TIGR01612 973 IDKINELDKAFKDASLNdYEAKNNELIKYFNDLKANLGknkenmlyHQFDEKEKATNDIE---QKIEDANKNIPNiEIAI 1049
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1258 LQQMKAESEYKRKKLEGQVQELHAKVLEGDRLRadmVEKSSKLQNELE--NVSSLLEEAEKKGI----KLAKDVASMESQ 1331
Cdd:TIGR01612 1050 HTSIYNIIDEIEKEIGKNIELLNKEILEEAEIN---ITNFNEIKEKLKhyNFDDFGKEENIKYAdeinKIKDDIKNLDQK 1126
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1332 LQDTQELLQEETRQKLNQssrIRQLEEEKNNLQEQQEEEEEAR--KSLEKQILSLQSQLIEAK------KKVDDEVGTIE 1403
Cdd:TIGR01612 1127 IDHHIKALEEIKKKSENY---IDEIKAQINDLEDVADKAISNDdpEEIEKKIENIVTKIDKKKniydeiKKLLNEIAEIE 1203
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1404 ----GLEEVKKKLLKDTEGLGQRLEEKIiaYEKLEKTKNRLQQeLDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNIS 1479
Cdd:TIGR01612 1204 kdktSLEEVKGINLSYGKNLGKLFLEKI--DEEKKKSEHMIKA-MEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFN 1280
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1480 ARHAEER---------DRAEADAREKETKalslaraLDEALEAQDEFERLNKQLRAEMEDLMSSKDDVGK---------N 1541
Cdd:TIGR01612 1281 ISHDDDKdhhiiskkhDENISDIREKSLK-------IIEDFSEESDINDIKKELQKNLLDAQKHNSDINLylneianiyN 1353
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1542 VHELEKSKRALDQqVEEMRTQLEE----LEDELQGTED--AKLRLEVNMQAMKAQFERDLQTRDEQneekkrALVKQVRE 1615
Cdd:TIGR01612 1354 ILKLNKIKKIIDE-VKEYTKEIEEnnknIKDELDKSEKliKKIKDDINLEECKSKIESTLDDKDID------ECIKKIKE 1426
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1616 LEAELEDERKQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIKQlrKLQAQTKDYQRELEEARASRDDIFAQSKENEK 1695
Cdd:TIGR01612 1427 LKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKI--KKDNATNDHDFNINELKEHIDKSKGCKDEADK 1504
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1696 KLKGLEA-EILQLQEELAASERSRRHAEQErdeLADEISNSTSGKSALLDEKRRLEARIAhlEEELEEEQSNMELLNDRF 1774
Cdd:TIGR01612 1505 NAKAIEKnKELFEQYKKDVTELLNKYSALA---IKNKFAKTKKDSEIIIKEIKDAHKKFI--LEAEKSEQKIKEIKKEKF 1579
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1775 RkttlqvdtLNSELAAERSSGQKSENARQQLER-QNKELKakLQELEGSVKSKFKATiATLESKIAQLE-EQLEQEAKER 1852
Cdd:TIGR01612 1580 R--------IEDDAAKNDKSNKAAIDIQLSLENfENKFLK--ISDIKKKINDCLKET-ESIEKKISSFSiDSQDTELKEN 1648
|
890 900 910 920
....*....|....*....|....*....|....*....|....*..
gi 148223878 1853 VASNKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANTRMKQLKR 1899
Cdd:TIGR01612 1649 GDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKK 1695
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1586-1732 |
5.16e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.00 E-value: 5.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1586 AMKAQFER--DLQTRD---EQNEEKKRALVKQVRELEAELEDERKQRAMAVAIKKKLEMDMKDFESQIEAAnkgrEDAIK 1660
Cdd:COG1579 1 AMPEDLRAllDLQELDselDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV----EARIK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148223878 1661 QLRKLQAQTKDY------QRELEEARASRDDIFAQSKENEKKLKGLEAEILQLQEELAASERSRRHAEQERDELADEI 1732
Cdd:COG1579 77 KYEEQLGNVRNNkeyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1264-1725 |
5.58e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1264 ESEYKRKKLEGQVQELHAKVLEGDRLRADMVEksskLQNELENVSSLLEEAEK--KGIKLAKDVASMESQLQDTQELLQE 1341
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEE----LEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1342 ETRQKLNQSSRIRQLEEEKNNLQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLKDTEGLGQ 1421
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1422 RLEEKIIAYEKLEKTK-NRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEeknISARHAEERDRAEADAREKETKA 1500
Cdd:COG4717 231 QLENELEAAALEERLKeARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLG---LLALLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1501 LSLARalDEALEAQdefeRLNKQLRAEMEDLMSSKDDVGKNVHELekskraldQQVEEMRTQLEELEDELQgTEDAKLRL 1580
Cdd:COG4717 308 QALPA--LEELEEE----ELEELLAALGLPPDLSPEELLELLDRI--------EELQELLREAEELEEELQ-LEELEQEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1581 EVNMQAMKAQFERDLQTRDEQNEEkKRALVKQVRELEAELEDERK--QRAMAVAIKKKLEMDMKDFESQIEAANKGREDA 1658
Cdd:COG4717 373 AALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGelEELLEALDEEELEEELEELEEELEELEEELEEL 451
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148223878 1659 IKQLRKLQAQTKDY--QRELEEARASRDDIFAQSKENEKklkglEAEILQLQEELAasERSRRHAEQER 1725
Cdd:COG4717 452 REELAELEAELEQLeeDGELAELLQELEELKAELRELAE-----EWAALKLALELL--EEAREEYREER 513
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1480-1852 |
6.17e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 54.13 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1480 ARHAEERDRaEADAREKETKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKSKRALDQQVEEM 1559
Cdd:pfam07888 49 AQEAANRQR-EKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1560 RTQLEELEDELQGTEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKralvkqvrELEAELEderkqramavaikkklem 1639
Cdd:pfam07888 128 EARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERK--------QLQAKLQ------------------ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1640 dmkdfesQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDIFAQSKENEKKLKGLEAEILQLQEELAASERSrr 1719
Cdd:pfam07888 182 -------QTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERK-- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1720 hAEQERDELADEISNSTSGKSALldEKRRLEAR----------------IAHLEEELEEEQSNMELLNDRFRKTTLQVDT 1783
Cdd:pfam07888 253 -VEGLGEELSSMAAQRDRTQAEL--HQARLQAAqltlqladaslalregRARWAQERETLQQSAEADKDRIEKLSAELQR 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1784 LNSELAAERSSGQKSE---------NARQQLE--RQNKELKAKLQELEGSvKSKFKATIATLESKIAQLEEQLEQEAKER 1852
Cdd:pfam07888 330 LEERLQEERMEREKLEvelgrekdcNRVQLSEsrRELQELKASLRVAQKE-KEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
985-1534 |
6.48e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 55.06 E-value: 6.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 985 QLEKVTAEA-------KIKKMEEDILVLEDQNSKFLKE-KKLLEERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEE 1056
Cdd:TIGR01612 1154 DLEDVADKAisnddpeEIEKKIENIVTKIDKKKNIYDEiKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDE 1233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1057 RLKKEEKTRQELEKAKRKLDGETTDFQDQIAELQAQIEELK----LQLAKKEEELQAALARGDEEVLQ--KNNTLKLVRE 1130
Cdd:TIGR01612 1234 EKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAemetFNISHDDDKDHHIISKKHDENISdiREKSLKIIED 1313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1131 L--QAQIAELQEDLESEKAsrnKAEKQKRDLSEELEALkTELEDTLDTTAAQQELRTKRE--QEVAELRKSIEEETRNHE 1206
Cdd:TIGR01612 1314 FseESDINDIKKELQKNLL---DAQKHNSDINLYLNEI-ANIYNILKLNKIKKIIDEVKEytKEIEENNKNIKDELDKSE 1389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1207 AQIQEMRQRqaTALEELSEQLEQAKRFKVNLEKNKQSLESDNKELATEVKSLQQMKAESEYKR------KKLE-GQVQEL 1279
Cdd:TIGR01612 1390 KLIKKIKDD--INLEECKSKIESTLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNEnvlllfKNIEmADNKSQ 1467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1280 HAKVLEGDRLRADMVEKSSKLQNELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQE----ETRQKLNQSSR--- 1352
Cdd:TIGR01612 1468 HILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKysalAIKNKFAKTKKdse 1547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1353 --IRQLEEEKNNLQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLK-------------DTE 1417
Cdd:TIGR01612 1548 iiIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLKisdikkkindclkETE 1627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1418 GLGQRLEEKIIAYEKLEKTKNRLQ-QELDDLMVDLDHQRQivsNLEKKQKKFDQLLAEEKNIsarhaeerdRAEADAREK 1496
Cdd:TIGR01612 1628 SIEKKISSFSIDSQDTELKENGDNlNSLQEFLESLKDQKK---NIEDKKKELDELDSEIEKI---------EIDVDQHKK 1695
|
570 580 590
....*....|....*....|....*....|....*...
gi 148223878 1497 ETKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSS 1534
Cdd:TIGR01612 1696 NYEIGIIEKIKEIAIANKEEIESIKELIEPTIENLISS 1733
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
957-1552 |
6.52e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.52 E-value: 6.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 957 LQNEKKKMQTHVQDLEEQLDEEEAAQKLQL---EKVTAEAKIKKMEEDILVLEDQN-SKFLKEKKLLEERIAESTSQLAE 1032
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLkeiERLSIEYNNAMDDYNNLKSALNElSSLEDMKNRYESEIKTAESDLSM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1033 EEEKAKNlaklknkqemmISDLEERLKKEEKTRQeleKAKRKLDGETTDFQDQIAELQAQIEELKLQLAKKEEELQAAla 1112
Cdd:PRK01156 268 ELEKNNY-----------YKELEERHMKIINDPV---YKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKL-- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1113 rgdeevlqknntlklvrelqaqiaelqEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEva 1192
Cdd:PRK01156 332 ---------------------------SVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEY-- 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1193 elrksiEEETRNHEAQIQEMRQRQATALEELSEQLEQAKRfkvnlekNKQSLESDNKELATEVKSLQQMKAESEYKRKKL 1272
Cdd:PRK01156 383 ------SKNIERMSAFISEILKIQEIDPDAIKKELNEINV-------KLQDISSKVSSLNQRIRALRENLDELSRNMEML 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1273 EGQ----VQELHAKVLEGDRLRADMVEKSSKLQ---NELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQEETRQ 1345
Cdd:PRK01156 450 NGQsvcpVCGTTLGEEKSNHIINHYNEKKSRLEekiREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARA 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1346 klnqssrirQLEEEKNNLQEQQEEEEEArKSLEKQILSLQSQLIEAKK---------KVDDEVGTIEGLEEVKKKLLKDT 1416
Cdd:PRK01156 530 ---------DLEDIKIKINELKDKHDKY-EEIKNRYKSLKLEDLDSKRtswlnalavISLIDIETNRSRSNEIKKQLNDL 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1417 EglgQRLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQIVSNL----EKKQKKFDQLlaeEKNISARHAEERDRAEAD 1492
Cdd:PRK01156 600 E---SRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENkiliEKLRGKIDNY---KKQIAEIDSIIPDLKEIT 673
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148223878 1493 AR--EKETKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKSKRAL 1552
Cdd:PRK01156 674 SRinDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAI 735
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1375-1945 |
7.24e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.46 E-value: 7.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1375 KSLEKQILSLQSQLIEAKkkvDDEVGTIEGLEEVKKKLlkdteglgQRLEEKIIAYEKLEKTK-NRLQQELDDLMVDLDH 1453
Cdd:pfam12128 251 NTLESAELRLSHLHFGYK---SDETLIASRQEERQETS--------AELNQLLRTLDDQWKEKrDELNGELSAADAAVAK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1454 QRQIVSNLEKKQKKFDQLLAEEKnisARHAEERD--RAEADAREKETKALslaraLDEALEAQDEFERLnKQLRAEmedl 1531
Cdd:pfam12128 320 DRSELEALEDQHGAFLDADIETA---AADQEQLPswQSELENLEERLKAL-----TGKHQDVTAKYNRR-RSKIKE---- 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1532 mSSKDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDELQGTEDAKLRlevnmqamkaqferdlqtrdEQNEEKKRalvk 1611
Cdd:pfam12128 387 -QNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKL--------------------EFNEEEYR---- 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1612 qvreLEAELEdERKQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIKQLRKLQaqtkdyqRELEEARASRDDIFAQSK 1691
Cdd:pfam12128 442 ----LKSRLG-ELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQ-------SELRQARKRRDQASEALR 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1692 ENEKKLKGLEAEILQLQEELAASERS-----RRHAEQERDELADEISNSTSGKSAL-------------------LDEKR 1747
Cdd:pfam12128 510 QASRRLEERQSALDELELQLFPQAGTllhflRKEAPDWEQSIGKVISPELLHRTDLdpevwdgsvggelnlygvkLDLKR 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1748 -----------RLEARIAHLEEELEEEQSNMELLNDRFRKTTLQVDTLNSELAAERSSGQKSENARQQLERQNKELKAKL 1816
Cdd:pfam12128 590 idvpewaaseeELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKK 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1817 QELEGSVKSKFKATIATLESKIAQLEEQLeQEAKERVASNKLVRRTEK--KLKEVfmqVEDERRHADQYKEQMEKANTrm 1894
Cdd:pfam12128 670 NKALAERKDSANERLNSLEAQLKQLDKKH-QAWLEEQKEQKREARTEKqaYWQVV---EGALDAQLALLKAAIAARRS-- 743
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 148223878 1895 kQLKRQLEEAEEEATRANASarklqRELDDATEANevLSREVSTLKNRLRR 1945
Cdd:pfam12128 744 -GAKAELKALETWYKRDLAS-----LGVDPDVIAK--LKREIRTLERKIER 786
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1435-1655 |
7.30e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1435 KTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAE-EKNISARhAEERDRAEADAREKETKALSLARALDEALEA 1513
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAlERRIAAL-ARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1514 QDEF-ERLNKQLRA--------EMEDLMSSKD--DVGKNVHELEKSKRALDQQVEEMRTQLEEL---EDELQGTEDAKLR 1579
Cdd:COG4942 99 LEAQkEELAELLRAlyrlgrqpPLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELaalRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148223878 1580 LEVNMQAMKAQFERDLQTRDEQNEEKKRALVKQVRELEAELEDERKQRAMAVAIKKKLEMDMKDFESQIEAANKGR 1655
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1415-1674 |
7.77e-07 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 54.26 E-value: 7.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1415 DTEGLGQRLEEKIIAYEKLEKTKNRLQQELDDLMVDLD--HQRQIVS--NLEKKQKKFDQLLAEEKNISARHAEERDRAE 1490
Cdd:pfam05667 227 NSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTeaTSGASRSaqDLAELLSSFSGSSTTDTGLTKGSRFTHTEKL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1491 ADAREKETKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDEL 1570
Cdd:pfam05667 307 QFTNEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQY 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1571 Q---GTEDAKLRLEVNMQAMKAQFE---RDLQTRDEQNEEKKRALVKQVRELEaELEDERKQRAmavaiKKKLEmDMKDF 1644
Cdd:pfam05667 387 KvkkKTLDLLPDAEENIAKLQALVDasaQRLVELAGQWEKHRVPLIEEYRALK-EAKSNKEDES-----QRKLE-EIKEL 459
|
250 260 270
....*....|....*....|....*....|....
gi 148223878 1645 ESQIEAAN---KGREDAIKQLRK-LQAQTKDYQR 1674
Cdd:pfam05667 460 REKIKEVAeeaKQKEELYKQLVAeYERLPKDVSR 493
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1423-1665 |
8.35e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 53.86 E-value: 8.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1423 LEEKIIA-YEKLEKTKNR-LQQELDDLMVDLDH-QRQIVS--------------NLEKKQKKFDQLLAEEKNISARHAEE 1485
Cdd:PHA02562 160 LDISVLSeMDKLNKDKIReLNQQIQTLDMKIDHiQQQIKTynknieeqrkkngeNIARKQNKYDELVEEAKTIKAEIEEL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1486 RDRAEADAREKETKALSLARALDEALEAQDEFERLNKQLRaemedlMSSKDDV----GKNVHELEKSKRALDQQVEEMRT 1561
Cdd:PHA02562 240 TDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIK------MYEKGGVcptcTQQISEGPDRITKIKDKLKELQH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1562 QLEELEDELQgtEDAKLRLEVNMQAMKAqfeRDLQTRDEQNEEKKRALVKQVRELEAELEderkqramavaikkKLEMDM 1641
Cdd:PHA02562 314 SLEKLDTAID--ELEEIMDEFNEQSKKL---LELKNKISTNKQSLITLVDKAKKVKAAIE--------------ELQAEF 374
|
250 260
....*....|....*....|....
gi 148223878 1642 KDFESQIEAANKGREDAIKQLRKL 1665
Cdd:PHA02562 375 VDNAEELAKLQDELDKIVKTKSEL 398
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
788-1271 |
1.07e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.20 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 788 AGVLAHLEEERDLKITDIIVLFQAVC---RGYLARKAFAKKQQQLIALKVLQRNCAAYLKLRHWQwwrLFTKVKPLLQVT 864
Cdd:TIGR00618 410 ATIDTRTSAFRDLQGQLAHAKKQQELqqrYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQ---LQTKEQIHLQET 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 865 RQEEELVAKDEELlkvKEKQSKVEGELVDMEQKHQQLVEE----------KNILAEQLHAETELFAEAEEMRARLAIKKQ 934
Cdd:TIGR00618 487 RKKAVVLARLLEL---QEEPCPLCGSCIHPNPARQDIDNPgpltrrmqrgEQTYAQLETSEEDVYHQLTSERKQRASLKE 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 935 EMEEILRDLEIRMEEEEERNQV---LQNEKKKMQTHVQDLEEQLDEEEAAQKLQLEKVTAEAKIKKmeediLVLEDQNsk 1011
Cdd:TIGR00618 564 QMQEIQQSFSILTQCDNRSKEDipnLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQD-----VRLHLQQ-- 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1012 FLKEKKLLEERIAESTSQLAEEEEKAKNLAkLKNKQEMMISDLEERLKKEEKTRQELEKAKRKLDgettdfqdQIAELQA 1091
Cdd:TIGR00618 637 CSQELALKLTALHALQLTLTQERVREHALS-IRVLPKELLASRQLALQKMQSEKEQLTYWKEMLA--------QCQTLLR 707
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1092 QIEELKLQLAKKEEELQAALARGDEEVLQKNNTL-KLVRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTEL 1170
Cdd:TIGR00618 708 ELETHIEEYDREFNEIENASSSLGSDLAAREDALnQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEI 787
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1171 EDTLDTTAAQQELRTKREQEVAELRKSIEEETRNHEAQIQEMRQRQATALEELSEQLEQAKRFKVNLEKNKQSLEsdnkE 1250
Cdd:TIGR00618 788 QFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA----Q 863
|
490 500
....*....|....*....|.
gi 148223878 1251 LATEVKSLQQMKAESEYKRKK 1271
Cdd:TIGR00618 864 LTQEQAKIIQLSDKLNGINQI 884
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1216-1438 |
1.12e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1216 QATALEELSEQLEQAKRFKVNLEKNKQSLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELHAKVlegDRLRADMVE 1295
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL---AELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1296 KSSKLQNELENVSSLLEEAEKKGI--------------KLAKDVASMESQLQDTQELLQEETRQKLNQSSRIRQLEEEKN 1361
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148223878 1362 NLQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLlkdtEGLGQRLEEKIIAYEKLEKTKN 1438
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL----EALIARLEAEAAAAAERTPAAG 247
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1461-1927 |
1.20e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1461 LEKKQKKFDQLLAEEKNISARHAEERDRAEADAREKETKALSLARALDEALEAQDEFERLnKQLRAEMEDLMSSKDDVgK 1540
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL-EAELEELREELEKLEKL-L 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1541 NVHELEKSKRALDQQVEEMRTQLEELED---ELQGTEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRALVKQVRELE 1617
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEErleELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1618 AELEDERKQRAMAVAIKKKLEMDMKDFESQIEAANKGRE-----------DAIKQLRKLQAQTKDYQRELEEARASRDDI 1686
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaAALLALLGLGGSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1687 FAQSKENEKKLKgleAEILQLQEELAASERSRRHAEQERDELADEISNSTSGKSALLDEKRRLEARIAHLEEELEEEQSN 1766
Cdd:COG4717 286 LALLFLLLAREK---ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1767 MELLNDRFRKTTLQVDTLNSELAAERSSGQKSEnARQQLERQNKELKAKLQELEGSVKSKFKA-TIATLESKIAQLEEQL 1845
Cdd:COG4717 363 LQLEELEQEIAALLAEAGVEDEEELRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEAlDEEELEEELEELEEEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1846 EQEAKERVASNKLVRRTEKKLKevfmQVEDERRHADQYKEQmekantrmKQLKRQLEEAEEEATRANASARKLQRELDDA 1925
Cdd:COG4717 442 EELEEELEELREELAELEAELE----QLEEDGELAELLQEL--------EELKAELRELAEEWAALKLALELLEEAREEY 509
|
..
gi 148223878 1926 TE 1927
Cdd:COG4717 510 RE 511
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1025-1943 |
1.31e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.81 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1025 ESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKKEEKTRQELEKAKRKLD--GETTDFQDQIAELQAQIEELKLQLAK 1102
Cdd:PRK04863 287 EALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNlvQTALRQQEKIERYQADLEELEERLEE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1103 KEEELQAALARGDEEVLQKNNTLKLVRELQAQIAELQEDLEsEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQE 1182
Cdd:PRK04863 367 QNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALD-VQQTRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1183 LRTKREQEVAELRKSIEEETRNHEAQIQEMRQ-------------------------RQATALEELSEQLEQAKRFKVNL 1237
Cdd:PRK04863 446 EFQAKEQEATEELLSLEQKLSVAQAAHSQFEQayqlvrkiagevsrseawdvarellRRLREQRHLAEQLQQLRMRLSEL 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1238 EKNKQSLESDNKELATEVKSLQQMKAESEykrkKLEGQVQELHAKVLEGDRLRADMVEKSSKLQNELENVSSLLEEAEKK 1317
Cdd:PRK04863 526 EQRLRQQQRAERLLAEFCKRLGKNLDDED----ELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAAR 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1318 G---IKLAKDVASMESQLQDTQELLQEETRQKLNQSSRIRQLEEEKNNLQEqqeeeeeARKSLEKQILSLQ-------SQ 1387
Cdd:PRK04863 602 ApawLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAA-------RKQALDEEIERLSqpggsedPR 674
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1388 LIEAKKKVD-------------DEVGTIEG-------------LEEVKKKLLKD---------TEGLGQRLEEKIIAYEK 1432
Cdd:PRK04863 675 LNALAERFGgvllseiyddvslEDAPYFSAlygparhaivvpdLSDAAEQLAGLedcpedlylIEGDPDSFDDSVFSVEE 754
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1433 LEKtknrlqqeldDLMVDLDhQRQI-VSNL--------EKKQKKFDQLLAEEKNISARHAEERDRAEADAREKETKALSL 1503
Cdd:PRK04863 755 LEK----------AVVVKIA-DRQWrYSRFpevplfgrAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFI 823
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1504 ARALDEALEAQDEferlnkqlrAEMEDLMSSKDDVGKNVHELEKSKRALDQQVEEMRTQL-------------------- 1563
Cdd:PRK04863 824 GSHLAVAFEADPE---------AELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLsalnrllprlnlladetlad 894
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1564 --EELEDELQGTEDAKLRLEVNMQAMkAQFERDLQTRDEqNEEKKRALVKQVRELEAELEDErKQRAMAVAikkklemdm 1641
Cdd:PRK04863 895 rvEEIREQLDEAEEAKRFVQQHGNAL-AQLEPIVSVLQS-DPEQFEQLKQDYQQAQQTQRDA-KQQAFALT--------- 962
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1642 kdfESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDdifaQSKEnekKLKGLEAEILQLQEELAASERSRRHA 1721
Cdd:PRK04863 963 ---EVVQRRAHFSYEDAAEMLAKNSDLNEKLRQRLEQAEQERT----RARE---QLRQAQAQLAQYNQVLASLKSSYDAK 1032
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1722 EQERDELADEISNSTSGKSALLDEKRRLeariahleeeleeeqsnmellndrfrkttlQVDTLNSELAAERSsgqksenA 1801
Cdd:PRK04863 1033 RQMLQELKQELQDLGVPADSGAEERARA------------------------------RRDELHARLSANRS-------R 1075
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1802 RQQLERQNKELKAKLQELEGSVKSkfkatiatLESKIAQLEEQLEQEAKERVASNKLVRR--TEKKLkevfMQVEDERRH 1879
Cdd:PRK04863 1076 RNQLEKQLTFCEAEMDNLTKKLRK--------LERDYHEMREQVVNAKAGWCAVLRLVKDngVERRL----HRRELAYLS 1143
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1880 ADQYKEQMEKANTRMKQ------LKRQLEEAEEEATRANA------SARKLQRE--------LDDATEANEVLSREVSTL 1939
Cdd:PRK04863 1144 ADELRSMSDKALGALRLavadneHLRDVLRLSEDPKRPERkvqfyiAVYQHLRErirqdiirTDDPVEAIEQMEIELSRL 1223
|
....
