|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
101-768 |
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: 1279.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITG 180
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 181 ESGAGKTVNTKRVIQYFATVAVQGPEKKKEqasGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSG 260
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKES---GKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 261 KLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEMTLITTNPYDFPMCSQGQITVASIDDKEELVATDTAI 340
Cdd:cd01377 158 KIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 341 DILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKGQT 420
Cdd:cd01377 238 DILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 421 VPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMFVL 500
Cdd:cd01377 318 KEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 501 EQEEYKKEGIVWEFIDFGMDLAACIELIEKP-LGIFSILEEECMFPKATDTSFKNKLYDQHLGKCNAFQKPKPakGKAEA 579
Cdd:cd01377 398 EQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKP--KKSEA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 580 HFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPVVEETgGGKKGGKKKGGSMQTVSSQFRENLGK 659
Cdd:cd01377 476 HFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESG-GGGGKKKKKGGSFRTVSQLHKEQLNK 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 660 LMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASVIPEGQFiD 739
Cdd:cd01377 555 LMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFD-D 633
|
650 660
....*....|....*....|....*....
gi 288856329 740 NKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd01377 634 GKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
101-768 |
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: 1229.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITG 180
Cdd:cd14913 1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 181 ESGAGKTVNTKRVIQYFATVAVQGPEKKKEQAsgKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSG 260
Cdd:cd14913 81 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDS--KMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 261 KLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEMTLITTNPYDFPMCSQGQITVASIDDKEELVATDTAI 340
Cdd:cd14913 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 341 DILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKGQT 420
Cdd:cd14913 239 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 421 VPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMFVL 500
Cdd:cd14913 319 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 501 EQEEYKKEGIVWEFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKCNAFQKPKPAKGKAEAH 580
Cdd:cd14913 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 581 FSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYP--PVVEETGGGKKGGKKKGGSMQTVSSQFRENLG 658
Cdd:cd14913 479 FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYAtfATADADSGKKKVAKKKGSSFQTVSALFRENLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 659 KLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASVIPEGQFI 738
Cdd:cd14913 559 KLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFI 638
|
650 660 670
....*....|....*....|....*....|
gi 288856329 739 DNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd14913 639 DSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
101-768 |
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: 1156.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITG 180
Cdd:cd14923 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 181 ESGAGKTVNTKRVIQYFATVAVQGpEKKKEQASGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSG 260
Cdd:cd14923 81 ESGAGKTVNTKRVIQYFATIAVTG-DKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 261 KLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEMTLITTNPYDFPMCSQGQITVASIDDKEELVATDTAI 340
Cdd:cd14923 160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 341 DILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKGQT 420
Cdd:cd14923 240 DILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 421 VPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMFVL 500
Cdd:cd14923 320 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 501 EQEEYKKEGIVWEFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKCNAFQKPKPAKGKAEAH 580
Cdd:cd14923 400 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 581 FSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPVVE----ETGGGKKGGKKKGGSMQTVSSQFREN 656
Cdd:cd14923 480 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGaeagDSGGSKKGGKKKGSSFQTVSAVFREN 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 657 LGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASVIPEGQ 736
Cdd:cd14923 560 LNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQ 639
|
650 660 670
....*....|....*....|....*....|..