gi 148223878 1940 KNRL 1943
Cdd:PRK04863 1224 TEEL 1227
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1421-1945 |
1.37e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.75 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1421 QRLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQL---LAEEKNISARHAEERDRAEADAREKE 1497
Cdd:PRK01156 152 KKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIkkqIADDEKSHSITLKEIERLSIEYNNAM 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1498 TKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKSKR-----------------ALDQQVEEMR 1560
Cdd:PRK01156 232 DDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKiindpvyknrnyindyfKYKNDIENKK 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1561 TQLEELEDELQGTEDAKLRLEVnMQAMKAQFERDLQTRDEQN---------EEKKRALVKQVRELEAELEDERKQR---- 1627
Cdd:PRK01156 312 QILSNIDAEINKYHAIIKKLSV-LQKDYNDYIKKKSRYDDLNnqilelegyEMDYNSYLKSIESLKKKIEEYSKNIerms 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1628 AMAVAIKKKLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDIFAQS----------------- 1690
Cdd:PRK01156 391 AFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgttlgeeksnhi 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1691 -KENEKKLKGLEAEILQLQEELAASERSRRHAEQERDELADEISNSTSGKSALLDEKRRLEARIAHLEEELEEEQSNMEL 1769
Cdd:PRK01156 471 iNHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1770 LNDRFRKTTLQ-VDTLNSE---LAAERSSgQKSENARQQLERQNKELK---AKLQELEGS---VKSKFKATIATLESKIA 1839
Cdd:PRK01156 551 IKNRYKSLKLEdLDSKRTSwlnALAVISL-IDIETNRSRSNEIKKQLNdleSRLQEIEIGfpdDKSYIDKSIREIENEAN 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1840 QLEEQLeQEAKERVASNKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANTRMKQLKRQLEeaeeeatRANASARKLQ 1919
Cdd:PRK01156 630 NLNNKY-NEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALD-------DAKANRARLE 701
|
570 580
....*....|....*....|....*.
gi 148223878 1920 RELDDATEANEVLSREVSTLKNRLRR 1945
Cdd:PRK01156 702 STIEILRTRINELSDRINDINETLES 727
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1407-1945 |
1.44e-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: 53.51 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1407 EVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQELDDLMVDL-DHQRQIVSNLEKKQKKFDQLLAEEKNISARhaee 1485
Cdd:TIGR00606 206 QMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLkNRLKEIEHNLSKIMKLDNEIKALKSRKKQM---- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1486 rdraEADAREKETKALSLARALDEALEAQDEFERlnKQLRAEMEDLMSSKDDVGKNvhelEKSKRALDQQVEEMRTQLEE 1565
Cdd:TIGR00606 282 ----EKDNSELELKMEKVFQGTDEQLNDLYHNHQ--RTVREKERELVDCQRELEKL----NKERRLLNQEKTELLVEQGR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1566 LEDELQGTEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRALVKQVREleaELEDERKQRAMAVAIKKKLEMDMKDFE 1645
Cdd:TIGR00606 352 LQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIE---RQEDEAKTAAQLCADLQSKERLKQEQA 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1646 SQIEAANKGREDAIK----QLRKLQAQTKDYQRELEEARASRDDIFAQSKENEKKLKGL------------EAEILQLQE 1709
Cdd:TIGR00606 429 DEIRDEKKGLGRTIElkkeILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELskaeknsltetlKKEVKSLQN 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1710 ELAASERSRRHAEQERDELADEISNSTSGKSALLDEK------RRLEARIAHLEEELEEEQSNMELLNDRFRKTTLQVDT 1783
Cdd:TIGR00606 509 EKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMdkdeqiRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQ 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1784 LNSELAAERSSGQKSENARQQLERQNKELKAKLQELEGSVkskFKA-TIATLESKIAQLEEQLEQEAKERV----ASN-- 1856
Cdd:TIGR00606 589 TRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKL---FDVcGSQDEESDLERLKEEIEKSSKQRAmlagATAvy 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1857 ------------------KLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANTRMKqlKRQLEEAEEEATRANASARKl 1918
Cdd:TIGR00606 666 sqfitqltdenqsccpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKE--KRRDEMLGLAPGRQSIIDLK- 742
|
570 580
....*....|....*....|....*..
gi 148223878 1919 QRELDDATEANEVLSREVSTLKNRLRR 1945
Cdd:TIGR00606 743 EKEIPELRNKLQKVNRDIQRLKNDIEE 769
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1046-1402 |
1.52e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.98 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1046 KQEMMISDLEERLKKEEKTRQELEKAKRKLDGETTD-------FQDQIAELQAQIEELKLQLAKKEEEL------QAALA 1112
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAQEAANRQREKEKERykrdreqWERQRRELESRVAELKEELRQSREKHeeleekYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1113 RGDEEVLQKNNTLKLVR-ELQAQIAELQEDLESekasrnkAEKQKRDLSEELEALKTELEDTL----DTTAAQQELRTKR 1187
Cdd:pfam07888 108 ASSEELSEEKDALLAQRaAHEARIRELEEDIKT-------LTQRVLERETELERMKERAKKAGaqrkEEEAERKQLQAKL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1188 EQEVAELRKSIEE--ETRNHEAQIQEMRQRQATALEELSEQLEQAKRFKVNLEKNKQSLESDNKELATEVKSLQQMKAES 1265
Cdd:pfam07888 181 QQTEEELRSLSKEfqELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEEL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1266 EYKRKKLEGQVQELHAKVLEGDRLRADMVEKSSKLQNELENVS----SLLEEAEKKGIKLAKdvasMESQLQDTQELLQE 1341
Cdd:pfam07888 261 SSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAqereTLQQSAEADKDRIEK----LSAELQRLEERLQE 336
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148223878 1342 ET--RQKL------NQSSRIRQLEEEKNNLQEQQEEEEEARKSLEkQILSLQSQLIEAKKKVDDEVGTI 1402
Cdd:pfam07888 337 ERmeREKLevelgrEKDCNRVQLSESRRELQELKASLRVAQKEKE-QLQAEKQELLEYIRQLEQRLETV 404
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1553-1754 |
1.60e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1553 DQQVEEMRTQLEELEDELQGTEDAKLRLEVNMQAMKAQFErDLQTRDEQNEEKKRALVKQVRELEAELEDERKQRAMAVA 1632
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1633 IKKKLEMDMKDFESQIEAANKGreDAIKQLRKLQAQTKDYQRELEEARASRDDIFAQSKENEKKLKGLEAEILQLQEELA 1712
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSESFS--DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 148223878 1713 ASERSRRHAEQERDELADEISNSTSGKSALLDEKRRLEARIA 1754
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1499-1853 |
1.63e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.98 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1499 KALSLARALDEALEAQDE----FERLNKQLRAEMEDLMSSKDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDELQGTE 1574
Cdd:pfam07888 28 RAELLQNRLEECLQERAEllqaQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1575 DAKLRLEVNMQAMKAQFERDLQtRDEQNEEKKRALVKQVRELEAELEDERKQRAMAVAIKKKLEMDMKDFES---QIEAA 1651
Cdd:pfam07888 108 ASSEELSEEKDALLAQRAAHEA-RIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAklqQTEEE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1652 NKGREDAIKQLRKLQAQTKDYQRELEEARASRDDIFAQSKENEKKLKGLEAEILQLQEELAASERSrrhAEQERDELADE 1731
Cdd:pfam07888 187 LRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERK---VEGLGEELSSM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1732 ISNSTSGKSALldEKRRLEARiahleeeleeeqsnmellndrfrKTTLQVdtlnselaAERSSGQKSENARQQLERQNKE 1811
Cdd:pfam07888 264 AAQRDRTQAEL--HQARLQAA-----------------------QLTLQL--------ADASLALREGRARWAQERETLQ 310
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 148223878 1812 LKAKLQelegsvkskfKATIATLESKIAQLEEQLEQEAKERV 1853
Cdd:pfam07888 311 QSAEAD----------KDRIEKLSAELQRLEERLQEERMERE 342
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1421-1632 |
2.72e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1421 QRLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAE-EKNISARHAEERDRA----EADARE 1495
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEaEAEIEERREELGERAralyRSGGSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1496 KETKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDdvgknvhELEKSKRALDQQVEEMRTQLEELEDELQGTED 1575
Cdd:COG3883 103 SYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKA-------ELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 148223878 1576 AKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRALVKQVRELEAELEDERKQRAMAVA 1632
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
994-1231 |
2.93e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 52.24 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 994 KIKKMEED-ILVLEDQNSKFLKE---------KKLLEERIAESTSQLAEEEEKAKN-LAKLKN-----------KQEMMI 1051
Cdd:PRK05771 2 APVRMKKVlIVTLKSYKDEVLEAlhelgvvhiEDLKEELSNERLRKLRSLLTKLSEaLDKLRSylpklnplreeKKKVSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1052 SDLEERLKKEEKTRQELEKAKRKLDGETTDFQDQIAELQAQIEELKLqLAKKEEELQaaLARGDEEVLQKNNTLKLVREL 1131
Cdd:PRK05771 82 KSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEP-WGNFDLDLS--LLLGFKYVSVFVGTVPEDKLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1132 QAQIAELQEDLESEKASRNK-------AEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKrEQEVAELRKSIEEETRN 1204
Cdd:PRK05771 159 ELKLESDVENVEYISTDKGYvyvvvvvLKELSDEVEEELKKLGFERLELEEEGTPSELIREI-KEELEEIEKERESLLEE 237
|
250 260
....*....|....*....|....*..
gi 148223878 1205 HEAQIQEMRQRQATALEELSEQLEQAK 1231
Cdd:PRK05771 238 LKELAKKYLEELLALYEYLEIELERAE 264
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1028-1697 |
3.01e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 52.65 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1028 SQLAEEEEKAKNLAKLKNKQEMMISDLEERLKKEEKTRQELEKAKRKLDGETTDFQDQIAELQAQIEELKlQLAKKEEEL 1107
Cdd:COG3096 529 RQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELA-ARAPAWLAA 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1108 QAALARGDEEVlqkNNTLKLVRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALkteledTLDTTAAQQELRTKR 1187
Cdd:COG3096 608 QDALERLREQS---GEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERL------SQPGGAEDPRLLALA 678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1188 EQEVAELRKSIEEETRNHEAQIQEMR---QRQATALEELS---EQLEQAKRFKVNL---EKNKQS-----LESDNKELAT 1253
Cdd:COG3096 679 ERLGGVLLSEIYDDVTLEDAPYFSALygpARHAIVVPDLSavkEQLAGLEDCPEDLyliEGDPDSfddsvFDAEELEDAV 758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1254 EVKSLQQMKAESEYK------RKKLEGQVQELHAKVLEGDRLRADMVEKSSKLQNELENVSSLLeeaekkgiklakdvas 1327
Cdd:COG3096 759 VVKLSDRQWRYSRFPevplfgRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFV---------------- 822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1328 mESQLQDTQELLQEETRQKLNQssRIRQLEEEKNNlqeqqeeeeearksLEKQILSLQSQLIEAKkkvddevgtiEGLEE 1407
Cdd:COG3096 823 -GGHLAVAFAPDPEAELAALRQ--RRSELERELAQ--------------HRAQEQQLRQQLDQLK----------EQLQL 875
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1408 VKKKL----LKDTEGLGQRLEEKIIAYEKLEKTKNRLQQ------ELDDlmvdldhqrqIVSNLEKKQKKFDQLLAEEKN 1477
Cdd:COG3096 876 LNKLLpqanLLADETLADRLEELREELDAAQEAQAFIQQhgkalaQLEP----------LVAVLQSDPEQFEQLQADYLQ 945
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1478 ISARHAEERDRAEAdarEKETKALSLARALDEALEAQDEFERLNKQLRAemedlmsskddvgknvhELEKSKRALDQQVE 1557
Cdd:COG3096 946 AKEQQRRLKQQIFA---LSEVVQRRPHFSYEDAVGLLGENSDLNEKLRA-----------------RLEQAEEARREARE 1005
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1558 EMRTQLEELEDELQGTEDAKLRLEVNMQaMKAQFERDLQ----TRDEQNEEKKRAlvkQVRELEAELEDERKQRAmavai 1633
Cdd:COG3096 1006 QLRQAQAQYSQYNQVLASLKSSRDAKQQ-TLQELEQELEelgvQADAEAEERARI---RRDELHEELSQNRSRRS----- 1076
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148223878 1634 kkKLEMDMKDFESQIEAANkgredaiKQLRKLQAQTKDYQRELEEARASRDDIFAQSKEN--EKKL 1697
Cdd:COG3096 1077 --QLEKQLTRCEAEMDSLQ-------KRLRKAERDYKQEREQVVQAKAGWCAVLRLARDNdvERRL 1133
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
870-1110 |
3.06e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 870 LVAKDEELLKVKEKQSKVEGELVDMEQKHQQLVEEKNILAEQLhaetelfAEAEEMRARLAIKKQEMEEILRDLEIRMEE 949
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL-------AALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 950 EEERNQVLQNEKKKMQTHVQDLEEQLDEEEAAQKLQLekVTAEAKIKKMEEDILVLEDQNSKFLKEKKLLEERIAESTSQ 1029
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1030 LAEEEEKAKNLAKLKNKQEMMISDLEERLKKEEKTRQELEKAKRKLDGETTDFQDQIAELQAQIEELKLQLAKKEEELQA 1109
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
.
gi 148223878 1110 A 1110
Cdd:COG4942 246 A 246
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1035-1167 |
3.21e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 52.52 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1035 EKAK-NLAKLKNKQEMMISDLEERLKKEEKTRQELEKAKRKLDGETTDFQDQIAELQAQIEELKLQLakkEEELQAALAR 1113
Cdd:PRK00409 505 EEAKkLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKE 581
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 148223878 1114 GDEEVLQKNNTLK-LVRELQAQIA--ELQEDLESEKASRNKAEKQKRDLSEELEALK 1167
Cdd:PRK00409 582 AKKEADEIIKELRqLQKGGYASVKahELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
982-1193 |
3.42e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 982 QKLQLEKVTAEAKIKKMEEDILVLEDQNSKFLKEKKLLEERIAESTSQLAEEEEKAKNLAKLKNKQEMMIS--------- 1052
Cdd:COG3883 33 EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSyldvllgse 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1053 DLEERLKKEEKTRQELEKAKRKLDgettdfqdQIAELQAQIEELKLQLAKKEEELQAALARGDEEVlqknntlklvRELQ 1132
Cdd:COG3883 113 SFSDFLDRLSALSKIADADADLLE--------ELKADKAELEAKKAELEAKLAELEALKAELEAAK----------AELE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148223878 1133 AQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAE 1193
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1700-1942 |
3.78e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1700 LEAEILQLQEELAASERSRRHAEQERDELAdeisnstsgksaLLDEKRRLEARIAHLEEELEEEQSNMELLNDRFRKTtl 1779
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAREQIE------------LLEPIRELAERYAAARERLAELEYLRAALRLWFAQR-- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1780 QVDTLNSELAAERSSGQKSENARQQLERQNKELKAKLQELEGSVKSKFKATIATLESKIAQLEEQLEQEAKERvasnklv 1859
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRR------- 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1860 RRTEKKLKEVFMQVEDErrhADQYKEQMEKANTRMKQLKRQLEEAEEEATRANASARKLQRELDDateanevLSREVSTL 1939
Cdd:COG4913 362 ARLEALLAALGLPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE-------LEAEIASL 431
|
...
gi 148223878 1940 KNR 1942
Cdd:COG4913 432 ERR 434
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1139-1518 |
3.82e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.05 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1139 QEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELRKsiEEETRNHEAQIQEMRQRQAT 1218
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQ--EERKRELERIRQEEIAMEIS 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1219 ALEELsEQLeQAKRFKVNlEKNKQSLESDNKELATE---VKSLQQMKAESEYKRKKLEgQVQELHAKVLEGDRLRadmve 1295
Cdd:pfam17380 376 RMREL-ERL-QMERQQKN-ERVRQELEAARKVKILEeerQRKIQQQKVEMEQIRAEQE-EARQREVRRLEEERAR----- 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1296 kssklqnELENVSslLEEAEKKgiklakdvASMESQLQDTQEllQEETRQKLNQSSRIRQLEEEKNnlqeqqeeeeeaRK 1375
Cdd:pfam17380 447 -------EMERVR--LEEQERQ--------QQVERLRQQEEE--RKRKKLELEKEKRDRKRAEEQR------------RK 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1376 SLEKQILSLQSQLIEakkkvddevgtieglEEVKKKLLKdteglgQRLEEKIIAYekLEKTKNRLQQELDDLMVDLDHQR 1455
Cdd:pfam17380 496 ILEKELEERKQAMIE---------------EERKRKLLE------KEMEERQKAI--YEEERRREAEEERRKQQEMEERR 552
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148223878 1456 QIVSNLEKKqkkfdqllaeeknisarhAEERDRAEADAREKEtkalsLARALDEALEAQDEFE 1518
Cdd:pfam17380 553 RIQEQMRKA------------------TEERSRLEAMERERE-----MMRQIVESEKARAEYE 592
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1280-1630 |
4.34e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 51.22 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1280 HAKVLEGDRLRADMVEKSSKLQNELENVSSLLEEAEKkgiklakDVASMESQLQDTQELLQEETRQKLNQSSRIRQLEEE 1359
Cdd:pfam19220 47 KSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEG-------ELEELVARLAKLEAALREAEAAKEELRIELRDKTAQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1360 KNNLQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNR 1439
Cdd:pfam19220 120 AEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1440 LQQELDDlmvdldhQRQIVSNLEKKqkkfdqlLAEEKNISARHAEERDRAEADAREKETkalSLARALDEALEAQDEFER 1519
Cdd:pfam19220 200 LETQLDA-------TRARLRALEGQ-------LAAEQAERERAEAQLEEAVEAHRAERA---SLRMKLEALTARAAATEQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1520 LNKQLRAEMEDLMSSKDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDELQGTEDAKLRLE--VNM-----QAMKAQFE 1592
Cdd:pfam19220 263 LLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEerAEMltkalAAKDAALE 342
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 148223878 1593 R------DLQTRDEQ----NEEKKRALVKQVRELEAELEDERKQRAMA 1630
Cdd:pfam19220 343 RaeeriaSLSDRIAEltkrFEVERAALEQANRRLKEELQRERAERALA 390
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1130-1283 |
6.40e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.54 E-value: 6.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1130 ELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTldttaaqQELRTKREQEVAELRKSIEE--------- 1200
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL-------EKEIKRLELEIEEVEARIKKyeeqlgnvr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1201 ---ETRNHEAQIQEMRQRQATALEELSEQLEQAKRFKVNLEKNKQSLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQ 1277
Cdd:COG1579 87 nnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*.
gi 148223878 1278 ELHAKV 1283
Cdd:COG1579 167 ELAAKI 172
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
990-1313 |
6.91e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 50.99 E-value: 6.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 990 TAEAKIKKMEEDILVL---EDQNSKFLKE---------KKLLEER------IAESTSQLAEEEEKAKNLAKLKN-----K 1046
Cdd:PRK04778 116 LIEEDIEQILEELQELlesEEKNREEVEQlkdlyrelrKSLLANRfsfgpaLDELEKQLENLEEEFSQFVELTEsgdyvE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1047 QEMMISDLEERLKKEEKTRQELEKAKRKLDgetTDFQDQIAELQAQIEELKLQ---------------LAKKEEELQAAL 1111
Cdd:PRK04778 196 AREILDQLEEELAALEQIMEEIPELLKELQ---TELPDQLQELKAGYRELVEEgyhldhldiekeiqdLKEQIDENLALL 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1112 ARGDEEVLQKNNtlklvRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAaqqelrtkREQEV 1191
Cdd:PRK04778 273 EELDLDEAEEKN-----EEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEID--------RVKQS 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1192 AELRKSIEEETRNHEAQIQEMRQRqataLEELSEQL-EQAKRF---KVNLEKNKQSLESDNKELATEVKSLQQMKAESEY 1267
Cdd:PRK04778 340 YTLNESELESVRQLEKQLESLEKQ----YDEITERIaEQEIAYselQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELE 415
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 148223878 1268 KRKKLEGQVQELHAKVLEGDRLR-----ADMVEKSSKLQNELENVSSLLEE 1313
Cdd:PRK04778 416 AREKLERYRNKLHEIKRYLEKSNlpglpEDYLEMFFEVSDEIEALAEELEE 466
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
994-1341 |
7.47e-06 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 51.01 E-value: 7.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 994 KIKKMEEDILVLEDQNSK--FLKEKKLLEEriaeSTSQLAEEEEKAKNlaklknkqemMISDLEERLKKEEKTRQELEKA 1071
Cdd:pfam06160 61 SLPDIEELLFEAEELNDKyrFKKAKKALDE----IEELLDDIEEDIKQ----------ILEELDELLESEEKNREEVEEL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1072 K-------RKLDGETTDFQDQIAELQAQIEELKLQLAKKEEELQAalarGD----EEVLQK-NNTLKLVRELQAQIAELQ 1139
Cdd:pfam06160 127 KdkyrelrKTLLANRFSYGPAIDELEKQLAEIEEEFSQFEELTES----GDyleaREVLEKlEEETDALEELMEDIPPLY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1140 EDLESEkasrnkaekqkrdLSEELEALK---TELED---TLDTTAAQQELRTKREQeVAELRKSIEE-ETRNHEAQIQEM 1212
Cdd:pfam06160 203 EELKTE-------------LPDQLEELKegyREMEEegyALEHLNVDKEIQQLEEQ-LEENLALLENlELDEAEEALEEI 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1213 RQRqataLEELSEQLEQAKRFKVNLEKNKQSLESD-------NKELATEVKSLQQ---MKAESEYKRKKLEGQVQELHAK 1282
Cdd:pfam06160 269 EER----IDQLYDLLEKEVDAKKYVEKNLPEIEDYlehaeeqNKELKEELERVQQsytLNENELERVRGLEKQLEELEKR 344
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148223878 1283 VlegDRLRADMVEKS---SKLQNELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQE 1341
Cdd:pfam06160 345 Y---DEIVERLEEKEvaySELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDE 403
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1568-1941 |
7.67e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 7.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1568 DELQGTEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRALVKQVRELEAELE--DERKQRAMAVAIKKKLEMDMKDFE 1645
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1646 SQIEAAnkgrEDAIKQLRKLQAQTKDYQRELEEARASRDDIFAQ-SKENEKKLKGLEAEILQLQEELAASERSRRHAEQE 1724
Cdd:COG4717 146 ERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1725 RDELADEISNSTSGKSALLDEKRRLEARI-------------------AHLEEELEEEQSNMELLNDRFRKTTLQVDTLN 1785
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERLKEARLllliaaallallglggsllSLILTIAGVLFLVLGLLALLFLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1786 SELAAERSSGQKSENARQQLERQNKELKAKLQELEGSVKSKFK--ATIATLESKIAQLEEQLEQEAkervasnkLVRRTE 1863
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDriEELQELLREAEELEEELQLEE--------LEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1864 KKLKEVFMQVEDERRHADQYKEQMEKANTRMKQLKRQLEEAEEEAT----------------RANASARKLQRELDDATE 1927
Cdd:COG4717 374 ALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEellealdeeeleeeleELEEELEELEEELEELRE 453
|
410
....*....|....
gi 148223878 1928 ANEVLSREVSTLKN 1941
Cdd:COG4717 454 ELAELEAELEQLEE 467
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1206-1466 |
7.82e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1206 EAQIQEMRQRQATALEELSEQLEqaKRFKVNLEKNKQ----SLESDNKELATEV----------KSLQQMKAESEYKRKK 1271
Cdd:COG3206 102 KLNLDEDPLGEEASREAAIERLR--KNLTVEPVKGSNvieiSYTSPDPELAAAVanalaeayleQNLELRREEARKALEF 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1272 LEGQVQELHAKVLEGDRLRADMVEKSS--KLQNELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQE--ETRQKL 1347
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSgpDALPEL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1348 NQSSRIRQLEEEKNNLQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLKDTEglgQRLEEKI 1427
Cdd:COG3206 260 LQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQARE---ASLQAQL 336
|
250 260 270
....*....|....*....|....*....|....*....
gi 148223878 1428 IAYEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQK 1466
Cdd:COG3206 337 AQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1357-1812 |
8.20e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 8.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1357 EEEKNNLQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEvkkkllkDTEGLGQRL---EEKIIAYEKL 1433
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQ-------DYQAASDHLnlvQTALRQQEKI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1434 EktknRLQQELDDLMVDLDHQRQIVSNLekkqkkfdqllaeeknisarhAEERDRAEADAREKETKALSLARALDEALEA 1513
Cdd:PRK04863 351 E----RYQADLEELEERLEEQNEVVEEA---------------------DEQQEENEARAEAAEEEVDELKSQLADYQQA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1514 QDEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKskraLDQQVEEMRTQLEELEDELQGTEDaKLRLEvnmQAMKAQFER 1593
Cdd:PRK04863 406 LDVQQTRAIQYQQAVQALERAKQLCGLPDLTADN----AEDWLEEFQAKEQEATEELLSLEQ-KLSVA---QAAHSQFEQ 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1594 DLQTRDEQNEEKKRALVKQV-RELEAELEDERKQRAMAVAIKKKLEMDMKDFESQiEAANKGREDAIKQLRKLQAQTKDY 1672
Cdd:PRK04863 478 AYQLVRKIAGEVSRSEAWDVaRELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQ-QRAERLLAEFCKRLGKNLDDEDEL 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1673 QRELEEarasrddifaqskenekklkgLEAEILQLQEELAASERSRRHAEQERDELADEISNSTSGKSALLDEKRRLEAR 1752
Cdd:PRK04863 557 EQLQEE---------------------LEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARL 615
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148223878 1753 IAHLEEELEEEQSNMELLND---RFRKTTLQVDtlnselaaerssgqKSENARQQLERQNKEL 1812
Cdd:PRK04863 616 REQSGEEFEDSQDVTEYMQQlleRERELTVERD--------------ELAARKQALDEEIERL 664
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1019-1168 |
8.45e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.01 E-value: 8.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1019 LEERIAESTSQLAEEEEKAKNLAKLKnkQEMMISDLEERLKKEEKTRQELEKakrkldgETTDFQDQIAELQAQIEELKL 1098
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEH--EERELTEEEEEIRRLEEQVERLEA-------EVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1099 QLAKKEEELQAALARGDEevlqknntlklVRELQAQIAELQEDLESEkasrnkaEKQKRDLSEELEALKT 1168
Cdd:COG2433 449 ELSEARSEERREIRKDRE-----------ISRLDREIERLERELEEE-------RERIEELKRKLERLKE 500
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1061-1355 |
9.11e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.82 E-value: 9.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1061 EEKTRQELEKAKrklDGETTDFQDQIAELQAQIEELklqlakkeEELQAALARGDEEVLQKNNTLKLVRELQAQIAElqe 1140
Cdd:PRK10929 25 EKQITQELEQAK---AAKTPAQAEIVEALQSALNWL--------EERKGSLERAKQYQQVIDNFPKLSAELRQQLNN--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1141 dlESEKASrnkaekqkrdlseelealkteledTLDTTAAQQELrtkrEQEVAELRKSIEEETRnhEAQIQEMRQRQ-ATA 1219
Cdd:PRK10929 91 --ERDEPR------------------------SVPPNMSTDAL----EQEILQVSSQLLEKSR--QAQQEQDRAREiSDS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1220 LEELSEQLEQAKRFKVNLEKNKQSLESDNKELATevKSLQQMKAESEYKRKKlegqVQELHAKVL------EGDRLRADM 1293
Cdd:PRK10929 139 LSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQ--AQLTALQAESAALKAL----VDELELAQLsannrqELARLRSEL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1294 VEK-SSKLQNELENVSSLL--------EEAEKKGIKLAKDVASME----SQLQDTQELLQE-------------ETRQKL 1347
Cdd:PRK10929 213 AKKrSQQLDAYLQALRNQLnsqrqreaERALESTELLAEQSGDLPksivAQFKINRELSQAlnqqaqrmdliasQQRQAA 292
|
....*...
gi 148223878 1348 NQSSRIRQ 1355
Cdd:PRK10929 293 SQTLQVRQ 300
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1078-1224 |
9.17e-06 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 50.11 E-value: 9.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1078 ETTDFQDQIAELQAQIEELKLQLAKKE------EELQAALARGDEEVLQKNNTLK----LVRELQAQIAELQEDLESEKA 1147
Cdd:pfam00529 52 DPTDYQAALDSAEAQLAKAQAQVARLQaeldrlQALESELAISRQDYDGATAQLRaaqaAVKAAQAQLAQAQIDLARRRV 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148223878 1148 SRNKAEKQKRDLsEELEALKTELEDTLDTTAAQQE-LRTKREQEVAELRKSIEEETRNHEAQIQEMRQRQATALEELS 1224
Cdd:pfam00529 132 LAPIGGISRESL-VTAGALVAQAQANLLATVAQLDqIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
983-1121 |
1.04e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 983 KLQLEKVTAEAKIKKMEEDILVLEDQNSKFLKEKKLLEERIAESTSQLAEEEEKAKNLAKLK---------NKQEMMISD 1053
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyealqkeiESLKRRISD 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148223878 1054 LEERLK----KEEKTRQELEKAKRKLDGETTDFQDQIAELQAQIEELKLQLAKKEEELQAALARGDEEVLQK 1121
Cdd:COG1579 108 LEDEILelmeRIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPELLAL 179
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
902-1281 |
1.06e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.72 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 902 VEEKNILAEQ-LHAETELF------AEAEEMRARLAIKKQEMEEILRDLEIRMEEEEERNQVLQNekkkmqthvqdleeq 974
Cdd:COG3096 277 ANERRELSERaLELRRELFgarrqlAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQT--------------- 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 975 ldeeeaaqklqleKVTAEAKIKKMEEDilvLEDQNSKFLKEKKLLEER-----IAESTSQLAEEE-EKAKN-LAKLKNKQ 1047
Cdd:COG3096 342 -------------ALRQQEKIERYQED---LEELTERLEEQEEVVEEAaeqlaEAEARLEAAEEEvDSLKSqLADYQQAL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1048 EMmisdLEERLKKEEKTRQELEKAKRKL---DGETTDFQDQIAELQAQIEEL---------KLQLAKK-----EEELQA- 1109
Cdd:COG3096 406 DV----QQTRAIQYQQAVQALEKARALCglpDLTPENAEDYLAAFRAKEQQAteevleleqKLSVADAarrqfEKAYELv 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1110 -----ALARGD-----EEVLQKNNTLKLVRE----LQAQIAELQEDLESEKASR------NKAEKQKRDLSEELEALKTE 1169
Cdd:COG3096 482 ckiagEVERSQawqtaRELLRRYRSQQALAQrlqqLRAQLAELEQRLRQQQNAErlleefCQRIGQQLDAAEELEELLAE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1170 LEDTLDTTAAQQElrtkreqEVAELRKSIEEETRNHEAQIQEMRQRQ------ATALEELSEQLEQAkrfkvnLEkNKQS 1243
Cdd:COG3096 562 LEAQLEELEEQAA-------EAVEQRSELRQQLEQLRARIKELAARApawlaaQDALERLREQSGEA------LA-DSQE 627
|
410 420 430
....*....|....*....|....*....|....*...
gi 148223878 1244 LESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELHA 1281
Cdd:COG3096 628 VTAAMQQLLEREREATVERDELAARKQALESQIERLSQ 665
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1060-1324 |
1.21e-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: 464932 [Multi-domain] Cd Length: 329 Bit Score: 49.42 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1060 KEEKTRQELEKAKRKLDGETTdfqdqiaELQAQIEELKLQLAKKEEELQAALArgdeevlQKNNTLKLVRELQAQIAELQ 1139
Cdd:pfam15905 70 KESKDQKELEKEIRALVQERG-------EQDKRLQALEEELEKVEAKLNAAVR-------EKTSLSASVASLEKQLLELT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1140 E--DLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELRKSIEEETRNHEAQIQEMR---- 1213
Cdd:pfam15905 136 RvnELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEkeki 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1214 ------QRQATALEELSEQLEQAKRFKVNLEKNKQSLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELHAkvlEGD 1287
Cdd:pfam15905 216 eeksetEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLES---EKE 292
|
250 260 270
....*....|....*....|....*....|....*..
gi 148223878 1288 RLRADMVEKSSKLQNELENVSSLLEEAEKKGIKLAKD 1324
Cdd:pfam15905 293 ELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1199-1387 |
1.29e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1199 EEETRNHEAQIQEMRQRQATALEELSEQLEQAKRFKVNLEKNKQSLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQE 1278
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1279 LH---------AKVLEGDRL-----RADMVEK-SSKLQNELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQEET 1343
Cdd:COG3883 95 LYrsggsvsylDVLLGSESFsdfldRLSALSKiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 148223878 1344 RQKLNQSSRIRQLEEEKNNLQEQQEEEEEARKSLEKQILSLQSQ 1387
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
903-1151 |
1.60e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 903 EEKNILAEQLHAETELFAEAEEMRARLAIKKQEMEEILRDLEIRMEEEEERNQVLQNEKKKMQThvqdleeqldeeeAAQ 982
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA-------------ELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 983 KLQLEKVTAEAKIKKMEEDilvLEDQNSKFLKEKKLLEERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKKEE 1062
Cdd:COG4942 87 ELEKEIAELRAELEAQKEE---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1063 KTRQELEKAKRKLDGETTDFQDQIAELQAQIEELKLQLAKKEEELQAALARGDEEVLQKNNTLKLVRELQAQIAELQEDL 1142
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
....*....
gi 148223878 1143 ESEKASRNK 1151
Cdd:COG4942 244 PAAGFAALK 252
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1535-1754 |
1.61e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1535 KDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDELQ------GTEDAKLRLEVNMQAMKaqferDLQTRDEQNEEKKRA 1608
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefrqknGLVDLSEEAKLLLQQLS-----ELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1609 LVKQVRELEAELEDERKQRAMAVA--IKKKLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQREL-EEARASRDD 1685
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLqQEAQRILAS 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148223878 1686 IFAQSKENEKKLKGLEAEILQLQEELAASERsrrhAEQERDELADEISNSTSGKSALLdeKRRLEARIA 1754
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARLAELPE----LEAELRRLEREVEVARELYESLL--QRLEEARLA 380
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1437-1945 |
1.74e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.22 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1437 KNRLQ-QELDDLMVDLDHQRQIVSN---LEKKQKKFDQLLAEEKNISARHAEERDRAEADAREKETKALSLARaldeale 1512
Cdd:pfam12128 215 KSRLNrQQVEHWIRDIQAIAGIMKIrpeFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAE------- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1513 aqdeferLNKQLRaemedlmSSKDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDELQGTEDAKLRLEVNMQAMKAQFE 1592
Cdd:pfam12128 288 -------LNQLLR-------TLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQ 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1593 RDLqtrdEQNEEKKRALVKQVRELEAELedERKQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKDy 1672
Cdd:pfam12128 354 SEL----ENLEERLKALTGKHQDVTAKY--NRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELRE- 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1673 qrELEEARASRDDIFAQSKENEKKLKGLEAEILQLQEELAASERSRRHAEQERDELadeiSNSTSGKSALLDEKRRLEAR 1752
Cdd:pfam12128 427 --QLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQ----EAANAEVERLQSELRQARKR 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1753 IAHLEEELEEEQSNMELLNDRFRKTTLQVDT--------LNSELAAERSSGQKSEnARQQLER----------------- 1807
Cdd:pfam12128 501 RDQASEALRQASRRLEERQSALDELELQLFPqagtllhfLRKEAPDWEQSIGKVI-SPELLHRtdldpevwdgsvggeln 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1808 -----------QNKELKAKLQELEgSVKSKFKATIATLESKIAQLEEQLEQEAKERVASNK---LVRRTEKKLKEVFMQV 1873
Cdd:pfam12128 580 lygvkldlkriDVPEWAASEEELR-ERLDKAEEALQSAREKQAAAEEQLVQANGELEKASReetFARTALKNARLDLRRL 658
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148223878 1874 EDERRhadQYKEQMEKANTRMKQLKRQleeaeeEATRANASARKLQRELDDATEANEVLSREVSTLKNRLRR 1945
Cdd:pfam12128 659 FDEKQ---SEKDKKNKALAERKDSANE------RLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQ 721
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
673-697 |
2.74e-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: 46.57 E-value: 2.74e-05
10 20
....*....|....*....|....*
gi 148223878 673 YKESLAKLMATLRNTNPNFVRCIIP 697
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
852-1284 |
2.94e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 852 RLFTKVKPLLQVTRQEEELVAKDEELLKVKEKQSKVEgELVDMEQKHQQLVEEKNILAEQLHAETELFAEAEEMRARLAI 931
Cdd:COG4717 89 EYAELQEELEELEEELEELEAELEELREELEKLEKLL-QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 932 KKQEMEEILRDLEirMEEEEERNQVLQNEKKKMQTHVQDLEEQLDEEEAAQKLQLEKVTAEAKIKKMEEDILVLEDQNSk 1011
Cdd:COG4717 168 LEAELAELQEELE--ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1012 fLKEKKLLEERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKKEEKTRQELEKAKRKLDGETTDFQDQIAELQA 1091
Cdd:COG4717 245 -LKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1092 QIEELKLQLAKKEEELQAALARGDEevlqknntlklVRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELE 1171
Cdd:COG4717 324 LLAALGLPPDLSPEELLELLDRIEE-----------LQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1172 DTLDTTAAQQELRTKREQEVAELRKSIEEETRNHEAQIQEMRQRQATALEELSEQLEQakrfkvnLEKNKQSLESDNKEL 1251
Cdd:COG4717 393 QAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEE-------LREELAELEAELEQL 465
|
410 420 430
....*....|....*....|....*....|...
gi 148223878 1252 ATEvKSLQQMKAESEYKRKKLEGQVQELHAKVL 1284
Cdd:COG4717 466 EED-GELAELLQELEELKAELRELAEEWAALKL 497
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1419-1872 |
3.07e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1419 LGQRLEEKIIAYEKLE-KTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEknisarhaeerdraeADAREKE 1497
Cdd:COG4717 47 LLERLEKEADELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEEL---------------EELEAEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1498 TKALSLARALDEALEAQDEFERLnKQLRAEMEDLMsskddvgknvHELEKSKRALdQQVEEMRTQLEELEDELQGTEDAK 1577
Cdd:COG4717 112 EELREELEKLEKLLQLLPLYQEL-EALEAELAELP----------ERLEELEERL-EELRELEEELEELEAELAELQEEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1578 LRLEVNMQAMKAQFERDLQTRDEQNEEKKRALVKQVRELEAELEDERKQRAMAVAIKKKLEMDMK--------------- 1642
Cdd:COG4717 180 EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaaall 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1643 ----------------------------DFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDIFAQSKENE 1694
Cdd:COG4717 260 allglggsllsliltiagvlflvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1695 KKLKGLEAEILQLQEELAASERSRR--HAEQERDELADEISNST----SGKSALLDEKRRLEARIAHLEEELEEEQSNME 1768
Cdd:COG4717 340 LELLDRIEELQELLREAEELEEELQleELEQEIAALLAEAGVEDeeelRAALEQAEEYQELKEELEELEEQLEELLGELE 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1769 LLNDrfrktTLQVDTLNSELAAERSSGQKSENARQQLERQNKELKAKLQELEGSvkskfkATIATLESKIAQLEEQLEQE 1848
Cdd:COG4717 420 ELLE-----ALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED------GELAELLQELEELKAELREL 488
|
490 500
....*....|....*....|....
gi 148223878 1849 AKERvASNKLVRRTEKKLKEVFMQ 1872
Cdd:COG4717 489 AEEW-AALKLALELLEEAREEYRE 511
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1514-1942 |
3.31e-05 |
|
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: 48.86 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1514 QDEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKskraLDQQVEEMRTQLEELEDELQGTEDAKLRLEVNMQAMKAQFer 1593
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEK----LNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL-- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1594 dlqTRDEQNEEKKRALVKQVRELEAELEDERKQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQ 1673
Cdd:TIGR04523 197 ---LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQ 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1674 RELEEARAsrddifaQSKENEKKLKGLEAEILQLQEELAASERSR-----RHAEQERDELADEISNSTSGKSALLDEKRR 1748
Cdd:TIGR04523 274 KELEQNNK-------KIKELEKQLNQLKSEISDLNNQKEQDWNKElkselKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1749 LEARIAHLeeeleeeQSNMELLNDRFRKTTLQVDTLNSELAAERSSGQKSENARQQLERQNKELKAKLQELEGSVKskfk 1828
Cdd:TIGR04523 347 LKKELTNS-------ESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK---- 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1829 atiaTLESKIAQLEEQLEQEAKERVASNKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANTRMKQLKRQLEEAEEEA 1908
Cdd:TIGR04523 416 ----KLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEL 491
|
410 420 430
....*....|....*....|....*....|....
gi 148223878 1909 TRANASARKLQRELDDATEANEVLSREVSTLKNR 1942
Cdd:TIGR04523 492 KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK 525
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
986-1154 |
3.43e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 986 LEKVTAEAKIKKMEED---ILVLEDQNSKFLKEKKLLE--ERIAESTSQLAEE-EEKAKNLAKLKNKQEMMISDLEERLK 1059
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEakrILEEAKKEAEAIKKEALLEakEEIHKLRNEFEKElRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1060 KEEKTRQELEKAKRKLDGEttdfQDQIAELQAQIEELKLQLAKKEEE---LQAALARgdEEVLQknntlKLVRELQAQIA 1136
Cdd:PRK12704 104 LLEKREEELEKKEKELEQK----QQELEKKEEELEELIEEQLQELERisgLTAEEAK--EILLE-----KVEEEARHEAA 172
|
170
....*....|....*...
gi 148223878 1137 ELQEDLESEkaSRNKAEK 1154
Cdd:PRK12704 173 VLIKEIEEE--AKEEADK 188
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1031-1383 |
3.65e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1031 AEEEEKAKNLAKLKNKQEMMISDLEERLKKEEKTRQELEKAKRKLDGETTDFQDQIAELQAQIEELKLQLAKKEEELQaa 1110
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1111 largdEEVLQKNNTLKLVRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQE 1190
Cdd:COG4372 84 -----ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1191 VAELRKSIEEETRNHEAQIQEMRQRQataLEELSEQLEQAKRFKVNLEKNKQSLESDNKELATEVKSLQQMKAESEYKRK 1270
Cdd:COG4372 159 LESLQEELAALEQELQALSEAEAEQA---LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1271 KLEGQVQELHAKVLEGDRLRADMVEKSSKLQNELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQEETRQKLNQS 1350
Cdd:COG4372 236 SALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
330 340 350
....*....|....*....|....*....|...
gi 148223878 1351 SRIRQLEEEKNNLQEQQEEEEEARKSLEKQILS 1383
Cdd:COG4372 316 ALLAALLELAKKLELALAILLAELADLLQLLLV 348
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1510-1945 |
3.79e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.81 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1510 ALEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDELqgtedAKLRLEVNMQAMKA 1589
Cdd:TIGR00618 182 ALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH-----AYLTQKREAQEEQL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1590 QFERDLQTRDEQnEEKKRALVKQVRELEAELEDERKQRAMAVAIKKKLEMDMKDFE--SQIEAANKGREDAIKQLRKLQA 1667
Cdd:TIGR00618 257 KKQQLLKQLRAR-IEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRihTELQSKMRSRAKLLMKRAAHVK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1668 QTKDY--QRELEEARASRDDIFAQSKENEK-------KLKGLEAEILQLQEELAASERSRRHAEQERDELADEISNStsg 1738
Cdd:TIGR00618 336 QQSSIeeQRRLLQTLHSQEIHIRDAHEVATsireiscQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATI--- 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1739 kSALLDEKRRLEARIAHLEEELEEEQSNMELLnDRFRKTTLQVDTLnsELAAERSSGQKSENARQQLerQNKELKAKLQE 1818
Cdd:TIGR00618 413 -DTRTSAFRDLQGQLAHAKKQQELQQRYAELC-AAAITCTAQCEKL--EKIHLQESAQSLKEREQQL--QTKEQIHLQET 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1819 LEGSVKSKFKATIATLESKIAQLEEQLEQEAKERVASNKLVRRT----------EKKLKEVFMQVEDERRHADQYKEQME 1888
Cdd:TIGR00618 487 RKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMqrgeqtyaqlETSEEDVYHQLTSERKQRASLKEQMQ 566
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 148223878 1889 KANTRMKQLKRQleeaeeeATRANASARKLQRELDDATEANEVLSREVSTLKNRLRR 1945
Cdd:TIGR00618 567 EIQQSFSILTQC-------DNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHA 616
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
922-1279 |
3.93e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.35 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 922 AEEMRARLAIKKQEMEEILRDLEIRMEEEEERNQVLQNEKKKMQTHVQDLEEQLdeeeaaQKLQLEKVTAEAKIKKMEED 1001
Cdd:pfam07888 29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRV------AELKEELRQSREKHEELEEK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1002 ILVLEDQNSKFLKEKKLLEERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKKEEKTRQELEKAKRKLDGETTD 1081
Cdd:pfam07888 103 YKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1082 FQDQIAELQAQIEELKLQLAKKEEELQAALARGDEEVLQKNNTLKLVRELQAQIAELQEDLESEKASRNKAEKQKRDLSE 1161
Cdd:pfam07888 183 TEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1162 ---------------ELEALKTELEdTLDTTAAQQELRTKREQEVAELRKSIEEETRNHEAQIQEMRQRQATALEELSEQ 1226
Cdd:pfam07888 263 maaqrdrtqaelhqaRLQAAQLTLQ-LADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMER 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 148223878 1227 leqaKRFKVNLEKNKQSLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQEL 1279
Cdd:pfam07888 342 ----EKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1600-1752 |
4.30e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 46.74 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1600 EQNEEKKRALVKQVRELEAELEDERKQRAMAVAIKKKLEMDMKDFESQIE--------AANKGRED----AIKQLRKLQA 1667
Cdd:COG1842 19 DKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEkweekarlALEKGREDlareALERKAELEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1668 QTKDYQRELEEARASRDDIFAQSKENEKKLKGLEAEilqlQEELAASERSRRHAEQERDELADEISNSTSGKSALLDEK- 1746
Cdd:COG1842 99 QAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK----KDTLKARAKAAKAQEKVNEALSGIDSDDATSALERMEEKi 174
|
....*.