gi 288856329 737 FIDNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd14923 640 FIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
101-768 |
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: 1148.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITG 180
Cdd:cd14915 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 181 ESGAGKTVNTKRVIQYFATVAVQGPEKKKEQASGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSG 260
Cdd:cd14915 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 261 KLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEMTLITTNPYDFPMCSQGQITVASIDDKEELVATDTAI 340
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 341 DILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKGQT 420
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 421 VPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMFVL 500
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 501 EQEEYKKEGIVWEFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKCNAFQKPKPAKGKAEAH 580
Cdd:cd14915 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 581 FSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYP---PVVEETGGGKKGGKKKGGSMQTVSSQFRENL 657
Cdd:cd14915 481 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSggqTAEAEGGGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 658 GKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASVIPEGQF 737
Cdd:cd14915 561 NKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 288856329 738 IDNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd14915 641 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
101-768 |
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: 1146.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITG 180
Cdd:cd14910 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 181 ESGAGKTVNTKRVIQYFATVAVQGPEKKKEQASGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSG 260
Cdd:cd14910 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 261 KLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEMTLITTNPYDFPMCSQGQITVASIDDKEELVATDTAI 340
Cdd:cd14910 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 341 DILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKGQT 420
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 421 VPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMFVL 500
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 501 EQEEYKKEGIVWEFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKCNAFQKPKPAKGKAEAH 580
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 581 FSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPVV---EETGGGKKGGKKKGGSMQTVSSQFRENL 657
Cdd:cd14910 481 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAaaeAEEGGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 658 GKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASVIPEGQF 737
Cdd:cd14910 561 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 288856329 738 IDNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd14910 641 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
101-768 |
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: 1129.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITG 180
Cdd:cd14918 1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 181 ESGAGKTVNTKRVIQYFATVAVQGPEKKKEqaSGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSG 260
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEE--SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 261 KLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEMTLITTNPYDFPMCSQGQITVASIDDKEELVATDTAI 340
Cdd:cd14918 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 341 DILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKGQT 420
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 421 VPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMFVL 500
Cdd:cd14918 319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 501 EQEEYKKEGIVWEFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKCNAFQKPKPAKGKAEAH 580
Cdd:cd14918 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 581 FSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPV--VEETGGGKKGGKKKGGSMQTVSSQFRENLG 658
Cdd:cd14918 479 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYasAEADSGAKKGAKKKGSSFQTVSALFRENLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 659 KLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASVIPEGQFI 738
Cdd:cd14918 559 KLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFI 638
|
650 660 670
....*....|....*....|....*....|
gi 288856329 739 DNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd14918 639 DSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
101-768 |
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: 1118.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITG 180
Cdd:cd14912 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 181 ESGAGKTVNTKRVIQYFATVAVQGPEKKKEQASGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSG 260
Cdd:cd14912 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 261 KLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEMTLITTNPYDFPMCSQGQITVASIDDKEELVATDTAI 340
Cdd:cd14912 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 341 DILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKGQT 420
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 421 VPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMFVL 500
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 501 EQEEYKKEGIVWEFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKCNAFQKPKPAKGKAEAH 580
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 581 FSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPVVEETGG-----GKKGGKKKGGSMQTVSSQFRE 655
Cdd:cd14912 481 FSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGAsagggAKKGGKKKGSSFQTVSALFRE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 656 NLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASVIPEG 735
Cdd:cd14912 561 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 640
|
650 660 670
....*....|....*....|....*....|...
gi 288856329 736 QFIDNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd14912 641 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
102-768 |
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: 1112.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 102 SVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITGE 181
Cdd:cd14927 2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 182 SGAGKTVNTKRVIQYFATVAVQG--PEKKKEQASGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTS 259
Cdd:cd14927 82 SGAGKTVNTKRVIQYFAIVAALGdgPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 260 GKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEMTLITTNPYDFPMCSQGQITVASIDDKEELVATDTA 339
Cdd:cd14927 162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDHA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 340 IDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKGQ 419
Cdd:cd14927 242 MDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 420 TVPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMFV 499
Cdd:cd14927 322 SVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 500 LEQEEYKKEGIVWEFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKCNAFQKPKP-AKGKAE 578
Cdd:cd14927 402 LEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPdKKRKYE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 579 AHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPVV-----EETGGGKKGGKKKGGSMQTVSSQF 653
Cdd:cd14927 482 AHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVgsdstEDPKSGVKEKRKKAASFQTVSQLH 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 654 RENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASVIP 733
Cdd:cd14927 562 KENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIP 641
|
650 660 670
....*....|....*....|....*....|....*
gi 288856329 734 EGQFIDNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd14927 642 DDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
101-768 |
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: 1063.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITG 180
Cdd:cd14917 1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 181 ESGAGKTVNTKRVIQYFATVAVQGPEKKKEQASGKmqGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSG 260
Cdd:cd14917 81 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 261 KLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEMTLITTNPYDFPMCSQGQITVASIDDKEELVATDTAI 340
Cdd:cd14917 159 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 341 DILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKGQT 420
Cdd:cd14917 239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 421 VPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMFVL 500
Cdd:cd14917 319 VQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 501 EQEEYKKEGIVWEFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKCNAFQKPKPAKGKAEAH 580
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 581 FSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPV--VEETGGGKKGGKKKGGSMQTVSSQFRENLG 658
Cdd:cd14917 479 FSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYagADAPIEKGKGKAKKGSSFQTVSALHRENLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 659 KLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASVIPEGQFI 738
Cdd:cd14917 559 KLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 638
|
650 660 670
....*....|....*....|....*....|
gi 288856329 739 DNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd14917 639 DSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
101-768 |
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: 1060.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITG 180
Cdd:cd14916 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 181 ESGAGKTVNTKRVIQYFATVAVQGPEKKKEQASGKmQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSG 260
Cdd:cd14916 81 ESGAGKTVNTKRVIQYFASIAAIGDRSKKENPNAN-KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 261 KLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEMTLITTNPYDFPMCSQGQITVASIDDKEELVATDTAI 340
Cdd:cd14916 160 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 341 DILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKGQT 420
Cdd:cd14916 240 DVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 421 VPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMFVL 500
Cdd:cd14916 320 VQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 501 EQEEYKKEGIVWEFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKCNAFQKPKPAKGKAEAH 580
Cdd:cd14916 400 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 581 FSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATL---YPPVVEETGGGKKGGKKKGGSMQTVSSQFRENL 657
Cdd:cd14916 480 FSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLfstYASADTGDSGKGKGGKKKGSSFQTVSALHRENL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 658 GKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASVIPEGQF 737
Cdd:cd14916 560 NKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQF 639
|
650 660 670
....*....|....*....|....*....|.