gi 148223878 1747 RRLEAR 1752
Cdd:COG1842 175 EEMEAR 180
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1065-1836 |
5.15e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 48.21 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1065 RQELEKAKRKLDGETTDFQDQIAELQA-QIEELKlqlaKKEEELQaalargdeevLQKNNTLKLVRELQAQIAELQEDLE 1143
Cdd:pfam07111 43 GQGPGRRGRSLELEGSQALSQQAELISrQLQELR----RLEEEVR----------LLRETSLQQKMRLEAQAMELDALAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1144 SEKASRNKAEKQKRDLSEElEALKTELEDtldttAAQQELrtkreqevaelrksiEEETRNHEAQIQEMRQRQATALEEL 1223
Cdd:pfam07111 109 AEKAGQAEAEGLRAALAGA-EMVRKNLEE-----GSQREL---------------EEIQRLHQEQLSSLTQAHEEALSSL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1224 SEQLEqakrfkvNLEKNKQSLESDNkelATEVKSLQQMKAESEYKRKKLEGQVQELHAKVLEGDRLRADMVEkssklQNE 1303
Cdd:pfam07111 168 TSKAE-------GLEKSLNSLETKR---AGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKYVGE-----QVP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1304 LENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQeetrQKLNQSSRIRQLEEEKnnlqeqQEEEEEARKSLEKQIL- 1382
Cdd:pfam07111 233 PEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQ----VRVQSLTHMLALQEEE------LTRKIQPSDSLEPEFPk 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1383 SLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTknrLQQELDDLMVDLDHQRQIVSNLe 1462
Cdd:pfam07111 303 KCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAI---LQRALQDKAAEVEVERMSAKGL- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1463 kkQKKFDQllaeeknisARHAEERDRAEADAREKETKALSLARAldealEAQDEFERLNKQLRAEMEDLMSSKDDVGKNV 1542
Cdd:pfam07111 379 --QMELSR---------AQEARRRQQQQTASAEEQLKFVVNAMS-----STQIWLETTMTRVEQAVARIPSLSNRLSYAV 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1543 HELEKSKRALDQQVEEMRTQLE-------------ELEDELQGTEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRAL 1609
Cdd:pfam07111 443 RKVHTIKGLMARKVALAQLRQEscpppppappvdaDLSLELEQLREERNRLDAELQLSAHLIQQEVGRAREQGEAERQQL 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1610 VKQVRELEAELEdeRKQRAMAvaikkklemdmkDFESQIEAANKGREDAIKQLRKLQAQTKDYQreleearasrdDIFAQ 1689
Cdd:pfam07111 523 SEVAQQLEQELQ--RAQESLA------------SVGQQLEVARQGQQESTEEAASLRQELTQQQ-----------EIYGQ 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1690 SkenekklkgleaeilqLQEELAASErsrrhaeqerdeladeisnsTSGKSALLDEKRRL-EARIAHLEEELEEEQSNME 1768
Cdd:pfam07111 578 A----------------LQEKVAEVE--------------------TRLREQLSDTKRRLnEARREQAKAVVSLRQIQHR 621
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148223878 1769 LLNDRFRKTTLQvdTLNSElaAERSSGQKSENARQQLERQNKELKAKLQELEGSVKSKFKATIATLES 1836
Cdd:pfam07111 622 ATQEKERNQELR--RLQDE--ARKEEGQRLARRVQELERDKNLMLATLQQEGLLSRYKQQRLLAVLPS 685
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1409-1943 |
5.22e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.43 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1409 KKKLLKDTEGLGQ-------RLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKnisar 1481
Cdd:TIGR00618 165 KKELLMNLFPLDQytqlalmEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQ----- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1482 haeerdraeadareketKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKSKRAL-----DQQV 1556
Cdd:TIGR00618 240 -----------------QSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAplaahIKAV 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1557 EEMRTQLEELEDELQGTEDAKLRLEVNMQAMKAQferdlqtrdEQNEEKKRALVKQVRELEAELEDERKQRAMAVAIKKK 1636
Cdd:TIGR00618 303 TQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ---------QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQ 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1637 ---LEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDIFAQSKENEKKLKGLEAEILQLQEELAA 1713
Cdd:TIGR00618 374 qhtLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQC 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1714 SERSRRHAEQERDELADEISNSTSGKSALLDEKRRLEARIAhleeELEEEQSNMELLNDRFRKTTLQVdTLNSELAAERS 1793
Cdd:TIGR00618 454 EKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLA----RLLELQEEPCPLCGSCIHPNPAR-QDIDNPGPLTR 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1794 SGQKSENARQQLERQNKELKAKLQELEGSVKSkFKATIaTLESKIAQLEEQLEQEAKERVasNKLVRRTEKKLKEVFMQV 1873
Cdd:TIGR00618 529 RMQRGEQTYAQLETSEEDVYHQLTSERKQRAS-LKEQM-QEIQQSFSILTQCDNRSKEDI--PNLQNITVRLQDLTEKLS 604
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1874 EDERRHADQYKEQMEKANTRMKQLKRQLEEAEEEATRANASARKLQRELDDATEANEVLSREVSTLKNRL 1943
Cdd:TIGR00618 605 EAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKEL 674
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1406-1942 |
5.44e-05 |
|
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: 48.18 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1406 EEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQIVS-----------NLEKKQKKFDQLLAE 1474
Cdd:pfam05483 63 EGLKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEaqrkaiqelqfENEKVSLKLEEEIQE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1475 EKNI-----------------SARHAEERDRAEADAREKETKALSLARALDEALEAQDEFERLNKQLRAEMEdlMSSKDD 1537
Cdd:pfam05483 143 NKDLikennatrhlcnllketCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMH--FKLKED 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1538 VGKNVHELEKSKRALDQQVEEMRTQLEELEDELQGTEDAKLRLEVNMQAMKaqferDLQTRDEQNEEKKRALVKQVRELE 1617
Cdd:pfam05483 221 HEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKAN-----QLEEKTKLQDENLKELIEKKDHLT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1618 AELEDERKQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDIFAQSKE----N 1693
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQrlekN 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1694 EKKLKGLEAEILQLQEELAASERSRRHAEQERDELADEISNstsgKSALLDEKRRLEaRIAhlEEELEEEQSNMELLNDR 1773
Cdd:pfam05483 376 EDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE----DEKLLDEKKQFE-KIA--EELKGKEQELIFLLQAR 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1774 FRKTTLQVDTLNSELAAERSSGQKSENARQQLERQ---NKELKAKLQELEGSVKSKFK-ATIATLESKIAQLEEQLEQEA 1849
Cdd:pfam05483 449 EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEklkNIELTAHCDKLLLENKELTQeASDMTLELKKHQEDIINCKKQ 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1850 KERVASN-KLVRRTEKKLKEVFMQVEDE-RRHADQYKEQMEKANTRMKQLKRQLEEAEEEATRANASARKLQRELDDATE 1927
Cdd:pfam05483 529 EERMLKQiENLEEKEMNLRDELESVREEfIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNK 608
|
570
....*....|....*
gi 148223878 1928 ANEVLSREVSTLKNR 1942
Cdd:pfam05483 609 NIEELHQENKALKKK 623
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1600-1723 |
5.80e-05 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 46.21 E-value: 5.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1600 EQNEEKKRALVKQVRELEAELEDERKQRAMAVAIKKKLEM-------DMKDFESQIEAA-NKGRED----AIKQLRKLQA 1667
Cdd:pfam04012 18 DKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERrleqqteQAKKLEEKAQAAlTKGNEElareALAEKKSLEK 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 148223878 1668 QTKDYQRELEEARASRDDIFAQSKENEKKLKGLEAEilqlQEELAASERSRRHAEQ 1723
Cdd:pfam04012 98 QAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAK----KNLLKARLKAAKAQEA 149
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
867-1150 |
6.28e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 867 EEELVAKDEELLKVKEKQSKVEGELVDMEQKHQQLVEEKNILAEQLhaetelfaeaEEMRARLAIKKQEMEEILRDLEIR 946
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL----------EALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 947 MEEEEERNQVLQNEKKKMQThvqdleeqldeeeaaqklqlekvtaeakikkmeEDILVLEDQNSKFLKEKKLLEeRIAES 1026
Cdd:COG3883 85 REELGERARALYRSGGSVSY---------------------------------LDVLLGSESFSDFLDRLSALS-KIADA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1027 TSQLAEEEEKAKnlAKLKNKQemmiSDLEERLKKEEKTRQELEKAKRKLDGETTDFQDQIAELQAQIEELKLQLAKKEEE 1106
Cdd:COG3883 131 DADLLEELKADK--AELEAKK----AELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 148223878 1107 LQAALARGDEEVLQKNNTLKLVRELQAQIAELQEDLESEKASRN 1150
Cdd:COG3883 205 LAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1001-1151 |
6.42e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 47.27 E-value: 6.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1001 DILVLEDQNskflkeKKLLEERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLkkeektrQELEKAKRKLDGETT 1080
Cdd:PRK09039 67 DLLSLERQG------NQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRA-------GELAQELDSEKQVSA 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148223878 1081 DFQDQIAELQAQIEELKLQLAKKEEELQAALARGdeevlqknntlklvRELQAQIAELQEDLESEKASRNK 1151
Cdd:PRK09039 134 RALAQVELLNQQIAALRRQLAALEAALDASEKRD--------------RESQAKIADLGRRLNVALAQRVQ 190
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
991-1137 |
6.62e-05 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic 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: 463796 [Multi-domain] Cd Length: 712 Bit Score: 48.13 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 991 AEAKIKKM--EEDILVLEDQNSKFLKEKKLLEERIA---ESTSQLAEEEEKAKNL--AKLKNKQEMMISDLEERLKKEEK 1063
Cdd:pfam13166 344 LEAKRKDPfkSIELDSVDAKIESINDLVASINELIAkhnEITDNFEEEKNKAKKKlrLHLVEEFKSEIDEYKDKYAGLEK 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148223878 1064 TRQELEKAKRKLDGETTDFQDQIAELQAQIEELKLQLAKKEEELQAALARGDE-EVLQKNNTLKLVRELQAQIAE 1137
Cdd:pfam13166 424 AINSLEKEIKNLEAEIKKLREEIKELEAQLRDHKPGADEINKLLKAFGFGELElSFNEEGKGYRIIRKGGSQAAE 498
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1512-1822 |
6.68e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.20 E-value: 6.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1512 EAQDEFERLNKQ-LRAEMEDLMSSKDDVGKnVHELEKSKRA-LDQQV----EEMRTQLE-ELEDELQGTEDAKLRLEVNM 1584
Cdd:pfam17380 288 QQQEKFEKMEQErLRQEKEEKAREVERRRK-LEEAEKARQAeMDRQAaiyaEQERMAMErERELERIRQEERKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1585 Q---AMKAQFERDLQtRDEQNEEKKRALVKQvreleaELEDERKQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIKQ 1661
Cdd:pfam17380 367 QeeiAMEISRMRELE-RLQMERQQKNERVRQ------ELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1662 LRKLQAQTKDYQRELEEARASRDDIFAQsKENEKKLKGLEAEILQLQEELAASERsRRHAEQERDEladeisnstsGKSA 1741
Cdd:pfam17380 440 LEEERAREMERVRLEEQERQQQVERLRQ-QEEERKRKKLELEKEKRDRKRAEEQR-RKILEKELEE----------RKQA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1742 LLDEKRR---LEARIAHLEEELEEEQSNMELLNDRFRKTTL----QVDTLNSELAAERSSGQKSENARQQLeRQNKELKA 1814
Cdd:pfam17380 508 MIEEERKrklLEKEMEERQKAIYEEERRREAEEERRKQQEMeerrRIQEQMRKATEERSRLEAMEREREMM-RQIVESEK 586
|
....*...
gi 148223878 1815 KLQELEGS 1822
Cdd:pfam17380 587 ARAEYEAT 594
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1542-1714 |
6.70e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 6.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1542 VHELEKSKRALDQQVEEMRTQLEELEDELQGTEDAKLRLEVNMQAMKAQferdlQTRDEQNEEKKRALVKQVRELEAELE 1621
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKE-----IKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1622 DERKQRAMAVAIkKKLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDIFAQSKENEKKL---- 1697
Cdd:COG1579 87 NNKEYEALQKEI-ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELeaer 165
|
170 180
....*....|....*....|.
gi 148223878 1698 ----KGLEAEILQLQEELAAS 1714
Cdd:COG1579 166 eelaAKIPPELLALYERIRKR 186
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
861-1107 |
6.91e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.81 E-value: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 861 LQVTRQEEelvaKDEELLKVKEKQSKVEGELVDMEQKHQQLVEEKNILAEQ-LHAETELFAEAEEMRARLAIKKQEMEEI 939
Cdd:pfam17380 350 LERIRQEE----RKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQeLEAARKVKILEEERQRKIQQQKVEMEQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 940 LRDLEirmEEEEERNQVLQNEKKKMQTHVQDLEEQLDEeeaaQKLQLEKVTAEAKIKKMEEDilvLEDQNSKFLKE--KK 1017
Cdd:pfam17380 426 RAEQE---EARQREVRRLEEERAREMERVRLEEQERQQ----QVERLRQQEEERKRKKLELE---KEKRDRKRAEEqrRK 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1018 LLEERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKKEEKTRQELEKAKRKldgettDFQDQIaeLQAQIEELK 1097
Cdd:pfam17380 496 ILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR------RIQEQM--RKATEERSR 567
|
250
....*....|
gi 148223878 1098 LQLAKKEEEL 1107
Cdd:pfam17380 568 LEAMEREREM 577
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1432-1901 |
7.67e-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: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.81 E-value: 7.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1432 KLEKTKNRLQQELDDLM-VDLDHQRQIVsNLEKKQKKFDQLLAEE--KNIS-ARHAEERDRAEADAREKETKALSLARAL 1507
Cdd:pfam05557 3 ELIESKARLSQLQNEKKqMELEHKRARI-ELEKKASALKRQLDREsdRNQElQKRIRLLEKREAEAEEALREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1508 DEALEAQDEFERLNKQLRAEMEDLMSS-KDDVGKNVHELEKSKRALDQQ---VEEMRTQLEELEDELQGTEDAKLRLEVN 1583
Cdd:pfam05557 82 KKYLEALNKKLNEKESQLADAREVISClKNELSELRRQIQRAELELQSTnseLEELQERLDLLKAKASEAEQLRQNLEKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1584 MQAMKAQ--------FERDLQTRDEQNEEKKRALVKQVRELEAELEDERKQRAMAVAIKKK---LEMDMKDFESQIEAAN 1652
Cdd:pfam05557 162 QSSLAEAeqrikeleFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENkllLKEEVEDLKRKLEREE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1653 KGREDAIKqlrkLQAQTKDYQRELEEARasrdDIFAQSKENEKKLKGLEAEILQLQ-------EELAASERSRRHAEQER 1725
Cdd:pfam05557 242 KYREEAAT----LELEKEKLEQELQSWV----KLAQDTGLNLRSPEDLSRRIEQLQqreivlkEENSSLTSSARQLEKAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1726 DELADEISNStsgKSALLDEKRRLEariaHLEEELEEEQSNMELLNDRFRKTTLQVDTLNSELAAERSSGQKSENAR--- 1802
Cdd:pfam05557 314 RELEQELAQY---LKKIEDLNKKLK----RHKALVRRLQRRVLLLTKERDGYRAILESYDKELTMSNYSPQLLERIEeae 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1803 ---QQLERQNKELKAKLQELEGSVKSkFKATIATLESKIAQLEEQleQEAKERVASNKLVRRTEKKLKEVFMQVEDERR- 1878
Cdd:pfam05557 387 dmtQKMQAHNEEMEAQLSVAEEELGG-YKQQAQTLERELQALRQQ--ESLADPSYSKEEVDSLRRKLETLELERQRLREq 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 148223878 1879 ----------------------------------HADQYKEQMEKANTRMKQLKRQL 1901
Cdd:pfam05557 464 knelemelerrclqgdydpkktkvlhlsmnpaaeAYQQRKNQLEKLQAEIERLKRLL 520
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
862-1202 |
1.21e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.81 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 862 QVTRQEEELVAKDEELLKVKEKQSKVEGELVDMEQKHQQLVEEKNILAEQLHAETELFAEAEEMRARLAIKKQEMEEILR 941
Cdd:pfam07888 74 QRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 942 DLEIRMEEEEERNQVLQNEKKKMQThvqdleEQLDEEEAAQKLQLEKVTAEAKIKKMEEDILVLEDQNSKFLKEKKLLEE 1021
Cdd:pfam07888 154 RMKERAKKAGAQRKEEEAERKQLQA------KLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1022 RIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKKEEKTRQELEKAKRkldgETTDFQDQIAELQAQIEELKLQLA 1101
Cdd:pfam07888 228 KEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARL----QAAQLTLQLADASLALREGRARWA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1102 KKEEELQAAlARGDEEVLQKnntlklvreLQAQIAELQEDLESEKASRNKAE---KQKRD-----LSEELEALkTELEDT 1173
Cdd:pfam07888 304 QERETLQQS-AEADKDRIEK---------LSAELQRLEERLQEERMEREKLEvelGREKDcnrvqLSESRREL-QELKAS 372
|
330 340
....*....|....*....|....*....
gi 148223878 1174 LDTTAAQQELRTKREQEVAELRKSIEEET 1202
Cdd:pfam07888 373 LRVAQKEKEQLQAEKQELLEYIRQLEQRL 401
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1500-1738 |
1.30e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1500 ALSLARALDEALEAQDEFERLNK---QLRAEMEDLMSSKDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDELqgtEDA 1576
Cdd:COG3883 1 ALALALAAPTPAFADPQIQAKQKelsELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI---AEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1577 KLRLEVNMQAMKAQFeRDLQTRDEQNEE--------------KKRALVKQVRELEAELEDERKQRamavaiKKKLEMDMK 1642
Cdd:COG3883 78 EAEIEERREELGERA-RALYRSGGSVSYldvllgsesfsdflDRLSALSKIADADADLLEELKAD------KAELEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1643 DFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDIFAQSKENEKKLKGLEAEILQLQEELAASERSRRHAE 1722
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
250
....*....|....*.
gi 148223878 1723 QERDELADEISNSTSG 1738
Cdd:COG3883 231 AAAAAAAAAAAAAASA 246
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1075-1677 |
1.32e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.20 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1075 LDGETTDFQDQIAELQAQIEELKLQLA---KKEEELQAALARGDEEVLQKNNTLKLVRELQAQIAELQEDLESEKASRNK 1151
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSitlKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1152 AEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELRKSIEeetrNHEAQIQ--EMRQRQATALEELSEQLEQ 1229
Cdd:PRK01156 268 ELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILS----NIDAEINkyHAIIKKLSVLQKDYNDYIK 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1230 AKRFKVNLEKNKQSLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELhAKVLEGDRLRADMVEKssklqnELENVSS 1309
Cdd:PRK01156 344 KKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFI-SEILKIQEIDPDAIKK------ELNEINV 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1310 LLEEAEKKGIKLAKDVASMESQLQDTQELLQEETRQKL----------NQSSRIRQ-LEEEKNNLQEQQEEEEEARKSLE 1378
Cdd:PRK01156 417 KLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgttlgeEKSNHIINhYNEKKSRLEEKIREIEIEVKDID 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1379 KQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQElddlmvdldhqrqiv 1458
Cdd:PRK01156 497 EKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLE--------------- 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1459 sNLEKKQKKFDQLLAEEKNISArhaeerdraEADAREKETKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDDV 1538
Cdd:PRK01156 562 -DLDSKRTSWLNALAVISLIDI---------ETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNL 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1539 GKNVHELEKSKRaldqQVEEMRTQLEELEDELQGTEDAKLRL-EVNMQAMkaQFERDLQTRDEQ------NEEKKRALVK 1611
Cdd:PRK01156 632 NNKYNEIQENKI----LIEKLRGKIDNYKKQIAEIDSIIPDLkEITSRIN--DIEDNLKKSRKAlddakaNRARLESTIE 705
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148223878 1612 QVRELEAELEDERKQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIkqLRK-----LQAQTKDYQRELE 1677
Cdd:PRK01156 706 ILRTRINELSDRINDINETLESMKKIKKAIGDLKRLREAFDKSGVPAM--IRKsasqaMTSLTRKYLFEFN 774
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1547-1919 |
1.48e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 46.93 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1547 KSKRALDQQVEEMRTQLEELEDELQGTEDAKLRLEvnMQAMKAQFERDLQTRDEQNEEK-----KRALVKQVRELEAELE 1621
Cdd:NF033838 58 EHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKK--LSDIKTEYLYELNVLKEKSEAEltsktKKELDAAFEQFKKDTL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1622 DERKQRAMAvaiKKKLEMDMKDFESQIEAANkgREDAIKQLRKLQAQTKDYQRELEEARASRDDIFAQSKENEKKLKGLE 1701
Cdd:NF033838 136 EPGKKVAEA---TKKVEEAEKKAKDQKEEDR--RNYPTNTYKTLELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQAK 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1702 AEILQLQEELAASER---SRRHAEQERDELADEISNSTSGKSALLDEKRRLEARIAHLEEELEEEQSNMEllND-RFRKT 1777
Cdd:NF033838 211 AKVESKKAEATRLEKiktDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKE--NDaKSSDS 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1778 TLQVDTLNSelaAERSSGQKSENARQQLERQNKELKAKLQELEGSVKSKfkaTIATLESKIAQLEEQLEQEAKERVASNK 1857
Cdd:NF033838 289 SVGEETLPS---PSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRRNYPTN---TYKTLELEIAESDVKVKEAELELVKEEA 362
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148223878 1858 LVRRTEKKLKEVFMQVEDERRHAdqykeqmekanTRMKQLKRQLEEAEEEATRANASARKLQ 1919
Cdd:NF033838 363 KEPRNEEKIKQAKAKVESKKAEA-----------TRLEKIKTDRKKAEEEAKRKAAEEDKVK 413
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
1471-1678 |
1.51e-04 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 46.90 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1471 LLAEEKNISArhAEERDRaeaDAREketkalslarALDEALE---AQDEFERLNKQLRAEMEDLMSSKDDVGKnvHELEK 1547
Cdd:pfam13779 477 LRIEDGDLSD--AERRLR---AAQE----------RLSEALErgaSDEEIAKLMQELREALDDYMQALAEQAQ--QNPQD 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1548 SKRALDQQVEEMRTQ-LEELEDELQ-----GTEDAKLRLEVNMQAM-----KAQFERDLQTRDEQNEEKKRALVKQVREl 1616
Cdd:pfam13779 540 LQQPDDPNAQEMTQQdLQRMLDRIEelarsGRRAEAQQMLSQLQQMlenlqAGQPQQQQQQGQSEMQQAMDELGDLLRE- 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148223878 1617 EAELEDErKQRAMAVAIKKKLEMD----------MKDFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEE 1678
Cdd:pfam13779 619 QQQLLDE-TFRQLQQQGGQQQGQPgqqgqqgqgqQPGQGGQQPGAQMPPQGGAEALGDLAERQQALRRRLEE 689
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
985-1242 |
1.64e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.61 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 985 QLEKVTAE-AKIKKMEEDILVLEDQNSKFLKEKKLLEERIAESTS---QLAEEEEKAKNLAKLKNKQEMM--ISDLEERL 1058
Cdd:COG0497 156 LLEEYREAyRAWRALKKELEELRADEAERARELDLLRFQLEELEAaalQPGEEEELEEERRRLSNAEKLReaLQEALEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1059 KKEE--------KTRQELEKAKRkLDGETTDFQDQIAELQAQIEELKLQLAKKEEELQAalargDEEVLQknntlklvrE 1130
Cdd:COG0497 236 SGGEggaldllgQALRALERLAE-YDPSLAELAERLESALIELEEAASELRRYLDSLEF-----DPERLE---------E 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1131 LQAQIAELQedleseKASRnkaeKQKRDLsEELEALKTELEDTLDTTAAQQELRTKREQEVAELRKSIEEETrnheAQIQ 1210
Cdd:COG0497 301 VEERLALLR------RLAR----KYGVTV-EELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAA----EKLS 365
|
250 260 270
....*....|....*....|....*....|....*..
gi 148223878 1211 EMRQRQATALEE-LSEQLEQAK----RFKVNLEKNKQ 1242
Cdd:COG0497 366 AARKKAAKKLEKaVTAELADLGmpnaRFEVEVTPLEE 402
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1093-1278 |
1.67e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.74 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1093 IEELKLQLAKKEEELqaalargdEEVLQKNNTLKlvRELQAQIAELQEDLEsekasrnKAEKQKRDLSEELEALKTELED 1172
Cdd:PRK00409 504 IEEAKKLIGEDKEKL--------NELIASLEELE--RELEQKAEEAEALLK-------EAEKLKEELEEKKEKLQEEEDK 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1173 TLdttaaqQELRTKREQEVAELRKSIEEETRN-HEAQIQEMRQRQATALEELSEQLEQAKRfKVNLEKNKQSLESDNKEL 1251
Cdd:PRK00409 567 LL------EEAEKEAQQAIKEAKKEADEIIKElRQLQKGGYASVKAHELIEARKRLNKANE-KKEKKKKKQKEKQEELKV 639
|
170 180
....*....|....*....|....*....
gi 148223878 1252 ATEVK--SLQQmKAESEYKRKKLEGQVQE 1278
Cdd:PRK00409 640 GDEVKylSLGQ-KGEVLSIPDDKEAIVQA 667
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
877-1270 |
1.69e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 46.39 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 877 LLKVKEKQSKVEGELVDMEQKHQQLVEEKNILAEQlhaetelfaeaeEMRARLAIkkQEMEEILRDLeirmeeeeeRNQV 956
Cdd:pfam06160 81 FKKAKKALDEIEELLDDIEEDIKQILEELDELLES------------EEKNREEV--EELKDKYREL---------RKTL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 957 LQNEKKKMQThvqdleeqldeeeaaqklqLEKVtaEAKIKKMEEDILVLEDQNSK--FLKEKKLLEErIAESTSQLAEEE 1034
Cdd:pfam06160 138 LANRFSYGPA-------------------IDEL--EKQLAEIEEEFSQFEELTESgdYLEAREVLEK-LEEETDALEELM 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1035 EKAKNL-AKLKNkqemmisDLEERLKKEEKTRQELEKAKRKLdgETTDFQDQIAELQAQIEELKLQLAKkeeelqaalar 1113
Cdd:pfam06160 196 EDIPPLyEELKT-------ELPDQLEELKEGYREMEEEGYAL--EHLNVDKEIQQLEEQLEENLALLEN----------- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1114 gdeevLQKNNTLKLVRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAE 1193
Cdd:pfam06160 256 -----LELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYTLNENELER 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1194 LR------KSIEEETRNHEAQIQEMRQRQATALEELSEQLEQAKRFKVNLEKNKQSLESDNKELATEVKSLQQMKAE-SE 1266
Cdd:pfam06160 331 VRglekqlEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLElRE 410
|
....
gi 148223878 1267 YKRK 1270
Cdd:pfam06160 411 IKRL 414
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1012-1204 |
1.91e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 46.24 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1012 FLKEKKLLEERiAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKKEEKTRQELEKAKRKLDGETtdfqDQIAELQA 1091
Cdd:PRK12705 24 LLKKRQRLAKE-AERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKE----EQLDARAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1092 QIEELKLQLAKKEEELQAALARGDEEVLQKNNTLKLVRELQAQ------IAELQEDLESEKASRNKAEKQKRDLSEELEA 1165
Cdd:PRK12705 99 KLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEqarkllLKLLDAELEEEKAQRVKKIEEEADLEAERKA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 148223878 1166 ---LKTELEDTLDTTAAQQELRTKREQEVAELRKSIEEETRN 1204
Cdd:PRK12705 179 qniLAQAMQRIASETASDLSVSVVPIPSDAMKGRIIGREGRN 220
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1087-1229 |
2.03e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.73 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1087 AELQAQIEELKLQLAKKEEE---LQAALARGDEEVlqknntlklvRELQAQIAELQEDLESEKASRNKAEKQKRDLSEEL 1163
Cdd:PRK09039 77 QDLQDSVANLRASLSAAEAErsrLQALLAELAGAG----------AAAEGRAGELAQELDSEKQVSARALAQVELLNQQI 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148223878 1164 EALKTELedtldttAAQQELrtkreqevaeLRKSiEEETRNHEAQIQEMRQRQATALEELSEQLEQ 1229
Cdd:PRK09039 147 AALRRQL-------AALEAA----------LDAS-EKRDRESQAKIADLGRRLNVALAQRVQELNR 194
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1089-1241 |
2.12e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.39 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1089 LQAQIEELKLQLAKKEEELQAALARGDEEVLQKNNtlKLVRELQAQIAELQEdlesekasrnkaekQKRDLSEELEALKT 1168
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEERELTEEE--EEIRRLEEQVERLEA--------------EVEELEAELEEKDE 441
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148223878 1169 ELEDtldttaAQQELRTKREQEVAELRKSIE-----EETRNHEAQIQEMRQRqataLEELSEQLEQAKRFKVNLEKNK 1241
Cdd:COG2433 442 RIER------LERELSEARSEERREIRKDREisrldREIERLERELEEERER----IEELKRKLERLKELWKLEHSGE 509
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1015-1214 |
2.43e-04 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic 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: 463796 [Multi-domain] Cd Length: 712 Bit Score: 46.21 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1015 EKKLLEERIAESTSQLAEE-EEKAKNLAKLKNKQEMMISDLEERLKK---EEKTRQELEKAKRKLDGETTDFQDQIAELQ 1090
Cdd:pfam13166 262 GQPLPAERKAALEAHFDDEfTEFQNRLQKLIEKVESAISSLLAQLPAvsdLASLLSAFELDVEDIESEAEVLNSQLDGLR 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1091 AQIEELKLQLAK--KEEELQAALARGDEEVLQKNNTLKL----VRELQAQIAELQEDLESEKASRNKAEKQKrdLSEELE 1164
Cdd:pfam13166 342 RALEAKRKDPFKsiELDSVDAKIESINDLVASINELIAKhneiTDNFEEEKNKAKKKLRLHLVEEFKSEIDE--YKDKYA 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 148223878 1165 ALKTELEDTLDTTAAQQELRTKREQEVAELRKSIeeetRNHEAQIQEMRQ 1214
Cdd:pfam13166 420 GLEKAINSLEKEIKNLEAEIKKLREEIKELEAQL----RDHKPGADEINK 465
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
953-1260 |
2.45e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 45.57 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 953 RNQVLQNEKKKMQTHVQDLEEQLDEEEAAQKLQLEKVTAEAKIKKMEEDILVLEDQNSKFLKEKKLLEERIAESTSQLAE 1032
Cdd:pfam15905 54 RKVKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1033 EEeKAKNLAKLK-----NKQEMMISDLEERlkkeeKTRQELEKAKRKLDGETTDFQDQIAELQAQIEELKLQLAKKEEEL 1107
Cdd:pfam15905 134 LT-RVNELLKAKfsedgTQKKMSSLSMELM-----KLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1108 qaaLARGDEEVLQKNNTLKLVRElqaqIAELQedlesekasrnkaekqkrDLSEELEALKTELedtldttAAQQELRTKR 1187
Cdd:pfam15905 208 ---VSTEKEKIEEKSETEKLLEY----ITELS------------------CVSEQVEKYKLDI-------AQLEELLKEK 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148223878 1188 EQEVAELRKSIEEETRNHEAQIQEMRQRQATALEELSEQLEQAKRFKVNLEKNKQSLESDNKELATEVKSLQQ 1260
Cdd:pfam15905 256 NDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1086-1363 |
2.76e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 46.00 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1086 IAELQAQIEELKLQLAKKEEELQAALARGDEEVLQKnntlkLVRELQAQIAE------LQEDLESEKASRNKAEKQK--- 1156
Cdd:PLN03229 431 VRELEGEVEKLKEQILKAKESSSKPSELALNEMIEK-----LKKEIDLEYTEaviamgLQERLENLREEFSKANSQDqlm 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1157 -RDLSEELEALKTELEDTLDTTAAQQELRTKREQ-EVAELRKSIEEETRNHEAQIQEMRQRQATALEElSEQLEQAKRFK 1234
Cdd:PLN03229 506 hPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDMlNEFSRAKALSEKKSKAEKLKAEINKKFKEVMDR-PEIKEKMEALK 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1235 VNLEKNKQS----LESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELHAKVLEGDRLRADMVEKSSKLQNE------- 1303
Cdd:PLN03229 585 AEVASSGASsgdeLDDDLKEKVEKMKKEIELELAGVLKSMGLEVIGVTKKNKDTAEQTPPPNLQEKIESLNEEinkkier 664
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1304 LENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQEETRQKLNQSSRIRQLEEEKNNL 1363
Cdd:PLN03229 665 VIRSSDLKSKIELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEALNSSELKEKFEEL 724
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
866-1337 |
2.76e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.26 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 866 QEEELVAKDEELLKVKEKQSKVEG--ELVDMEQKHQQLVEEKNILAEQLHAETElfaEAEEMRARLAIKKQEMEEILRDL 943
Cdd:pfam15921 621 RELEARVSDLELEKVKLVNAGSERlrAVKDIKQERDQLLNEVKTSRNELNSLSE---DYEVLKRNFRNKSEEMETTTNKL 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 944 EIRMEEEEERNQVLQNEKKKMQThvqdleEQLDEEEAAQKLQLEKVTAEAKIKKMEEDILVLEDQNSKFLKEKKLLEEri 1023
Cdd:pfam15921 698 KMQLKSAQSELEQTRNTLKSMEG------SDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKE-- 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1024 aestsqlaEEEEKAKNLAKLKNKQEMMISDLEERLKKEEKTRQELEKAKRKLDGETTDF---QDQIAELQAQIEELKLQL 1100
Cdd:pfam15921 770 --------EKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFaecQDIIQRQEQESVRLKLQH 841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1101 AKKEEELQ-----------------AALARGDEEVLQKNNTLKLVRELQAQIAELQED--------LESEKASRNKAEKQ 1155
Cdd:pfam15921 842 TLDVKELQgpgytsnssmkprllqpASFTRTHSNVPSSQSTASFLSHHSRKTNALKEDptrdlkqlLQELRSVINEEPTV 921
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1156 KRDLSEELEALKT--ELEDTLDTTAAQQELRTKREQEVAELRKSieEETRNHEAQIQEMRQRQATALEELSEQLEQAKRF 1233
Cdd:pfam15921 922 QLSKAEDKGRAPSlgALDDRVRDCIIESSLRSDICHSSSNSLQT--EGSKSSETCSREPVLLHAGELEDPSSCFTFPSTA 999
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1234 KVNLeKNKQSLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELHA--KVLEGDRLRADMVEKS-SKLQNELENVSSL 1310
Cdd:pfam15921 1000 SPSV-KNSASRSFHSSPKKSPVHSLLTSSAEGSIGSSSQYRSAKTIHSpdSVKDSQSLPIETTGKTcRKLQNRLESLQTL 1078
|
490 500
....*....|....*....|....*..
gi 148223878 1311 LEEAEKKGIKLAKDVASMESQLQDTQE 1337
Cdd:pfam15921 1079 VEDLQLKNQAMSSMIRNQEKRIQKVKD 1105
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1651-1734 |
2.92e-04 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 45.44 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1651 ANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDI---FAQSKENEKKLKGLEAEILQLQEELAASERSRRHAEQERDE 1727
Cdd:PRK05431 19 AKRGFPLDVDELLELDEERRELQTELEELQAERNALskeIGQAKRKGEDAEALIAEVKELKEEIKALEAELDELEAELEE 98
|
....*..
gi 148223878 1728 LADEISN 1734
Cdd:PRK05431 99 LLLRIPN 105
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1120-1415 |
3.02e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.69 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1120 QKNNTLKLVRELQA-QIAELQEDLESEKASrnKAEKQKRDLSEELEALKTELEDTldtTAAQQELRTKREQEVAELRKSI 1198
Cdd:PRK05771 17 YKDEVLEALHELGVvHIEDLKEELSNERLR--KLRSLLTKLSEALDKLRSYLPKL---NPLREEKKKVSVKSLEELIKDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1199 EEEtrnheaqiqemrqrqataLEELSEQLEqakrfkvnleknkqSLESDNKELATEVKSLQQMKAESEYkRKKLEGQVQE 1278
Cdd:PRK05771 92 EEE------------------LEKIEKEIK--------------ELEEEISELENEIKELEQEIERLEP-WGNFDLDLSL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1279 LhakvLEGDRLRADMVEKSSKLQNELENVSS---LLEEAEKKG------IKLAKDVASMESQLQDTqELLQEETRQKLNQ 1349
Cdd:PRK05771 139 L----LGFKYVSVFVGTVPEDKLEELKLESDvenVEYISTDKGyvyvvvVVLKELSDEVEEELKKL-GFERLELEEEGTP 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148223878 1350 SSRIRQLEEEKNNLQEQqeeeeeaRKSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLKD 1415
Cdd:PRK05771 214 SELIREIKEELEEIEKE-------RESLLEELKELAKKYLEELLALYEYLEIELERAEALSKFLKT 272
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1054-1228 |
3.36e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 43.41 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1054 LEERLKKEEKTRQELEK-----AKRKLDGETTDFQDQIAELQAQIEELKLQLAKKEEELQAALARgdeevlqknNTLKLV 1128
Cdd:pfam01442 2 LEDSLDELSTYAEELQEqlgpvAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQ---------NVEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1129 RELQAQIAELQEDLesekasRNKAEKQKRDLSEELEALKTELEDTLDTTAAQ-----QELRTKREQEVAELRKSIEEETR 1203
Cdd:pfam01442 73 QRLEPYTEELRKRL------NADAEELQEKLAPYGEELRERLEQNVDALRARlapyaEELRQKLAERLEELKESLAPYAE 146
|
170 180
....*....|....*....|....*....
gi 148223878 1204 NHEAQ----IQEMRQRQATALEELSEQLE 1228
Cdd:pfam01442 147 EVQAQlsqrLQELREKLEPQAEDLREKLD 175
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1021-1273 |
3.84e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1021 ERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKKEEKTRQELEKAKRKLDGETTDFQDQIAELQAQIEELK--- 1097
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKeer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1098 LQLAKKEEELQAALARGDEEVLQKNNTLKLVRELQAQIAELQEDLESEKASRNKAEK---QKRDLSEELEALKTELEDTL 1174
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKElveKIKELEKELEKAKKALEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1175 DTTAAQQELRTKREQevaelRKSIEEETRNHEAQIQEMRQRQATALEELSEQLEQAKRFKVNLEKNKQSLESDNKELATE 1254
Cdd:COG1340 161 KLKELRAELKELRKE-----AEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIEL 235
|
250
....*....|....*....
gi 148223878 1255 VKSLQQMKAESEYKRKKLE 1273
Cdd:COG1340 236 QKELRELRKELKKLRKKQR 254
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1375-1899 |
4.52e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 45.13 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1375 KSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQELDDLmvdldHQ 1454
Cdd:pfam07111 76 RRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQRELEEIQRL-----HQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1455 RQIVSNLEKKQKKFDQLlaeeknisarhaeerdRAEADAREKETKALSLARA--LDEALEAQDEFERLNKQLRAEMEDLM 1532
Cdd:pfam07111 151 EQLSSLTQAHEEALSSL----------------TSKAEGLEKSLNSLETKRAgeAKQLAEAQKEAELLRKQLSKTQEELE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1533 SS---------------------------KDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDELQGTEDAKLRLEVNMQ 1585
Cdd:pfam07111 215 AQvtlveslrkyvgeqvppevhsqtweleRQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSD 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1586 AMKAQFERDLQTRDEQNEEKKRALVKQVRELEAELEDERKQRAMAVAIKKKLEMDmkdfESQIEAA-NKGREDAIKQLRK 1664
Cdd:pfam07111 295 SLEPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTS----QSQEQAIlQRALQDKAAEVEV 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1665 LQAQTKDYQRELEEARASRDDIFAQSKENEKKLKGLEAEILQLQEELAASERSRRHAEQERDELADEISNST-------- 1736
Cdd:pfam07111 371 ERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVrkvhtikg 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1737 --SGKSAL----------------------------------LDEKRRLEARIAHLEEELEEEQSNME---------LLN 1771
Cdd:pfam07111 451 lmARKVALaqlrqescpppppappvdadlsleleqlreernrLDAELQLSAHLIQQEVGRAREQGEAErqqlsevaqQLE 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1772 DRFRKTTLQVDTLNSELAAERSSGQKSE----NARQQLERQNKELKAKLQELEGSVKSKFKATIATLESKiaqLEEQLEQ 1847
Cdd:pfam07111 531 QELQRAQESLASVGQQLEVARQGQQESTeeaaSLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRR---LNEARRE 607
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 148223878 1848 EAKERVASNKLVRRT--EKKLKEVFMQVEDERRhadqyKEQMEKANTRMKQLKR 1899
Cdd:pfam07111 608 QAKAVVSLRQIQHRAtqEKERNQELRRLQDEAR-----KEEGQRLARRVQELER 656
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
862-1427 |
4.58e-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: 45.43 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 862 QVTRQEEELVAKDEELLKVKEKQSKVEGELVDMEQKHQQLVEEKNILAEQLHAETELFAEA---EEMRARLAIKkqEMEE 938
Cdd:TIGR01612 1170 EIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKideEKKKSEHMIK--AMEA 1247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 939 ILRDL-EIRMEEEEERNQ--VLQNEKKKMQTHVQDLEEQLDEEEAAQKLQLEKVTAEAKIKKMEEDILVLEDQNSKflke 1015
Cdd:TIGR01612 1248 YIEDLdEIKEKSPEIENEmgIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREKSLKIIEDFSEESDINDI---- 1323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1016 KKLLEERIAESTSQLAEEEEKAKNLAKLKNKQemmisdleeRLKKEEKTRQELEKAKRKLDGETTDFQDQIAELQAQIEE 1095
Cdd:TIGR01612 1324 KKELQKNLLDAQKHNSDINLYLNEIANIYNIL---------KLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKK 1394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1096 LKLQLAKKEEELQAALARGDEEVlqkNNTLKLVRELQAQIAelqedleSEKASRNKAEKQKRDLSEELEALKTELEdtLD 1175
Cdd:TIGR01612 1395 IKDDINLEECKSKIESTLDDKDI---DECIKKIKELKNHIL-------SEESNIDTYFKNADENNENVLLLFKNIE--MA 1462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1176 TTAAQQELRTKREQEVAELRKSIEE--ETRNHEAQIQEMRQRQATALEELSEQLEQAKRFKVNLEKNKQSLESDNKELAT 1253
Cdd:TIGR01612 1463 DNKSQHILKIKKDNATNDHDFNINElkEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAKT 1542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1254 EVKSLQQMKAESEYKRK-KLEGQVQELHAKVLEGDRLR-ADMVEKSSKLQNELENVSSLLEEAEKKGIKLAKDVASMESQ 1331
Cdd:TIGR01612 1543 KKDSEIIIKEIKDAHKKfILEAEKSEQKIKEIKKEKFRiEDDAAKNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDC 1622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1332 LQDTQELLQEETRQKLN-QSSRIRQLEEEKNNLQEQQEEEEEARKSLE---KQILSLQSQLIEAKKKVDD-----EVGTI 1402
Cdd:TIGR01612 1623 LKETESIEKKISSFSIDsQDTELKENGDNLNSLQEFLESLKDQKKNIEdkkKELDELDSEIEKIEIDVDQhkknyEIGII 1702
|
570 580
....*....|....*....|....*
gi 148223878 1403 EGLEEVKKKLLKDTEGLGQRLEEKI 1427
Cdd:TIGR01612 1703 EKIKEIAIANKEEIESIKELIEPTI 1727
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1156-1325 |
4.70e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1156 KRDLSEELEALKTELEDTLDttAAQQELRTKREQEVAELRKSIEEETRNHEAQIQEMR---QRQATALEELSEQLEQAKR 1232
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRnelQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1233 fkvNLEKNKQSLESDNKELATEVKSLQQMKAESEYKRKKlegQVQEL---------HAKVLEGDRLRADMVEKSSKLQNE 1303
Cdd:PRK12704 104 ---LLEKREEELEKKEKELEQKQQELEKKEEELEELIEE---QLQELerisgltaeEAKEILLEKVEEEARHEAAVLIKE 177
|
170 180
....*....|....*....|..
gi 148223878 1304 LEnvssllEEAEKKGIKLAKDV 1325
Cdd:PRK12704 178 IE------EEAKEEADKKAKEI 193
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1041-1193 |
4.84e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.07 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1041 AKLKNKQEMMISDLEERLKKEEKTRQELEKAKRKLDGETtdfQDQIAELQAQIEELKlqlakkeEELQAALARGDEEvlq 1120
Cdd:COG0542 400 ARVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEAS---FERLAELRDELAELE-------EELEALKARWEAE--- 466
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148223878 1121 knntlklvRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDttaaqqelrtkrEQEVAE 1193
Cdd:COG0542 467 --------KELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVT------------EEDIAE 519
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1385-1719 |
5.38e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 44.67 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1385 QSQLIEAKKKVDDEVGTIEGLEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKk 1464
Cdd:pfam19220 47 KSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALER- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1465 qkkfdQLLAEEKNISARhAEERDRAEADAREKETKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHE 1544
Cdd:pfam19220 126 -----QLAAETEQNRAL-EEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1545 LEKSKRALDQQVEEMRTQLEELEDELQ------GTEDAKLRLEVNMQAMK--------AQFERDL-QTRDEQNEEKKral 1609
Cdd:pfam19220 200 LETQLDATRARLRALEGQLAAEQAEREraeaqlEEAVEAHRAERASLRMKlealtaraAATEQLLaEARNQLRDRDE--- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1610 vkQVRELEAELEDERKQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIKQ----LRKLQAQTKDYQRELEEARASRDD 1685
Cdd:pfam19220 277 --AIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERaemlTKALAAKDAALERAEERIASLSDR 354
|
330 340 350
....*....|....*....|....*....|....
gi 148223878 1686 IFAQSKENEKKLKGLEAEILQLQEELAAsERSRR 1719
Cdd:pfam19220 355 IAELTKRFEVERAALEQANRRLKEELQR-ERAER 387
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1555-1945 |
5.42e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.12 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1555 QVEEMRTQLEELEDELQGTEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRALvKQVRELEAELEDERKQRAMAVAIK 1634
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRI-RLLEKREAEAEEALREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1635 KKLEMDM----KDFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDIFAQSKENEKKLKGLEaeilQLQEE 1710
Cdd:pfam05557 82 KKYLEALnkklNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAE----QLRQN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1711 LAASERSRRHAEQERDELADEISNSTSGK-------------SALLDEKRRLEARIAHLEEEleeeQSNMELLN------ 1771
Cdd:pfam05557 158 LEKQQSSLAEAEQRIKELEFEIQSQEQDSeivknskselariPELEKELERLREHNKHLNEN----IENKLLLKeevedl 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1772 ----DRFRKTTLQVDTL---NSELAAERSSGQKSENAR--------------QQLERQNKELKAKLQELEGSVKSKfKAT 1830
Cdd:pfam05557 234 krklEREEKYREEAATLeleKEKLEQELQSWVKLAQDTglnlrspedlsrriEQLQQREIVLKEENSSLTSSARQL-EKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1831 IATLESKIAQLEEQLEQEAKERVASNKLVRRTEKKL-------------------------------------------- 1866
Cdd:pfam05557 313 RRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVllltkerdgyrailesydkeltmsnyspqllerieeaedmtqkm 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1867 ----KEVFMQVEDERRHADQYKEQMEKANTRMKQLKRQLEEAEEEATRANASArkLQRELDDATEANEVLSREVSTLKNR 1942
Cdd:pfam05557 393 qahnEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDS--LRRKLETLELERQRLREQKNELEME 470
|
...
gi 148223878 1943 LRR 1945
Cdd:pfam05557 471 LER 473
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
862-1340 |
5.46e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.12 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 862 QVTRQEEELVAKDEELLKVKEKQSKVEGELVDMEQKHQQLVEEKNILAEQLHAETELFAEAEEMRARLAIKKQEMEEILR 941
Cdd:pfam05557 119 QIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELAR 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 942 DLEirmeeeeernqvLQNEKKKMQTHVQDLEEQLDEEEAaqkLQLEKVTAEAKIKKME---EDILVLEDQNSKFLKEKKL 1018
Cdd:pfam05557 199 IPE------------LEKELERLREHNKHLNENIENKLL---LKEEVEDLKRKLEREEkyrEEAATLELEKEKLEQELQS 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1019 LEERIAESTSQLAEEEEKAKNLAKLKNKQEMMI---SDLEERLKKEEKTRQELEKAKRKLDGETTDFQDQIAELQAQIEE 1095
Cdd:pfam05557 264 WVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKeenSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRR 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1096 L--KLQLAKKEEE-LQAALARGDEEVLQKNNTLKL---VRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTE 1169
Cdd:pfam05557 344 LqrRVLLLTKERDgYRAILESYDKELTMSNYSPQLlerIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERE 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1170 LeDTLDTTAAQQELRTKREqEVAELRKSIEEetrnHEAQIQEMRQRQatalEELSEQLEqakrfkvnleknKQSLESDNK 1249
Cdd:pfam05557 424 L-QALRQQESLADPSYSKE-EVDSLRRKLET----LELERQRLREQK----NELEMELE------------RRCLQGDYD 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1250 ELATEVKSLQQMKAESEYKRKKlegqvQELHAKVLEGDRLRadmvEKSSKLQNELENVSSL----LEEAEKKGIKLAKDV 1325
Cdd:pfam05557 482 PKKTKVLHLSMNPAAEAYQQRK-----NQLEKLQAEIERLK----RLLKKLEDDLEQVLRLpettSTMNFKEVLDLRKEL 552
|
490
....*....|....*
gi 148223878 1326 ASMESQLQDTQELLQ 1340
Cdd:pfam05557 553 ESAELKNQRLKEVFQ 567
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1227-1399 |
5.65e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1227 LEQAKRFKVNL---EKNKQSLESDNKELatevkslQQMKAESEYKRKKLEGQVQELHAKVLEGDRLRADMVEKSSKLQNE 1303
Cdd:PRK00409 491 FEIAKRLGLPEniiEEAKKLIGEDKEKL-------NELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1304 LENVSSLLEEAEKKGIKLAKDVAsmESQLQDTQELLQEETRqklnqSSRIRQLEEeknnlqeqqeeeeeARKSLEKQILS 1383
Cdd:PRK00409 564 EDKLLEEAEKEAQQAIKEAKKEA--DEIIKELRQLQKGGYA-----SVKAHELIE--------------ARKRLNKANEK 622
|
170 180
....*....|....*....|.
gi 148223878 1384 LQSQLIEAKKKVD-----DEV 1399
Cdd:PRK00409 623 KEKKKKKQKEKQEelkvgDEV 643
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
995-1332 |
5.69e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.89 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 995 IKKMEEDILVLE-------DQNSKFLKEKKLLEERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLeERLKKEEKTRQE 1067
Cdd:PLN02939 137 IQNAEKNILLLNqarlqalEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQL-EKLRNELLIRGA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1068 LEKA-KRKLDGETTDFQDQIAELQAQIEELKLQLAKkeeelqaaLARGDEEV--LQKNNTL--KLVRELQAQIAELQEDL 1142
Cdd:PLN02939 216 TEGLcVHSLSKELDVLKEENMLLKDDIQFLKAELIE--------VAETEERVfkLEKERSLldASLRELESKFIVAQEDV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1143 esEKASRNKAEKqkrdLSEELEalktELEDTLDTTAAQQelrtkrEQEVAELRksieeetrnheaQIQEMRQRqataLEE 1222
Cdd:PLN02939 288 --SKLSPLQYDC----WWEKVE----NLQDLLDRATNQV------EKAALVLD------------QNQDLRDK----VDK 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1223 LSEQLEQAKRFKVNLEKnkqslesdnkelateVKSLQQmkaeseyKRKKLEGQVQELHAKVLEGDRLRADMVEKSSklqn 1302
Cdd:PLN02939 336 LEASLKEANVSKFSSYK---------------VELLQQ-------KLKLLEERLQASDHEIHSYIQLYQESIKEFQ---- 389
|
330 340 350
....*....|....*....|....*....|
gi 148223878 1303 elENVSSLLEEAEKKGikLAKDVASMESQL 1332
Cdd:PLN02939 390 --DTLSKLKEESKKRS--LEHPADDMPSEF 415
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1048-1182 |
5.76e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 44.46 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1048 EMMISDLEERLKKE---------EKTRQELEKAKRKLdgetTDFQD---------QIAELQAQIEELKLQLAKKEEELQA 1109
Cdd:COG3524 164 EELVNQLSERAREDavrfaeeevERAEERLRDAREAL----LAFRNrngildpeaTAEALLQLIATLEGQLAELEAELAA 239
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148223878 1110 ALARGDEEVLQknntlklVRELQAQIAELQEDLESEKA--SRNKAEKQKRDLSEELEALKTEL---EDTLDTTAAQQE 1182
Cdd:COG3524 240 LRSYLSPNSPQ-------VRQLRRRIAALEKQIAAERArlTGASGGDSLASLLAEYERLELERefaEKAYTSALAALE 310
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1417-1755 |
5.82e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 44.67 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1417 EGLGQRLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARHAEERDRAEADAREK 1496
Cdd:pfam19220 6 ELLRVRLGEMADRLEDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1497 ETKALSLARALDEALEAQDEFERLN---KQLRAEMEDLMSSKDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDELQGT 1573
Cdd:pfam19220 86 EELVARLAKLEAALREAEAAKEELRielRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1574 EDAKLRLEVNMQAMKAQFER------DLQTRDEQNEEKKRALVKQVRELEAELEDERKQRAMAVAI-----------KKK 1636
Cdd:pfam19220 166 RERLALLEQENRRLQALSEEqaaelaELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQleeaveahraeRAS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1637 LEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDIfaqskenEKKLKGLEAEILQLQEELAASER 1716
Cdd:pfam19220 246 LRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTL-------ERRLAGLEADLERRTQQFQEMQR 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 148223878 1717 SRRHAEQERDEL-------------ADEISNSTSGKSA-----LLDEKRRLEARIAH 1755
Cdd:pfam19220 319 ARAELEERAEMLtkalaakdaalerAEERIASLSDRIAeltkrFEVERAALEQANRR 375
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1489-1741 |
5.98e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1489 AEADAREKETKAlSLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKSKRALDQQVEEMRTQLEELED 1568
Cdd:COG3883 12 AFADPQIQAKQK-ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1569 ---ELQGTEDAKLRLEV------------NMQAMKAQFERDLQTRDEQNEEKKralvkQVRELEAELEDERKQramAVAI 1633
Cdd:COG3883 91 rarALYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEELKADKA-----ELEAKKAELEAKLAE---LEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1634 KKKLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDIFAQSKENEKKLKGLEAEILQLQEELAA 1713
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
250 260
....*....|....*....|....*...
gi 148223878 1714 SERSRRHAEQERDELADEISNSTSGKSA 1741
Cdd:COG3883 243 AASAAGAGAAGAAGAAAGSAGAAGAAAG 270
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1091-1201 |
6.04e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.07 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1091 AQIEELKLQLAKKEEELQAALARGDEEVLQKnntlklVRELQAQIAELQEDLESEKAsRNKAEKQkrdLSEELEALKTEL 1170
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEASFER------LAELRDELAELEEELEALKA-RWEAEKE---LIEEIQELKEEL 480
|
90 100 110
....*....|....*....|....*....|.
gi 148223878 1171 EDTLDTTAAQQELRTKREQEVAELRKSIEEE 1201
Cdd:COG0542 481 EQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1129-1866 |
6.49e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1129 RELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALK-------TELEDTLD------TTAAQQELRTKREQEVAELR 1195
Cdd:PRK04863 282 RVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNeaesdleQDYQAASDhlnlvqTALRQQEKIERYQADLEELE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1196 KSIEE--ETRNHEAQIQEMRQRQATALEelseqlEQAKRFKVNLEKNKQSLEsdnkelATEVKSLQQMKAESEYKRKKLE 1273
Cdd:PRK04863 362 ERLEEqnEVVEEADEQQEENEARAEAAE------EEVDELKSQLADYQQALD------VQQTRAIQYQQAVQALERAKQL 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1274 GQVQELHAKVLEG--DRLRADMVEKSSKLqNELENVSSLLEEA----EKKGIKLAKDVASME-SQLQDT-QELLQEETRQ 1345
Cdd:PRK04863 430 CGLPDLTADNAEDwlEEFQAKEQEATEEL-LSLEQKLSVAQAAhsqfEQAYQLVRKIAGEVSrSEAWDVaRELLRRLREQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1346 KlNQSSRIRQLEEEKNNLQEQQEEEEEARKSLE--KQILSLQSQLIEAKKKVDDEVG-TIEGLEEVKKKLLKDTEGLGQR 1422
Cdd:PRK04863 509 R-HLAEQLQQLRMRLSELEQRLRQQQRAERLLAefCKRLGKNLDDEDELEQLQEELEaRLESLSESVSEARERRMALRQQ 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1423 LEEKIIAYEKLEKTK----------NRLQ----------QELDDLMVD-LDHQRQIVSNLEKKQKKFDQLLAEEKNISAR 1481
Cdd:PRK04863 588 LEQLQARIQRLAARApawlaaqdalARLReqsgeefedsQDVTEYMQQlLERERELTVERDELAARKQALDEEIERLSQP 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1482 HAEERDRAEADAREKETKALSLARAlDEALEAQDEFERLNKQLR---------------AEMEDL----------MSSKD 1536
Cdd:PRK04863 668 GGSEDPRLNALAERFGGVLLSEIYD-DVSLEDAPYFSALYGPARhaivvpdlsdaaeqlAGLEDCpedlyliegdPDSFD 746
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1537 DVGKNVHELEKS----------------------KRALDQQVEEMRTQLEELEDELqgtedAKLRLEVN-MQAMKAQFER 1593
Cdd:PRK04863 747 DSVFSVEELEKAvvvkiadrqwrysrfpevplfgRAAREKRIEQLRAEREELAERY-----ATLSFDVQkLQRLHQAFSR 821
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1594 DLQTR-----DEQNEEKKRALVKQVRELEAELED----ERKQRAMAVAIKKKLEM-----------DMKDFESQIEAAnk 1653
Cdd:PRK04863 822 FIGSHlavafEADPEAELRQLNRRRVELERALADhesqEQQQRSQLEQAKEGLSAlnrllprlnllADETLADRVEEI-- 899
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1654 grEDAIKQLRKLQAQTKDYQRELEEArasrDDIFAQSKENEKKLKGLEAEILQLQEELAASE---------RSRRHA--- 1721
Cdd:PRK04863 900 --REQLDEAEEAKRFVQQHGNALAQL----EPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKqqafaltevVQRRAHfsy 973
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1722 EQERDELADEISNSTSGKSALLD-EKRRLEARIAHLEEELEEEQSNMEL--LNDRFRKTTLQVDTLNSEL---------- 1788
Cdd:PRK04863 974 EDAAEMLAKNSDLNEKLRQRLEQaEQERTRAREQLRQAQAQLAQYNQVLasLKSSYDAKRQMLQELKQELqdlgvpadsg 1053
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1789 AAERSSGQKSE---------NARQQLERQNKELKAKLQELEGSVKSkfkatiatLESKIAQLEEQLEQEAKERVASNKLV 1859
Cdd:PRK04863 1054 AEERARARRDElharlsanrSRRNQLEKQLTFCEAEMDNLTKKLRK--------LERDYHEMREQVVNAKAGWCAVLRLV 1125
|
....*....
gi 148223878 1860 RR--TEKKL 1866
Cdd:PRK04863 1126 KDngVERRL 1134
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1206-1442 |
7.12e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 7.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1206 EAQIQEMRQRQATALEELSEQLEQAKRFKVNLEKNKQSLESDNK--ELATEVKSLQQMKAESEYKRKKLEGQVQELHAKV 1283
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1284 legDRLRadmveksSKLQNELENVSSLLEEAEkkgiklakdVASMESQLQDTQELLQEETRQKLNQSSRIRQLEEEKNNL 1363
Cdd:COG3206 243 ---AALR-------AQLGSGPDALPELLQSPV---------IQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAAL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1364 QEQ-QEEEEEARKSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLlkdteglgQRLEEKI-IAYEKLEKTKNRLQ 1441
Cdd:COG3206 304 RAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL--------RRLEREVeVARELYESLLQRLE 375
|
.
gi 148223878 1442 Q 1442
Cdd:COG3206 376 E 376
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
989-1102 |
7.33e-04 |
|
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region.
Pssm-ID: 394970 [Multi-domain] Cd Length: 598 Bit Score: 44.56 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 989 VTAEAKIKKMEEDILVledQNSKFLKEKKllEERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKKEEKtrQEL 1068
Cdd:pfam00012 480 VSAKDKGTGKEQEITI---EASEGLSDDE--IERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEGD--KVP 552
|
90 100 110
....*....|....*....|....*....|....*....
gi 148223878 1069 EKAKRKLDGETTD-----FQDQIAELQAQIEELKLQLAK 1102
Cdd:pfam00012 553 EAEKSKVESAIEWlkdelEGDDKEEIEAKTEELAQVSQK 591
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1083-1214 |
7.73e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 44.25 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1083 QDQIAELQAQIEELKLQLAKKEEE---LQAALARGDEEVLQ--------------KNNTLKLVRELQAQIAELQEDLESE 1145
Cdd:pfam05667 334 EEELEELQEQLEDLESSIQELEKEikkLESSIKQVEEELEElkeqneelekqykvKKKTLDLLPDAEENIAKLQALVDAS 413
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148223878 1146 KAS----RNKAEKQKRDLSEELEALKTELEDTLDTTAAQ----QELRTKrEQEVAELRKSIEEETRNHEAQIQEMRQ 1214
Cdd:pfam05667 414 AQRlvelAGQWEKHRVPLIEEYRALKEAKSNKEDESQRKleeiKELREK-IKEVAEEAKQKEELYKQLVAEYERLPK 489
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1400-1945 |
7.79e-04 |
|
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: 44.58 E-value: 7.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1400 GTIEGLEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQ--ELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEE-- 1475
Cdd:pfam02463 142 GKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENlaELIIDLEELKLQELKLKEQAKKALEYYQLKEKLel 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1476 -------KNISARHAEERDRAEADAREKETKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKS 1548
Cdd:pfam02463 222 eeeyllyLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1549 KRALDQQVEEMRTQLEELEDELQGTEDAKLRLEVNM---QAMKAQFERDLQTRDEQNEEKKRALVKQVRELEAELEDERK 1625
Cdd:pfam02463 302 LLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIeelEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1626 QRAMAVAIKKKLE--MDMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDIFAQSKENEKKLKGLEAE 1703
Cdd:pfam02463 382 ESERLSSAAKLKEeeLELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1704 ILQLQEELAASERSRRHAEQERDELADEISnstSGKSALLDEKRRLEARIAHLEEELEEEQSNMELLNDRFRKTTLQVDT 1783
Cdd:pfam02463 462 KDELELKKSEDLLKETQLVKLQEQLELLLS---RQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAV 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1784 LNSELAAERSSGQKSENARQQLERQNKELKAKLQ--------ELEGSVKSKFKATIATLESKIAQLEEQLEQEAKERVAS 1855
Cdd:pfam02463 539 ENYKVAISTAVIVEVSATADEVEERQKLVRALTElplgarklRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADED 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1856 NKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANTRMKQLKRQLEEAEEEATRANASARKLQRELDDATEANEVLSRE 1935
Cdd:pfam02463 619 DKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQ 698
|
570
....*....|
gi 148223878 1936 VSTLKNRLRR 1945
Cdd:pfam02463 699 LEIKKKEQRE 708
|
|
| Use1 |
pfam09753 |
Membrane fusion protein Use1; This entry is of a family of proteins all approximately 300 ... |
1117-1227 |
7.87e-04 |
|
Membrane fusion protein Use1; This entry is of a family of proteins all approximately 300 residues in length. The proteins have a single C-terminal trans-membrane domain and a SNARE [soluble NSF (N-ethylmaleimide-sensitive fusion protein) attachment protein receptor] domain of approximately 60 residues. The SNARE domains are essential for membrane fusion and are conserved from yeasts to humans. Use1 is one of the three protein subunits that make up the SNARE complex and it is specifically required for Golgi-endoplasmic reticulum retrograde transport.
Pssm-ID: 462882 [Multi-domain] Cd Length: 245 Bit Score: 43.47 E-value: 7.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1117 EVLQKNNTLKLVRELQAQIAELQEDLESEKASRNKAEKQK-RDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELR 1195
Cdd:pfam09753 14 ERLAKEDRSDNQWRLEKYVKALEEMLEELQKERDKPSKDVlNEYSERVEFLKGLLEAEKLSSPEEKALANQFLAPGFAES 93
|
90 100 110
....*....|....*....|....*....|...
gi 148223878 1196 KSIEEETRNHEAQIQEMRQRQATALE-ELSEQL 1227
Cdd:pfam09753 94 PRSPEESSERESASKELRQKTKAKYQsELRKEL 126
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1696-1852 |
8.44e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1696 KLKGLEAEILQLQEELAASERSRRHAEQERDELADEISNSTSGKSALLDEKRRLEARIAHLEEELEEEQSNMELLndrfr 1775
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1776 KTTLQVDTLNSELAAERSSGQKSENARQQLERQNKELKAKLQELEG---SVKSKFKATIATLESKIAQLEEQLEQEAKER 1852
Cdd:COG1579 86 RNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAelaELEAELEEKKAELDEELAELEAELEELEAER 165
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1477-1679 |
8.49e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 8.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1477 NISARHAEERDRAEADAREkeTKALSLARALDEALEaqdeferlnKQLRAEMEDLMSSKDDVGKNVHELEKSKRALDQQV 1556
Cdd:COG2433 354 RVEKKVPPDVDRDEVKARV--IRGLSIEEALEELIE---------KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQV 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1557 EEMRTQLEELEDELQGTEDAKLRLEvnmqaMKAQFERDLQTRDEQNEEKKRALVKQVRELEAELEDERKQRamavaikKK 1636
Cdd:COG2433 423 ERLEAEVEELEAELEEKDERIERLE-----RELSEARSEERREIRKDREISRLDREIERLERELEEERERI-------EE 490
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 148223878 1637 LEMDMKDFESQIEAANKGREDAIKQLRKLqaqTKDYQRELEEA 1679
Cdd:COG2433 491 LKRKLERLKELWKLEHSGELVPVKVVEKF---TKEAIRRLEEE 530
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1016-1179 |
9.17e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 43.51 E-value: 9.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1016 KKLLEERIAESTSQLAEEEEKAKNLAKlknkqemmiSDLEERLKKEEKTRQELEKAKRKLdgetTDFQDQIAELQAQIEE 1095
Cdd:cd22656 94 AEILELIDDLADATDDEELEEAKKTIK---------ALLDDLLKEAKKYQDKAAKVVDKL----TDFENQTEKDQTALET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1096 LKLQLAKKEEELQAALARGDEEVLQK---NNTLKLVRELQAQIAELQEDLESEKASRNKAEKqkrdLSEELEALKTELED 1172
Cdd:cd22656 161 LEKALKDLLTDEGGAIARKEIKDLQKeleKLNEEYAAKLKAKIDELKALIADDEAKLAAALR----LIADLTAADTDLDN 236
|
....*..
gi 148223878 1173 TLDTTAA 1179
Cdd:cd22656 237 LLALIGP 243
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1021-1228 |
9.18e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.09 E-value: 9.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1021 ERIAESTsqlaEEEEKAKNLAKlknKQEMMISDLEERLKKEEKTRQELEKAKRKldgettdfqdqIAELQAQIEELKlql 1100
Cdd:COG2268 192 RKIAEII----RDARIAEAEAE---RETEIAIAQANREAEEAELEQEREIETAR-----------IAEAEAELAKKK--- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1101 AKKEEELQAALARGDEEVLQKNNTLKLVRELQAQIAELQEDLESEKASRNKAEKQ-KRDLSEELEALKTELEdtldtTAA 1179
Cdd:COG2268 251 AEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAElEADVRKPAEAEKQAAE-----AEA 325
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 148223878 1180 QQELRTKREQEVAE---LRKSIEEETRNHEAQIQEMR-QRQATALEELSEQLE 1228
Cdd:COG2268 326 EAEAEAIRAKGLAEaegKRALAEAWNKLGDAAILLMLiEKLPEIAEAAAKPLE 378
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1465-1943 |
9.23e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.65 E-value: 9.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1465 QKKFDQLLAEEKNISArhaEERDRAEADAREKETKALSLARALDEalEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHE 1544
Cdd:TIGR00606 172 KQKFDEIFSATRYIKA---LETLRQVRQTQGQKVQEHQMELKYLK--QYKEKACEIRDQITSKEAQLESSREIVKSYENE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1545 LEKSKRALdQQVEEMRTQLEELEDELQGTEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRALVKQVRELEAELEDER 1624
Cdd:TIGR00606 247 LDPLKNRL-KEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1625 KQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDIFAQSKENEKKLKgleaei 1704
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLV------ 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1705 lqlqeeLAASERSRRHAEQERDELADEISNSTSGKSALLDEKRRLEARIAHLEEELEEEQSNMellndRFRKTTLQVDTL 1784
Cdd:TIGR00606 400 ------IERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEEL-----KFVIKELQQLEG 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1785 NSELAAERSSGQKSENARQQLERQNKELKAKLQELEgsvksKFKATIATLESKIAQLEEQLEQEAKERVASNKLVRRTEK 1864
Cdd:TIGR00606 469 SSDRILELDQELRKAERELSKAEKNSLTETLKKEVK-----SLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKD 543
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148223878 1865 KLKEVFMQVEDERRHADQYKEQMEKANTRmKQLKRQLEEAEEEATRANASARKLQRELDDATEANEVLSREVSTLKNRL 1943
Cdd:TIGR00606 544 KMDKDEQIRKIKSRHSDELTSLLGYFPNK-KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQL 621
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1033-1627 |
1.00e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 44.36 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1033 EEEKAKNLAKLKNKQEMMISDL----EERLKKEEKTRQELEKAKRKLDGETTDFQDQIAELQAQIEELKLQLAKKEEELQ 1108
Cdd:pfam07111 135 EEGSQRELEEIQRLHQEQLSSLtqahEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1109 AALArgdeevlqknntlkLVRELQAQIAElqedlesekasrnkaEKQKRDLSEELEALKTELEDTLdttaaqqelrtkre 1188
Cdd:pfam07111 215 AQVT--------------LVESLRKYVGE---------------QVPPEVHSQTWELERQELLDTM-------------- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1189 QEVAELRKSIEEETRNHEAQIQEMRQRQATALEELSEQLEQAKRFKVNLEKNKQSLESDNKELATEVksLQQMKAESEYK 1268
Cdd:pfam07111 252 QHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFAL--MVQLKAQDLEH 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1269 R---KKLEGQVQELHAKVLEGDRLRAdmvekssKLQNELENVSSLLeEAEKKGIKlakdvaSMESQLQDTQELLQEETRQ 1345
Cdd:pfam07111 330 RdsvKQLRGQVAELQEQVTSQSQEQA-------ILQRALQDKAAEV-EVERMSAK------GLQMELSRAQEARRRQQQQ 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1346 KLNQSSRIRQLEEEKNNLQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDdevgTIEGLeeVKKKLlkdteGLGQRLEE 1425
Cdd:pfam07111 396 TASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVH----TIKGL--MARKV-----ALAQLRQE 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1426 KIIAYEKLEKTKNrlqqeldDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKnisarhAEERDRAEADAREKETKALSLAR 1505
Cdd:pfam07111 465 SCPPPPPAPPVDA-------DLSLELEQLREERNRLDAELQLSAHLIQQEV------GRAREQGEAERQQLSEVAQQLEQ 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1506 ALDealEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKSK----RALDQQVEEMRTQL-EELEDELQGTEDAKLRl 1580
Cdd:pfam07111 532 ELQ---RAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQeiygQALQEKVAEVETRLrEQLSDTKRRLNEARRE- 607
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 148223878 1581 evnmQAMKAQFERDLQTRDEQNEEKKRALvkqvRELEAELEDERKQR 1627
Cdd:pfam07111 608 ----QAKAVVSLRQIQHRATQEKERNQEL----RRLQDEARKEEGQR 646
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
996-1241 |
1.21e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 996 KKMEEDILVLedqnSKFLKEKKLLEERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEE-----RLKKEEKTRQELEK 1070
Cdd:PHA02562 153 RKLVEDLLDI----SVLSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKkngenIARKQNKYDELVEE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1071 AKrkldgettDFQDQIAELQAQIEELKLQLAKKEEELQA---ALARGDEEVLQKNNTLKLVRELQ------AQIAELQED 1141
Cdd:PHA02562 229 AK--------TIKAEIEELTDELLNLVMDIEDPSAALNKlntAAAKIKSKIEQFQKVIKMYEKGGvcptctQQISEGPDR 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1142 LESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELrKSIEEETRNHEAQIQEM---RQRQAT 1218
Cdd:PHA02562 301 ITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSL-ITLVDKAKKVKAAIEELqaeFVDNAE 379
|
250 260
....*....|....*....|...
gi 148223878 1219 ALEELSEQLEQAKRFKVNLEKNK 1241
Cdd:PHA02562 380 ELAKLQDELDKIVKTKSELVKEK 402
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1086-1325 |
1.30e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 44.05 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1086 IAELQAQIEELKLQLAKKEeelQAALARGDEEVLQKNNTlKLVRELQAQIAEL---QEDLES--EKASRNKAEKQKRDLS 1160
Cdd:NF012221 1537 TSESSQQADAVSKHAKQDD---AAQNALADKERAEADRQ-RLEQEKQQQLAAIsgsQSQLEStdQNALETNGQAQRDAIL 1612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1161 EELEALKTELE------DTLDTTAAQQELRTK--REQEVAELRKSIEEE---TRNH-EAQIQEMRQRQATALEELSEQLE 1228
Cdd:NF012221 1613 EESRAVTKELTtlaqglDALDSQATYAGESGDqwRNPFAGGLLDRVQEQlddAKKIsGKQLADAKQRHVDNQQKVKDAVA 1692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1229 QAKRFKVNLEKNKQSLESDNKELATEVKslqqmKAESEYKRKKLEGQVQELHAK-VLEGDRLRADmvEKSSKLQNELENV 1307
Cdd:NF012221 1693 KSEAGVAQGEQNQANAEQDIDDAKADAE-----KRKDDALAKQNEAQQAESDANaAANDAQSRGE--QDASAAENKANQA 1765
|
250
....*....|....*...
gi 148223878 1308 sslleEAEKKGIKLAKDV 1325
Cdd:NF012221 1766 -----QADAKGAKQDESD 1778
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1023-1232 |
1.42e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.53 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1023 IAESTSQL-------AEEEEKAKnlaklknKQEMMISDLEERLKKEEKTRQELEKAKRKLDGETTDFQDQIAELQAQIEE 1095
Cdd:PRK11637 42 ASDNRDQLksiqqdiAAKEKSVR-------QQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1096 LKLQLAKKE----EELQAALARGDEEVLQknntLKLVRE-------LQAQIAEL----QEDLESEKASRNKAEKQKRDLS 1160
Cdd:PRK11637 115 LEQQQAAQErllaAQLDAAFRQGEHTGLQ----LILSGEesqrgerILAYFGYLnqarQETIAELKQTREELAAQKAELE 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148223878 1161 EELEALKTELEDTLDTTAAQQELRTKREQEVAELRKSIEEEtrnhEAQIQEMRQRQAtaleELSEQLEQAKR 1232
Cdd:PRK11637 191 EKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKD----QQQLSELRANES----RLRDSIARAER 254
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1084-1332 |
1.44e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1084 DQIAELQAQIEELKLQLAKKEEELQaalargdeevLQKNNTLKLVRELQAQIAELQEDLESEKASRNKAEKQKRDLSEEL 1163
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIK----------TYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1164 EALKTELEdtlDTTAAQQELRTKREQ---EVAELRKSIEEETRNHE--------AQIQEMRQRQATALEELSEQLEQAKR 1232
Cdd:PHA02562 244 LNLVMDIE---DPSAALNKLNTAAAKiksKIEQFQKVIKMYEKGGVcptctqqiSEGPDRITKIKDKLKELQHSLEKLDT 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1233 FKVNLEK-----NKQSLESdnKELATEVKSLQQMKAESEYKRKKLEGQVQELHAKvlegdrlRADMVEKSSKLQNELENV 1307
Cdd:PHA02562 321 AIDELEEimdefNEQSKKL--LELKNKISTNKQSLITLVDKAKKVKAAIEELQAE-------FVDNAEELAKLQDELDKI 391
|
250 260
....*....|....*....|....*
gi 148223878 1308 SSlleeaEKKGIKLAKDVASMESQL 1332
Cdd:PHA02562 392 VK-----TKSELVKEKYHRGIVTDL 411
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1015-1217 |
1.47e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 43.77 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1015 EKKLLEERIaestsQLAEEEEKAKNLAklknkqEMMISDLEERLKKEEKTRQELEKAKRKLDGETTDFQ------DQIAE 1088
Cdd:PLN03188 1046 EKKLEQERL-----RWTEAESKWISLA------EELRTELDASRALAEKQKHELDTEKRCAEELKEAMQmameghARMLE 1114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1089 LQAQIEELKLQLAKKEEELQ---------AALA--RGDEEvlqknntlKLVRELQAQIAELqedleseKASRnkaEKQKR 1157
Cdd:PLN03188 1115 QYADLEEKHIQLLARHRRIQegiddvkkaAARAgvRGAES--------KFINALAAEISAL-------KVER---EKERR 1176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148223878 1158 DLSEELEALKTELEDTLDTTAAQQELRT-------------KR----EQEVAELRKSIEEETRNHEAQIQEMRQRQA 1217
Cdd:PLN03188 1177 YLRDENKSLQAQLRDTAEAVQAAGELLVrlkeaeealtvaqKRamdaEQEAAEAYKQIDKLKRKHENEISTLNQLVA 1253
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1694-1820 |
1.54e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.03 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1694 EKKLKGLEAEILQLQEELAASERSRRHAEQERDELADEISNSTsGKSALLDEKRRLEARIAHLEeeleeeQSNMELLNDr 1773
Cdd:PRK09039 73 RQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAE-GRAGELAQELDSEKQVSARA------LAQVELLNQ- 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 148223878 1774 frkttlQVDTLNSELAAERSSGQKSENARQQLERQ--------NKELKAKLQELE 1820
Cdd:PRK09039 145 ------QIAALRRQLAALEAALDASEKRDRESQAKiadlgrrlNVALAQRVQELN 193
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1430-1863 |
1.68e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 43.36 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1430 YEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLaeEKNISARHAEERDRAEADAREKETKALS---LARA 1506
Cdd:COG5278 81 YEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAEL--EQVIALRRAGGLEAALALVRSGEGKALMdeiRARL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1507 LDEALEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKSKRALDQQVEEMRTQLEELEDELQGTEDAKLRLEVNMQA 1586
Cdd:COG5278 159 LLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAAL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1587 MKAQFERDLQTRDEQNEEKKRALVKQVRELEAELEDERKQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIKQLRKLQ 1666
Cdd:COG5278 239 ALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1667 AQTKDYQRELEEARASRDDIFAQSKENEKKLKGLEAEILQLQEELAASERSRRHAEQERDELADEISNSTSGKSALLDEK 1746
Cdd:COG5278 319 AAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAA 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1747 RRLEARIAHLEEELEEEQSNMELLNDRFRKTTLQVDTLNSELAAERSSGQKSENARQQLERQNKELKAKLQELEGSVKSK 1826
Cdd:COG5278 399 AAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALA 478
|
410 420 430
....*....|....*....|....*....|....*..
gi 148223878 1827 FKATIATLESKIAQLEEQLEQEAKERVASNKLVRRTE 1863
Cdd:COG5278 479 AAAAALAEAEAAAALAAAAALSLALALAALLLAAAEA 515
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1143-1363 |
1.94e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1143 ESEKASRNKAEKQKRDLSEELEALKTELEdtldttAAQQELRTKREQEVAElrkSIEEETRNHEAQIQEMRQRQATALEE 1222
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELE------EAEAALEEFRQKNGLV---DLSEEAKLLLQQLSELESQLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1223 LSEQLEQAKRFKVNLEKNKQSLESDNKelATEVKSLQQMKAESEYKRKKLEGQVQELHAKVLEgdrlradmveksskLQN 1302
Cdd:COG3206 235 LAEAEARLAALRAQLGSGPDALPELLQ--SPVIQQLRAQLAELEAELAELSARYTPNHPDVIA--------------LRA 298
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148223878 1303 ELENVSSLL-EEAEKKGIKLAKDVASMESQLQdtqeLLQEETRQKLNQSSRIRQLEEEKNNL 1363
Cdd:COG3206 299 QIAALRAQLqQEAQRILASLEAELEALQAREA----SLQAQLAQLEARLAELPELEAELRRL 356
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
955-1104 |
1.96e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 955 QVLQNEKKKMQTHVQDLEEQLDEEEAAQKLQLEKVTAE--AKIKKMEEDIL----VLEDQNSKFLKEKKLLEERIAESTS 1028
Cdd:PRK12704 42 RILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRErrNELQKLEKRLLqkeeNLDRKLELLEKREEELEKKEKELEQ 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148223878 1029 QLAEEEEKAKNLAKLKNKQemmISDLEE--RLKKEEKTRQELEKAKRKLdgettdfQDQIAELQAQIEELKLQLAKKE 1104
Cdd:PRK12704 122 KQQELEKKEEELEELIEEQ---LQELERisGLTAEEAKEILLEKVEEEA-------RHEAAVLIKEIEEEAKEEADKK 189
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
868-964 |
2.01e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 868 EELVAKDEEL-LKVKEKQSKVEGELVDMEQKHQQLVEEKNILAEQLHaetELFAEAEEmRARLAIK--KQEMEEILRDL- 943
Cdd:PRK00409 519 NELIASLEELeRELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEED---KLLEEAEK-EAQQAIKeaKKEADEIIKELr 594
|
90 100
....*....|....*....|..
gi 148223878 944 -EIRMEEEEERNQVLQNEKKKM 964
Cdd:PRK00409 595 qLQKGGYASVKAHELIEARKRL 616
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1643-1861 |
2.02e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1643 DFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARASRDDIFAQSKEN------EKKLKGLEAEILQLQEELA---- 1712
Cdd:PRK11281 70 ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTlslrqlESRLAQTLDQLQNAQNDLAeyns 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1713 -------ASERSRR---HAEQERDELADEISNSTSGKSALLDEKR-RLEARiahleeeleeeQSNMELLNDrFRKTTLQV 1781
Cdd:PRK11281 150 qlvslqtQPERAQAalyANSQRLQQIRNLLKGGKVGGKALRPSQRvLLQAE-----------QALLNAQND-LQRKSLEG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1782 DTLNSELAAERSSgQKSENArQQLERQnkelkakLQELEGSVKSKfkatiaTLESKIAQLEEQLEQEAKERVASNKLVRR 1861
Cdd:PRK11281 218 NTQLQDLLQKQRD-YLTARI-QRLEHQ-------LQLLQEAINSK------RLTLSEKTVQEAQSQDEAARIQANPLVAQ 282
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1642-1945 |
2.16e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1642 KDFESQIEAANKGREdaikqlrkLQAQTKDYQRELEEARASRDDIFAQSKENE---KKLKGLEAEILQLQEELAASERSr 1718
Cdd:PRK11281 39 ADVQAQLDALNKQKL--------LEAEDKLVQQDLEQTLALLDKIDRQKEETEqlkQQLAQAPAKLRQAQAELEALKDD- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1719 rhaeqerdelADEISNSTSGKSALldekRRLEARIAHLEEELEEEQSNMellndrfrkttlqvDTLNSELAA-----ERS 1793
Cdd:PRK11281 110 ----------NDEETRETLSTLSL----RQLESRLAQTLDQLQNAQNDL--------------AEYNSQLVSlqtqpERA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1794 SGQKSENAR--QQLERQNKELKAKLQELEGSVKSKFKATIATLESKIAQLEEQLE-----QEA--KERVASNKLVRRTEK 1864
Cdd:PRK11281 162 QAALYANSQrlQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEgntqlQDLlqKQRDYLTARIQRLEH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1865 KLKEVFMQVEDERRhaDQYKEQMEKANTRMKQLKRQLEEAEEEATRANasaRKLQRELDDATEANEVLSREVSTLKNRLR 1944
Cdd:PRK11281 242 QLQLLQEAINSKRL--TLSEKTVQEAQSQDEAARIQANPLVAQELEIN---LQLSQRLLKATEKLNTLTQQNLRVKNWLD 316
|
.
gi 148223878 1945 R 1945
Cdd:PRK11281 317 R 317
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1336-1697 |
2.28e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1336 QELLQEETRQKLNQSSRIRQLEEEKNNLQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLKD 1415
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1416 TEGLGQRLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQIVSNL---------EKKQKKFDQLLAEEKNISARHAEER 1486
Cdd:pfam07888 117 KDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAgaqrkeeeaERKQLQAKLQQTEEELRSLSKEFQE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1487 DRAEADAREKETKAL-----SLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKSKRALDQQVEEM-R 1560
Cdd:pfam07888 197 LRNSLAQRDTQVLQLqdtitTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELhQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1561 TQLEELEDELQgTEDAKLRLEVNmQAMKAQFERDLQTRDEQNEEKKRALVKQVRELEAELEDERKQRamavaIKKKLEMD 1640
Cdd:pfam07888 277 ARLQAAQLTLQ-LADASLALREG-RARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMER-----EKLEVELG 349
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 148223878 1641 MKDFESQIEAANKGREdaikqLRKLQAQTKDYQRELEEARASRDDIFAQSKENEKKL 1697
Cdd:pfam07888 350 REKDCNRVQLSESRRE-----LQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRL 401
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1093-1228 |
2.38e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 43.13 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1093 IEELKLQLAKKEEELQAALARGDEEVLQknntlklVRELQAQIAELQEDLESEKASRNKAEKQ-------KRDLSEELEA 1165
Cdd:pfam05911 690 FEQLKSEKENLEVELASCTENLESTKSQ-------LQESEQLIAELRSELASLKESNSLAETQlkcmaesYEDLETRLTE 762
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148223878 1166 LKTELEdtldttaaqqELRTKREQEVAELrksiEEETRNHEAQIqemrqrqaTALEELSEQLE 1228
Cdd:pfam05911 763 LEAELN----------ELRQKFEALEVEL----EEEKNCHEELE--------AKCLELQEQLE 803
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
1130-1349 |
2.41e-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: 464838 [Multi-domain] Cd Length: 384 Bit Score: 42.36 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1130 ELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDtldttaAQQELRtKREQEVAELRKSIEEETRNHEAQI 1209
Cdd:pfam15742 45 DLKQHNSLLQEENIKIKAELKQAQQKLLDSTKMCSSLTAEWKH------CQQKIR-ELELEVLKQAQSIKSQNSLQEKLA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1210 QEmRQRQATALE---ELSEQLEQAKRFKVN----LEKNKqsLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELHAK 1282
Cdd:pfam15742 118 QE-KSRVADAEEkilELQQKLEHAHKVCLTdtciLEKKQ--LEERIKEASENEAKLKQQYQEEQQKRKLLDQNVNELQQQ 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148223878 1283 V----LEGDRLRADMVEKSSKLQ------NELENVSSLLEEAEKKGIKLAKDVasmeSQLQDTQELLQEETRQKLNQ 1349
Cdd:pfam15742 195 VrslqDKEAQLEMTNSQQQLRIQqqeaqlKQLENEKRKSDEHLKSNQELSEKL----SSLQQEKEALQEELQQVLKQ 267
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1514-1945 |
2.44e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.09 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1514 QDEFERLNKQLRAEMEDLMSSKD---DVGKNVHELEKSKRALDQQVEEMRTQLEELEDELQGTEDAKLRLEVNMQAMKAQ 1590
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKelkNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1591 FERDlqtrdeqnEEKKRALVKQVRELEAELEDERKQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTK 1670
Cdd:TIGR04523 112 IKND--------KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1671 DYQRELEEARASR---DDIFAQSKENEKKLKGLEAEILQLQEELAASERSRRHAEQERDELADEISNSTSGKSALLDEKR 1747
Cdd:TIGR04523 184 NIQKNIDKIKNKLlklELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1748 RLEARIahleeelEEEQSNMELLNDRFRKTTLQVDTLNSELAAERSsgQKSENARQQLERQNKELKAKLQELEgsvkskf 1827
Cdd:TIGR04523 264 KIKKQL-------SEKQKELEQNNKKIKELEKQLNQLKSEISDLNN--QKEQDWNKELKSELKNQEKKLEEIQ------- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1828 kATIATLESKIAQLEEQLEQEAKERVASNKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANTRMKQLKRQLEEAEEE 1907
Cdd:TIGR04523 328 -NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL 406
|
410 420 430
....*....|....*....|....*....|....*...
gi 148223878 1908 ATRANASARKLQRELDDATEANEVLSREVSTLKNRLRR 1945
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
861-1167 |
2.51e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 861 LQVTRQEEELVAKDEELLKVKEKQSKVEGELVDMEQ--KHQQLVEE--------KNILAEQLHAETElfaEAEEMRARLA 930
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQlkeleeklKKYNLEELEKKAE---EYEKLKEKLI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 931 IKKQEMEEILRDLEirmeeeeernqvlqnekkkmqthvqdleeqldeeeAAQKLQLEKVTAEAKIKKMEEDILVLEDqns 1010
Cdd:PRK03918 536 KLKGEIKSLKKELE-----------------------------------KLEELKKKLAELEKKLDELEEELAELLK--- 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1011 kflKEKKLLEERIAESTSQLAEEEEKAKNLAKLKNKQemmiSDLEERLKKEEKTRQELEKAKRKLDGETTDFQdqiaELQ 1090
Cdd:PRK03918 578 ---ELEELGFESVEELEERLKELEPFYNEYLELKDAE----KELEREEKELKKLEEELDKAFEELAETEKRLE----ELR 646
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148223878 1091 AQIEELKLQLAKKE-EELQAALARGDEEVLQKNNTLKLVRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALK 1167
Cdd:PRK03918 647 KELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
993-1208 |
2.52e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 41.52 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 993 AKIKKMEEDILVLEDQNSKFLKEKKLLEERIAesTSQLAEEEEKAKNLAKLKnkqemmISDLEERLKKEEKTRQELEKAK 1072
Cdd:pfam12795 30 DKIDASKQRAAAYQKALDDAPAELRELRQELA--ALQAKAEAAPKEILASLS------LEELEQRLLQTSAQLQELQNQL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1073 RKLDGETTDFQDQIAELQAQIEELKLQLAKKEEELQAALARGdeEVLQKNNTLKLVRELQAQIAELQEdLESEKASRNK- 1151
Cdd:pfam12795 102 AQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPG--EPLSEAQRWALQAELAALKAQIDM-LEQELLSNNNr 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1152 ---AEKQKRDLSEELEALKTELEdtldttAAQQELRTKREQEVAELRKSIEEETRNHEAQ 1208
Cdd:pfam12795 179 qdlLKARRDLLTLRIQRLEQQLQ------ALQELLNEKRLQEAEQAVAQTEQLAEEAAGD 232
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1286-1581 |
2.57e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.11 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1286 GDRLRADMVEKSSKLQNELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQE---ETRQKLNQSSRIRQLEEEKNN 1362
Cdd:pfam15905 26 SQRFRKQKAAESQPNLNNSKDASTPATARKVKSLELKKKSQKNLKESKDQKELEKEiraLVQERGEQDKRLQALEEELEK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1363 LQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVD------DEVGTIEGLEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKT 1436
Cdd:pfam15905 106 VEAKLNAAVREKTSLSASVASLEKQLLELTRVNEllkakfSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1437 KNRLQQelddlmvDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARHAEERDRAEADAREKETKALSLARALDEALEAQDE 1516
Cdd:pfam15905 186 LQVTQK-------NLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDE 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148223878 1517 FERLNKQLRAEMEDLMSSKDDVGKNVHELEKSKralDQQVEEMRTQLEELEDELQGTEDaKLRLE 1581
Cdd:pfam15905 259 IESLKQSLEEKEQELSKQIKDLNEKCKLLESEK---EELLREYEEKEQTLNAELEELKE-KLTLE 319
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1022-1291 |
2.60e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 42.63 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1022 RIAESTSQLAEEEEKAKNLAKLKNKQEmmisdlEERLKKEEKTRQEleKAKRKLDGETTDFQDQIAELQAQIEELKLQLA 1101
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKARFEAR------QARLEREKAAREA--RHKKAAEARAAKDKDAVAAALARVKAKKAAAT 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1102 KKEEELQAALARGDEEVLQKNNTLKLVRELQAQIAELQEDLESEKA-----SRNKAEKQkrdlseELEALKTELEDTLDT 1176
Cdd:PRK05035 504 QPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAvaaaiARAKAKKA------AQQAANAEAEEEVDP 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1177 TAAQQELRTKReqevAELRKSIEEETRNHEAQIQEMRQRQATALEELSEQLEQAKRFKVNLEKNKQSLESDNKELATEVK 1256
Cdd:PRK05035 578 KKAAVAAAIAR----AKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIA 653
|
250 260 270
....*....|....*....|....*....|....*
gi 148223878 1257 slqqmKAeseyKRKKLEGQVQELHAKVLEGDRLRA 1291
Cdd:PRK05035 654 -----RA----KARKAAQQQANAEPEEAEDPKKAA 679
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
997-1196 |
2.60e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 42.00 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 997 KMEEDILVLEdqNSKFLKEKKLLEERIAESTSQLAEEEEKAKNLAKLKNKQ-----EMMISDLEERLKKEEKTRQELEKA 1071
Cdd:pfam15294 78 KLQADISELE--NRELLEQIAEFEEREFTSSNKKPNFELNKPKLEPLNEGGgsallHMEIERLKEENEKLKERLKTLESQ 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1072 KRKLDGETTDFQDQIAELQAQIEELKLQLA-----KKEEELQAALargdeevlqKNNTLKLVRELQAQIAELQEDLESEK 1146
Cdd:pfam15294 156 ATQALDEKSKLEKALKDLQKEQGAKKDVKSnlkeiSDLEEKMAAL---------KSDLEKTLNASTALQKSLEEDLASTK 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 148223878 1147 asrnkaeKQKRDLSEELEALKTELEDTLDTTAAQQELR---TKREQEVAELRK 1196
Cdd:pfam15294 227 -------HELLKVQEQLEMAEKELEKKFQQTAAYRNMKemlTKKNEQIKELRK 272
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1543-1943 |
2.63e-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: 461718 [Multi-domain] Cd Length: 562 Bit Score: 42.71 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1543 HELEKSKRAL---DQQVEEMRTQLEELEDELQGT----EDAKLRLEvNMQAMKAQFERDLQTRDEQNEEKKRALVKQVR- 1614
Cdd:pfam05701 42 LELEKVQEEIpeyKKQSEAAEAAKAQVLEELESTkrliEELKLNLE-RAQTEEAQAKQDSELAKLRVEEMEQGIADEASv 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1615 ELEAELEDERKQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIKqlrklqaqtkdyqrELEEArasrddiFAQSKENE 1694
Cdd:pfam05701 121 AAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIK--------------RAEEA-------VSASKEIE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1695 KKLKGLEAEILQLQEELAASERSRRHAEQERDELA-----DEISNSTSGKSALlDEKRRLEARIAHLEEELEEEQSNMEL 1769
Cdd:pfam05701 180 KTVEELTIELIATKESLESAHAAHLEAEEHRIGAAlareqDKLNWEKELKQAE-EELQRLNQQLLSAKDLKSKLETASAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1770 LNDrfrkttlqvdtLNSELAAERSSGQKSENARQQLERQ-NKELKAKL----QELEGSVKSKFKAT--IATLESKIAQLE 1842
Cdd:pfam05701 259 LLD-----------LKAELAAYMESKLKEEADGEGNEKKtSTSIQAALasakKELEEVKANIEKAKdeVNCLRVAAASLR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1843 EQLEQEaKERVASnklVRRTEKKLKEVFMQVEDERRHADQ----YKEQMEKANTRMKQLKRQLEEAEEEATRANASARKL 1918
Cdd:pfam05701 328 SELEKE-KAELAS---LRQREGMASIAVSSLEAELNRTKSeialVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAA 403
|
410 420
....*....|....*....|....*
gi 148223878 1919 QRELDDATEANEVLSREVSTLKNRL 1943
Cdd:pfam05701 404 REELRKAKEEAEQAKAAASTVESRL 428
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1352-1446 |
2.77e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1352 RIRQLEEEKNNLQEQQEEEEEAR-KSLEKQILSLQSQLIEAKKKVDDEVGTIEGLEEVKKKLLKDTEGLGQRLEEKIIAY 1430
Cdd:COG0542 419 RLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAELE 498
|
90
....*....|....*.
gi 148223878 1431 EKLEKTKNRLQQELDD 1446
Cdd:COG0542 499 EELAELAPLLREEVTE 514
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1250-1440 |
2.78e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1250 ELATEVKSLQQMKAESEYKRKKLEGQVQELHAKVLEGDRLRADMVEKSSKLQNELENVSSLLEEAEKK--GIKLAKDVAS 1327
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgNVRNNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1328 MESQLQdtqellqeetrqklNQSSRIRQLEEEKNNLQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDDEvgtIEGLEE 1407
Cdd:COG1579 94 LQKEIE--------------SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE---LAELEA 156
|
170 180 190
....*....|....*....|....*....|....
gi 148223878 1408 VKKKLLKDTEGLGQRLEEKIIA-YEKLEKTKNRL 1440
Cdd:COG1579 157 ELEELEAEREELAAKIPPELLAlYERIRKRKNGL 190
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1002-1355 |
2.81e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.87 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1002 ILVLEDQNSKFLKEKKLLEERIAESTSQLAEEEEK-AKNLAKLKNKQEMM-----ISDLEERLKKEEKTRQELEKAK--- 1072
Cdd:PRK10246 428 LVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAAlNEMRQRYKEKTQQLadvktICEQEARIKDLEAQRAQLQAGQpcp 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1073 ----------------------RKLDG---ETTDFQDQIAELQAQIEELKLQLAKKEEELQAALArgDEEVLQKnntlkl 1127
Cdd:PRK10246 508 lcgstshpaveayqalepgvnqSRLDAlekEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQ--EEQALTQ------ 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1128 vrELQAQIAEL------QEDLESEKASRNKAEKQKRDLSEELEaLKTELEDTLD-TTAAQQELRTKREQEVAELRK---S 1197
Cdd:PRK10246 580 --QWQAVCASLnitlqpQDDIQPWLDAQEEHERQLRLLSQRHE-LQGQIAAHNQqIIQYQQQIEQRQQQLLTALAGyalT 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1198 IEEE--------TRNHEAQIQEMRQRQATALEE-------LSEQLEQAKrfkvNLEKNKQSLESDN-KELATEVKSLQ-- 1259
Cdd:PRK10246 657 LPQEdeeaswlaTRQQEAQSWQQRQNELTALQNriqqltpLLETLPQSD----DLPHSEETVALDNwRQVHEQCLSLHsq 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1260 -QMKAESEYKRKKLEGQVQELHAKVLEG---------------DRLRADMVEKSSKLQNELENVSSLLEEAEK------- 1316
Cdd:PRK10246 733 lQTLQQQDVLEAQRLQKAQAQFDTALQAsvfddqqaflaalldEETLTQLEQLKQNLENQRQQAQTLVTQTAQalaqhqq 812
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 148223878 1317 ---KGIKLAKDVASMESQLQDTQELLQE------ETRQKLNQSSRIRQ 1355
Cdd:PRK10246 813 hrpDGLDLTVTVEQIQQELAQLAQQLREnttrqgEIRQQLKQDADNRQ 860
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
877-1106 |
2.87e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 877 LLKVKEKQSKVEGELVDMEQKH--------QQLVEEKNILAEQLHAE-----TELFAEAEEMRARLAIKKQEMEEILRDL 943
Cdd:PHA02562 171 LNKDKIRELNQQIQTLDMKIDHiqqqiktyNKNIEEQRKKNGENIARkqnkyDELVEEAKTIKAEIEELTDELLNLVMDI 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 944 EIRMEEEEERNQVLQNEKKKMQthvqdleeqldeeeaaqklQLEKV-----------TAEAKIKKMEEDILVLEDQNSKF 1012
Cdd:PHA02562 251 EDPSAALNKLNTAAAKIKSKIE-------------------QFQKVikmyekggvcpTCTQQISEGPDRITKIKDKLKEL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1013 LKEKKLLEERIAESTSQLAEEEEKAKNLAKLKNKqemmISDLEERLKKEEKTRQELEKAKRKLDGETTDFQDQIAELQAQ 1092
Cdd:PHA02562 312 QHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNK----ISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDE 387
|
250
....*....|....
gi 148223878 1093 IEELKLQLAKKEEE 1106
Cdd:PHA02562 388 LDKIVKTKSELVKE 401
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1452-1625 |
2.92e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic 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: 463796 [Multi-domain] Cd Length: 712 Bit Score: 42.74 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1452 DHQRQIVSNLEKKQKKFDQLLAEEKNISarHAEERDRAEADAREKetkALSLARALDEAL-EAQDEFERLNKQL--RAEM 1528
Cdd:pfam13166 283 EFQNRLQKLIEKVESAISSLLAQLPAVS--DLASLLSAFELDVED---IESEAEVLNSQLdGLRRALEAKRKDPfkSIEL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1529 EDLMSSKDDVGKNVHELEKSKRA-------LDQQVEEMRTQLE-----ELEDELQGTEDAKLRLEvnmqamkAQFErDLQ 1596
Cdd:pfam13166 358 DSVDAKIESINDLVASINELIAKhneitdnFEEEKNKAKKKLRlhlveEFKSEIDEYKDKYAGLE-------KAIN-SLE 429
|
170 180
....*....|....*....|....*....
gi 148223878 1597 TRDEQNEEKKRALVKQVRELEAELEDERK 1625
Cdd:pfam13166 430 KEIKNLEAEIKKLREEIKELEAQLRDHKP 458
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1352-1622 |
3.07e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.83 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1352 RIRQLEEEKNNLQEQQEEEEEARKSLEKQILSL-QSQLIEAKKKVDDEVGTIEGLEEVKKKLLKDTEGLGQRLEEKIIAY 1430
Cdd:pfam00038 19 KVRFLEQQNKLLETKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1431 EKLEKTKNRLQQELDDLM---VDLDHQRQIVSNLEKKQKKFDQllAEEKNISARHAEERDRAEADArekeTKALSLARAL 1507
Cdd:pfam00038 99 TSAENDLVGLRKDLDEATlarVDLEAKIESLKEELAFLKKNHE--EEVRELQAQVSDTQVNVEMDA----ARKLDLTSAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1508 DEaLEAQdeFERLNKQLRAEMEDLMSSK-----DDVGKNVHELEKSKraldQQVEEMRTQLEELEDELQGTEDAKLRLEV 1582
Cdd:pfam00038 173 AE-IRAQ--YEEIAAKNREEAEEWYQSKleelqQAAARNGDALRSAK----EEITELRRTIQSLEIELQSLKKQKASLER 245
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 148223878 1583 NMQAMKAQFERDLQTRDEQNEEKKRALVKQVRELEAELED 1622
Cdd:pfam00038 246 QLAETEERYELQLADYQELISELEAELQETRQEMARQLRE 285
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1468-1901 |
3.13e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1468 FDQLLAEEKNISA----RHAEERdraeadaREKETKALSLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDD------ 1537
Cdd:PRK04863 259 FKHLITESTNYVAadymRHANER-------RVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDleqdyq 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1538 ------------------VGKNVHELEKSKRALDQQ---VEEMRTQLEELEDELQGTEDAKLRLEVNM----QAMKAQfe 1592
Cdd:PRK04863 332 aasdhlnlvqtalrqqekIERYQADLEELEERLEEQnevVEEADEQQEENEARAEAAEEEVDELKSQLadyqQALDVQ-- 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1593 rdlQTRDEQNEEKKRAL-------------VKQVRELEAELEDERKQRAMAV-AIKKKLEMDmkdfesqiEAANKGREDA 1658
Cdd:PRK04863 410 ---QTRAIQYQQAVQALerakqlcglpdltADNAEDWLEEFQAKEQEATEELlSLEQKLSVA--------QAAHSQFEQA 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1659 IKQLRKLQAQTkdyqreleearaSRDDIFAQSKENEKKLKGLEAEILQLQEelaaseRSRRHAEQERDeladeisnstsg 1738
Cdd:PRK04863 479 YQLVRKIAGEV------------SRSEAWDVARELLRRLREQRHLAEQLQQ------LRMRLSELEQR------------ 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1739 ksalLDEKRRLEARIAHLEEELEEEQSNMELLNDRFRKTTLQVDTLNSELA--AERSSGQKSEnaRQQLERQNKELKAKL 1816
Cdd:PRK04863 529 ----LRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSeaRERRMALRQQ--LEQLQARIQRLAARA 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1817 QELEgsvkskfkatiaTLESKIAQLEEQLEQEAKERVASNKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEK------- 1889
Cdd:PRK04863 603 PAWL------------AAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERlsqpggs 670
|
490
....*....|..
gi 148223878 1890 ANTRMKQLKRQL 1901
Cdd:PRK04863 671 EDPRLNALAERF 682
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
982-1284 |
3.33e-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: 42.59 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 982 QKLQLEKVTAEAKIKKMEEDILVLEDQNSKFLKEKKLLEERIAESTSQLAEEE-EKAKNLAKLKNK--QEMMISDLEERL 1058
Cdd:pfam15964 392 KEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEmDVTKVCGEMRYQlnQTKMKKDEAEKE 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1059 KKEEKTR---------QELEKAKRKLDGETTDF-QDQIAELQAQIEELKLQLAKKEEELQAALARGDEEVLQK---NNTL 1125
Cdd:pfam15964 472 HREYRTKtgrqleikdQEIEKLGLELSESKQRLeQAQQDAARAREECLKLTELLGESEHQLHLTRLEKESIQQsfsNEAK 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1126 KLVRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQ-QELRTKREQEVAELrksiEEETRN 1204
Cdd:pfam15964 552 AQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKlEEITQKSRSEVEQL----SQEKEY 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1205 HEAQIQEMRQRQatalEELSEQLEQAKRFKVNLEKNKQSLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELHAKVL 1284
Cdd:pfam15964 628 LQDRLEKLQKRN----EELEEQCVQHGRMHERMKQRLRQLDKHCQATAQQLVQLLSKQNQLFKERQNLTEEVQSLRSQVP 703
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1165-1499 |
3.47e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1165 ALKTELEDTLDTTAAQQELRTKREQEVAELRKSIEEETRNHEAQIQEMRQRQATaLEELSEQLEQAKRFKVNLEKNKQSL 1244
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE-LEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1245 ESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELHAKVLEGDRLRADMVEKSSKLQNELENVSSLLEEAEKKGIKLAKD 1324
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1325 VASMESQLQDTQELLQEETRQKLNQSSRI--RQLEEEKNNLQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDDEVGTI 1402
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRElaEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1403 EGLEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARH 1482
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
330
....*....|....*..
gi 148223878 1483 AEERDRAEADAREKETK 1499
Cdd:COG4372 347 LVGLLDNDVLELLSKGA 363
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1538-1703 |
3.68e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1538 VGKNVHE--LEKSKRALDQQVEEMRTQLEELEDElqgtedAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRALVKQVRE 1615
Cdd:PRK12704 24 VRKKIAEakIKEAEEEAKRILEEAKKEAEAIKKE------ALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1616 LEAELEDERKQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQRE--LEEARA-SRDDIFAQSKE 1692
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEilLEKVEEeARHEAAVLIKE 177
|
170
....*....|.
gi 148223878 1693 NEKKLKgLEAE 1703
Cdd:PRK12704 178 IEEEAK-EEAD 187
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1634-1844 |
3.84e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 42.35 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1634 KKKLEMDMKDFES-----QIEAAN--KGREDAIKQLRKLQAQTKDYQ----------RELEEARASRDDIFAQSKENEKk 1696
Cdd:PRK10929 25 EKQITQELEQAKAaktpaQAEIVEalQSALNWLEERKGSLERAKQYQqvidnfpklsAELRQQLNNERDEPRSVPPNMS- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1697 LKGLEAEILQLQEELAasERSRRhAEQERDElADEISNSTSGKSALLDEKRRL----EARI-AHLEEELEEEQSNMELLN 1771
Cdd:PRK10929 104 TDALEQEILQVSSQLL--EKSRQ-AQQEQDR-AREISDSLSQLPQQQTEARRQlneiERRLqTLGTPNTPLAQAQLTALQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1772 DRFRKTTLQVDTLnsELAaerssgQKSENARQQLER--------QNKELKAKLQELEGSVKS--KFKATIAtLESkIAQL 1841
Cdd:PRK10929 180 AESAALKALVDEL--ELA------QLSANNRQELARlrselakkRSQQLDAYLQALRNQLNSqrQREAERA-LES-TELL 249
|
...
gi 148223878 1842 EEQ 1844
Cdd:PRK10929 250 AEQ 252
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1618-1943 |
4.00e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.37 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1618 AELEDER--KQRAMAVAIKKKLEMDMKDfeSQIEAANKgredAIKQLRKLQA---QTKDYQRELEEARASRDDIFAQSKE 1692
Cdd:COG5022 734 AALEDMRdaKLDNIATRIQRAIRGRYLR--RRYLQALK----RIKKIQVIQHgfrLRRLVDYELKWRLFIKLQPLLSLLG 807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1693 NEKKLKGLEAEILQLQEELAASERSRRHAEQERDELADEISNSTSgkSALLDEKRrleARIAHLEEELEEEQSNMELLND 1772
Cdd:COG5022 808 SRKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFG--RSLKAKKR---FSLLKKETIYLQSAQRVELAER 882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1773 RFrkttlqvdtlnSELAAERSSGQKSENARQQLERQNKELKAKLQELEgSVKSKFK-ATIATLESKI--AQLEEQLEQEA 1849
Cdd:COG5022 883 QL-----------QELKIDVKSISSLKLVNLELESEIIELKKSLSSDL-IENLEFKtELIARLKKLLnnIDLEEGPSIEY 950
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1850 KERVASNKLvRRTEKKLKEVFMQVEDERRHADQYKEQMEKANTRMKQLKRQL---EEAEEEATRANASARKLQRELDDAT 1926
Cdd:COG5022 951 VKLPELNKL-HEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELaelSKQYGALQESTKQLKELPVEVAELQ 1029
|
330
....*....|....*..
gi 148223878 1927 EANEVLSREVSTLKNRL 1943
Cdd:COG5022 1030 SASKIISSESTELSILK 1046
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
1013-1111 |
4.05e-03 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 41.95 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1013 LKEK-KLLEERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKKEEKTRQELEKAKRkldgettdfqdQIAELQA 1091
Cdd:smart00435 282 LQEKiKALKYQLKRLKKMILLFEMISDLKRKLKSKFERDNEKLDAEVKEKKKEKKKEEKKKK-----------QIERLEE 350
|
90 100
....*....|....*....|
gi 148223878 1092 QIEELKLQLAKKEEELQAAL 1111
Cdd:smart00435 351 RIEKLEVQATDKEENKTVAL 370
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1019-1198 |
4.23e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.58 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1019 LEERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKK------EEKTRQELEKaKRKLDGETTDFQDQIAELQAQ 1092
Cdd:COG1842 35 MEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLalekgrEDLAREALER-KAELEAQAEALEAQLAQLEEQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1093 IEELKLQLAKKEEELQAALARGDEEVLQKNntlklVRELQAQIAELQEDLESEKASR--NKAEKQKRDLSEELEALKT-E 1169
Cdd:COG1842 114 VEKLKEALRQLESKLEELKAKKDTLKARAK-----AAKAQEKVNEALSGIDSDDATSalERMEEKIEEMEARAEAAAElA 188
|
170 180
....*....|....*....|....*....
gi 148223878 1170 LEDTLDTTAAQQELRTKREQEVAELRKSI 1198
Cdd:COG1842 189 AGDSLDDELAELEADSEVEDELAALKAKM 217
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1324-1516 |
4.29e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1324 DVASMESQLQDTQELLQEETRQKLNQSSRIRQLEEEKNNLQEQQEEEEEARKSLEKQILSLQSQLIEAKKKVDDEVGT-- 1401
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1402 ---------------------IEGLEEVKKKLLKDTEGLGQRLEEKiiayEKLEKTKNRLQQELDDLMVDLDHQRQIVSN 1460
Cdd:COG3883 97 rsggsvsyldvllgsesfsdfLDRLSALSKIADADADLLEELKADK----AELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 148223878 1461 LEKKQKKFDQLLAEEKNISARHAEERDRAEADAREKETKALSLARALDEALEAQDE 1516
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1593-1901 |
4.77e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.87 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1593 RDLQTRDEQNEEKKRALVKQVRELEAELEDERKQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKDY 1672
Cdd:COG5185 176 LKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1673 QRELEEARASRDDIFAQSKENEKKLKGLEAEILQLQEELaaSERSRRHAEQERDELADEISNSTSGKSALLDEkrrLEAR 1752
Cdd:COG5185 256 EKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENT--KEKIAEYTKSIDIKKATESLEEQLAAAEAEQE---LEES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1753 IAHLEEELEEEQSNMELLNDRFRKTTLQVDTLNSELAAERSSGQKSENARQ---QLERQNKELKAKLQELEGSVKSKFKA 1829
Cdd:COG5185 331 KRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSfkdTIESTKESLDEIPQNQRGYAQEILAT 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1830 ---TIATLESKIAQLEEQLEQEAKERVASNKLVRRTEKKLKEVFMQVEDERRHADQYK---------EQMEKANTRMKQL 1897
Cdd:COG5185 411 ledTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAydeinrsvrSKKEDLNEELTQI 490
|
....
gi 148223878 1898 KRQL 1901
Cdd:COG5185 491 ESRV 494
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1175-1346 |
5.26e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 40.27 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1175 DTTAAQQELRTKREQEVAELRKsIEEETRNHEAQIQEMRQRQATALEELSEQLEQAKRFKVNLEKNKQSLE---SDNKEL 1251
Cdd:pfam13851 19 DITRNNLELIKSLKEEIAELKK-KEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKnlkARLKVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1252 ATEVKSLQQMKAESEYKRKKLEGQVQELHAKvlegDRLRADMVEKSSKLQNEL--ENVSSLLEEAEKKGIKLAKDVASME 1329
Cdd:pfam13851 98 EKELKDLKWEHEVLEQRFEKVERERDELYDK----FEAAIQDVQQKTGLKNLLleKKLQALGETLEKKEAQLNEVLAAAN 173
|
170 180
....*....|....*....|
gi 148223878 1330 ---SQLQDTQELLQEETRQK 1346
Cdd:pfam13851 174 ldpDALQAVTEKLEDVLESK 193
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
991-1351 |
5.37e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 991 AEAKIKKMEEDILVLEDQNSKFLKE--KKL----LEERIAESTSQLAEEEEKAKN----LAKLKNKQEMMISDLEERLKK 1060
Cdd:PRK11281 92 APAKLRQAQAELEALKDDNDEETREtlSTLslrqLESRLAQTLDQLQNAQNDLAEynsqLVSLQTQPERAQAALYANSQR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1061 EEKTRQELEKAKrklDGETTDFQDQIAELQAQIEELKLQLAKKEEELQAALARGDEEVLQKNNTLKLVRELQAQIAELQE 1140
Cdd:PRK11281 172 LQQIRNLLKGGK---VGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1141 DLESE--KASRNKAEK-QKRDLSEELEA---LKTELE-------DTLDTTAA-----QQELRTKReqevaELRKSIEEEt 1202
Cdd:PRK11281 249 AINSKrlTLSEKTVQEaQSQDEAARIQAnplVAQELEinlqlsqRLLKATEKlntltQQNLRVKN-----WLDRLTQSE- 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1203 RNHEAQIQEMrqrQATALeeLSEQLEQakrfkvnlekNKQSLESD--NKELATEVKSLQ-----------QMKAESEYKR 1269
Cdd:PRK11281 323 RNIKEQISVL---KGSLL--LSRILYQ----------QQQALPSAdlIEGLADRIADLRleqfeinqqrdALFQPDAYID 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1270 KKLEGQVQE----LHAKVLEGDRLRADMVEKSSKLQNELENVSSLLEEAEKkgiklakdvasmesQLQDTQELLQEetrq 1345
Cdd:PRK11281 388 KLEAGHKSEvtdeVRDALLQLLDERRELLDQLNKQLNNQLNLAINLQLNQQ--------------QLLSVSDSLQS---- 449
|
....*.
gi 148223878 1346 KLNQSS 1351
Cdd:PRK11281 450 TLTQQI 455
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
1292-1617 |
5.67e-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: 464838 [Multi-domain] Cd Length: 384 Bit Score: 41.20 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1292 DMVEKSSKLQNELENVSSLLEEAEKKGIKLAKDVASMESQLQDTQELLQEETRQKLNQSSRIRQleeeKNNLQEQQEEEE 1371
Cdd:pfam15742 45 DLKQHNSLLQEENIKIKAELKQAQQKLLDSTKMCSSLTAEWKHCQQKIRELELEVLKQAQSIKS----QNSLQEKLAQEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1372 EARKSLEKQILSLQSQLIEAKKKVDDEVGTIEG--LEEVKKKLLKDTEGLGQRLEEKIIAYEKLEKTKNRLQQELDDLMV 1449
Cdd:pfam15742 121 SRVADAEEKILELQQKLEHAHKVCLTDTCILEKkqLEERIKEASENEAKLKQQYQEEQQKRKLLDQNVNELQQQVRSLQD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1450 DLDHQRQIVSNLEKKQKKFDQLLAEEKNisarhaEERDRAEA-DAREKETKALSLARALDEALeaQDEFERLNKQLRAEM 1528
Cdd:pfam15742 201 KEAQLEMTNSQQQLRIQQQEAQLKQLEN------EKRKSDEHlKSNQELSEKLSSLQQEKEAL--QEELQQVLKQLDVHV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1529 EDlMSSKDDVGKNvhELEKSKRALDQQVEEMRTQLEELEDELQGtedaklrLEVNMQAMKAqFERDLQTRDEQNEEKKRA 1608
Cdd:pfam15742 273 RK-YNEKHHHHKA--KLRRAKDRLVHEVEQRDERIKQLENEIGI-------LQQQSEKEKA-FQKQVTAQNEILLLEKRK 341
|
....*....
gi 148223878 1609 LVKQVRELE 1617
Cdd:pfam15742 342 LLEQLTEQE 350
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
993-1173 |
5.98e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 40.77 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 993 AKIKKMEEDILVLEdQNSKFLKEKKLLEERIAESTSQLAEEEEKAKNLAKLKNKQEMMISDLEERLKKEEKTRQELEKAK 1072
Cdd:PRK06669 2 PKVIFKRSNVINKE-KLKTHEIQKYRFKVLSIKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFEIVEAAEEEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1073 RKLDGETTDFQDQIAELQAQIEELKLQLAK-KEEELQAALARGDEEVLQKNNtlklvrelqaqiAELQEDLESEKASRNK 1151
Cdd:PRK06669 81 EELLKKTDEASSIIEKLQMQIEREQEEWEEeLERLIEEAKAEGYEEGYEKGR------------EEGLEEVRELIEQLNK 148
|
170 180
....*....|....*....|...
gi 148223878 1152 -AEKQKRDLSEELEALKTELEDT 1173
Cdd:PRK06669 149 iIEKLIKKREEILESSEEEIVEL 171
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1085-1251 |
6.35e-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: 462536 [Multi-domain] Cd Length: 176 Bit Score: 39.53 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1085 QIAELQAQIEELKLQLAKKEEELQAALARGDEEVLQKNNTLklVRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELE 1164
Cdd:pfam08614 11 RLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSAS--IQSLEQLLAQLREELAELYRSRGELAQRLVDLNEELQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1165 ALKTELEDTLDTTAAQQELRTKREQEVAELRKSIEEETRNHEAQIQEMrqrqatalEELSEQLEQAkrfkvnlEKNKQSL 1244
Cdd:pfam08614 89 ELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDEL--------VALQLQLNMA-------EEKLRKL 153
|
....*..
gi 148223878 1245 ESDNKEL 1251
Cdd:pfam08614 154 EKENREL 160
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1421-1683 |
6.81e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1421 QRLEEKIiayEKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDqllaeekniSARHAEERDRAEADAREKETKa 1500
Cdd:COG2433 409 TEEEEEI---RRLEEQVERLEAEVEELEAELEEKDERIERLERELSEAR---------SEERREIRKDREISRLDREIE- 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1501 lSLARALDEALEAQDEFERLNKQLRAEMEDLMSSKDDVGKNVHELEKSK-RALDQQVEEMRTQLEELEDELQGTEDAKLR 1579
Cdd:COG2433 476 -RLERELEEERERIEELKRKLERLKELWKLEHSGELVPVKVVEKFTKEAiRRLEEEYGLKEGDVVYLRDASGAGRSTAEL 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1580 LEvnmqamkaqferdlqtrdeqnEEKKRALVKQvRELEAELEDERKQRAMAVAIKKKLEMDMKD-----FESQIEAANKG 1654
Cdd:COG2433 555 LA---------------------EAGPRAVIVP-GELSEAADEVLFEEGIPVLPAEDVTIQEVDdlavvDEEELEAAIED 612
|
250 260
....*....|....*....|....*....
gi 148223878 1655 REDaIKQLRKLQAQTKDYQRELEEARASR 1683
Cdd:COG2433 613 WEE-RAEERRREKKAEMLERLISEYRAER 640
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1038-1387 |
7.35e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 41.15 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1038 KNLAKLKNKQEMMISDLEERLKKE--EKTRQELEKAKRKLDGETTDFQDQIAELQAQIEELKLQLAKKEEE--------- 1106
Cdd:NF033838 91 KKLSDIKTEYLYELNVLKEKSEAEltSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEdrrnyptnt 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1107 ---LQAALARGDEEVlqKNNTLKLVREL------QAQIAELQEDLESEKASRNKAEKQKRDLSE-ELEA-------LKTE 1169
Cdd:NF033838 171 yktLELEIAESDVEV--KKAELELVKEEakeprdEEKIKQAKAKVESKKAEATRLEKIKTDREKaEEEAkrradakLKEA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1170 LEDTLDTT-----------AAQQELRT--KREQEVAELRKSIEEET-----RNHEAQIQEMRQRQATALEELSEQLEQAK 1231
Cdd:NF033838 249 VEKNVATSeqdkpkrrakrGVLGEPATpdKKENDAKSSDSSVGEETlpspsLKPEKKVAEAEKKVEEAKKKAKDQKEEDR 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1232 R-FKVNLEKnkqSLESDNKELATEVKSLQQMKAESEYKRKKLEGQVQELHAKVlEGDRLRADMVEKSSKLQNELEnvssl 1310
Cdd:NF033838 329 RnYPTNTYK---TLELEIAESDVKVKEAELELVKEEAKEPRNEEKIKQAKAKV-ESKKAEATRLEKIKTDRKKAE----- 399
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148223878 1311 lEEAEKKGIKLAKDVASMESQLQDTQELLQEETRQKLNQSSRirQLEEEKNNlqEQQEEEEEARKSLEKQILSLQSQ 1387
Cdd:NF033838 400 -EEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEKPAE--QPKAEKPA--DQQAEEDYARRSEEEYNRLTQQQ 471
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1780-1943 |
7.86e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1780 QVDTLNSELAAERSSGQKSENARQQLERQNKELKAKLQELEGSvkskfkATIATLESKIAQLEEQLEQEAKERVASNKLV 1859
Cdd:COG3206 220 QLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS------PVIQQLRAQLAELEAELAELSARYTPNHPDV 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1860 RRTEKKLKEVFMQVEDE-RRHADQYKEQMEKANTRMKQLKRQleeaEEEATRANASARKLQRELDDateanevLSREVST 1938
Cdd:COG3206 294 IALRAQIAALRAQLQQEaQRILASLEAELEALQAREASLQAQ----LAQLEARLAELPELEAELRR-------LEREVEV 362
|
....*
gi 148223878 1939 LKNRL 1943
Cdd:COG3206 363 ARELY 367
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1120-1375 |
8.09e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1120 QKNNTLKLVRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELRKSIE 1199
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1200 EetrnHEAQIQEMRQrQATALEELSEQLEQAKRFKVNLEKNKQSLE----------SDNKELATEVKSLQQM---KAESE 1266
Cdd:COG1340 82 E----LNEKLNELRE-ELDELRKELAELNKAGGSIDKLRKEIERLEwrqqtevlspEEEKELVEKIKELEKElekAKKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1267 YKRKKLEGQVQELHAKVLEGDRLRADMVEKSSKLQNELENVSSLLEEAEkkgiKLAKDVASMESQLQDTQELLQEETRQK 1346
Cdd:COG1340 157 EKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEAD----ELRKEADELHKEIVEAQEKADELHEEI 232
|
250 260
....*....|....*....|....*....
gi 148223878 1347 LNQSSRIRQLEEEKNNLQEQQEEEEEARK 1375
Cdd:COG1340 233 IELQKELRELRKELKKLRKKQRALKREKE 261
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1022-1189 |
8.15e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.48 E-value: 8.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1022 RIAESTSQLAEEEEKAkNLAKLKNKQEmmisdleeRLKKEEKTRQELEKAKRKLDGETTDFQDQIAELQAQIEELKLQLA 1101
Cdd:pfam00529 50 QLDPTDYQAALDSAEA-QLAKAQAQVA--------RLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1102 KKEEELQAALARGDEEVLQKNntlKLVrELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEAL--KTELEDTLDTTAA 1179
Cdd:pfam00529 121 QAQIDLARRRVLAPIGGISRE---SLV-TAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEvrSELSGAQLQIAEA 196
|
170
....*....|
gi 148223878 1180 QQELRTKREQ 1189
Cdd:pfam00529 197 EAELKLAKLD 206
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1545-1749 |
8.18e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 8.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1545 LEKSK-RALDQQVEEMRTQLEELEDELQGTEDAKLRLEvnmqAMKAQFERDLQTRDEQNEEKKRALVKQVRELEAELED- 1622
Cdd:PHA02562 171 LNKDKiRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQR----KKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNl 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1623 ERKQRAMAVAIKK------KLEMDMKDFESQIEAANKGR---------EDAIKQLRKLQAQTKDYQRELEEARASRDD-- 1685
Cdd:PHA02562 247 VMDIEDPSAALNKlntaaaKIKSKIEQFQKVIKMYEKGGvcptctqqiSEGPDRITKIKDKLKELQHSLEKLDTAIDEle 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148223878 1686 -IFAQSKENEKKLKGLEAEILQLQEELAASERSRRHAEQERDELADEISNSTSGKSALLDEKRRL 1749
Cdd:PHA02562 327 eIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1020-1239 |
8.80e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.01 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1020 EERIAESTSQLAEEEEKAKNLAKLK-NKQEMMISDLEERLKKEEKTRQELEKAKRKLDGETTDFQDQIAELQAQIEELKL 1098
Cdd:pfam02029 117 KEEKRDSRLGRYKEEETEIREKEYQeNKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1099 QLAKKEEELQAALARGDEEVLQKNNTLKLVRELQAQIAELQEDLESEKASRNKAEKQKRDL----SEELEALKTEledtl 1174
Cdd:pfam02029 197 FLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRqekeSEEFEKLRQK----- 271
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148223878 1175 dttaaQQElrtkREQEVAELRKSIEEETRNHEAqiQEMRQRQATALEELSEQlEQAKRFKVNLEK 1239
Cdd:pfam02029 272 -----QQE----AELELEELKKKREERRKLLEE--EEQRRKQEEAERKLREE-EEKRRMKEEIER 324
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1058-1203 |
8.87e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1058 LKKEEKTRQELEKAKRKLDGETtdfqdQIAELQAQIEELKLQ------LAKKEEELQAALARgdeeVLQKNNTLKlvREL 1131
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIK-----KEALLEAKEEIHKLRnefekeLRERRNELQKLEKR----LLQKEENLD--RKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1132 QAqIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDT----TAAQ------QELRTKREQEVAELRKSIEEE 1201
Cdd:PRK12704 103 EL-LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisglTAEEakeillEKVEEEARHEAAVLIKEIEEE 181
|
..
gi 148223878 1202 TR 1203
Cdd:PRK12704 182 AK 183
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
902-1228 |
9.31e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 40.67 E-value: 9.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 902 VEEKNILAEQLHAETELFAEAEEMRARLAIKKQEMEEILRDLEIRMEEEEERNQVLQNEKKKMQTHVQDLEEQLDEEEAA 981
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 982 QKLQLEkvtAEAKIKKMEEDILVLEDQNSKFLKEKKLLEERIAEstsqlAEEEEKAKNLAKLKNKQEMMISDLEERLKKE 1061
Cdd:pfam13868 108 ERIQEE---DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKE-----EEREEDERILEYLKEKAEREEEREAEREEIE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1062 EKTRQELEKAKRKldgettdfQDQIAELQAQIEELKLQLAKKEEELQAALARGDEEVLQKNNTLKLVRELQAQIAELQed 1141
Cdd:pfam13868 180 EEKEREIARLRAQ--------QEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKE-- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1142 lesekasRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELRKSIEEETRNHEAQIQEMRQRQATALE 1221
Cdd:pfam13868 250 -------RRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLRE 322
|
....*..
gi 148223878 1222 ELSEQLE 1228
Cdd:pfam13868 323 EEAERRE 329
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1603-1938 |
9.61e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 9.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1603 EEKKRALVKQVRELEAELEDERKQRAMAVAIKKKLEMDMKDFESQIEAANKGREDAIKQLRKLQAQTKDYQRELEEARAS 1682
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1683 RDDIFAQSKENEKKLKGLEAEILQLQEELAASERSRRHAEQERDELADEISNSTSGKSALLDEKRRLEARIAHLEEELEE 1762
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1763 EQSNMELLNDRFRKTTLQVDTLNSELAAERSSGQKSENARQQLERQNKELKAKLQELEGSVKSKFKATIATLESKIAQLE 1842
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223878 1843 EQLEQEAKERVASNKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANTRMKQLKRQLEEAEEEATRANASARKLQREL 1922
Cdd:COG4372 270 EKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVG 349
|
330
....*....|....*.
gi 148223878 1923 DDATEANEVLSREVST 1938
Cdd:COG4372 350 LLDNDVLELLSKGAEA 365
|
|
| |