gi 288856329 738 IDNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd14916 640 IDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
101-768 |
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: 1008.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITG 180
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 181 ESGAGKTVNTKRVIQYFATVAVQGPEKKKeqasgkmQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSG 260
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKK-------LGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 261 KLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKpELIEMTLITTNPYDFPMCSQGQITVASIDDKEELVATDTAI 340
Cdd:cd14929 154 MLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 341 DILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKGQT 420
Cdd:cd14929 233 DILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 421 VPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMFVL 500
Cdd:cd14929 313 IEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 501 EQEEYKKEGIVWEFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKCNAFQKPKPAKGKAEAH 580
Cdd:cd14929 393 EQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAH 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 581 FSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPP--VVEETGGGKKGGKKKGGSMQTVSSQFRENLG 658
Cdd:cd14929 473 FELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENyiSTDSAIQFGEKKRKKGASFQTVASLHKENLN 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 659 KLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASVIPEGQFI 738
Cdd:cd14929 553 KLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKFV 632
|
650 660 670
....*....|....*....|....*....|
gi 288856329 739 DNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd14929 633 SSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
89-768 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1000.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 89 IEDMAMMTHLNEPSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFML 168
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 169 TDRENQSVLITGESGAGKTVNTKRVIQYFATVAVQGPEKKKeqasgkmqGSLEDQIIAANPLLEAYGNAKTVRNDNSSRF 248
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNV--------GRLEEQILQSNPILEAFGNAKTVRNNNSSRF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 249 GKFIRIHFGTSGKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEmTLITTNPYDFPMCSQ-GQITVASI 327
Cdd:pfam00063 153 GKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKK-ELRLTNPKDYHYLSQsGCYTIDGI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 328 DDKEELVATDTAIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGTEEADKIGYLLGLNSADMLKALCYPR 407
Cdd:pfam00063 232 DDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 408 VKVGNEFVTKGQTVPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQ-QRNFFIGVLDIAGFEIFDFNSMEQLCINFTN 486
Cdd:pfam00063 312 IKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTiEKASFIGVLDIYGFEIFEKNSFEQLCINYVN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 487 EKLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGmDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYDQHlGKCN 565
Cdd:pfam00063 392 EKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 566 AFQKPKPakgKAEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPVVEETGGGKKGGKKKG-- 643
Cdd:pfam00063 470 HFQKPRL---QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTpk 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 644 ----GSMQTVSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYAD 719
Cdd:pfam00063 547 rtkkKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQE 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 288856329 720 FKQRYKVLNASVIPEGqFIDNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:pfam00063 627 FVQRYRILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
82-780 |
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: 965.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 82 NPPKFDKIEDMAMMTHLNEPSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSD 161
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 162 NAYQFMLTDRENQSVLITGESGAGKTVNTKRVIQYFATVAvqgpekkkeqASGKMQGSLEDQIIAANPLLEAYGNAKTVR 241
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVS----------GSNTEVGSVEDQILESNPILEAFGNAKTLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 242 NDNSSRFGKFIRIHFGTSGKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEmTLITTNPYDFPMCSQGQ 321
Cdd:smart00242 151 NNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKK-ELGLKSPEDYRYLNQGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 322 -ITVASIDDKEELVATDTAIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQA-EPDGTEEADKIGYLLGLNSADM 399
Cdd:smart00242 230 cLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEEL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 400 LKALCYPRVKVGNEFVTKGQTVPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNFFIGVLDIAGFEIFDFNSMEQ 479
Cdd:smart00242 310 EKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 480 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGmDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYd 558
Cdd:smart00242 390 LCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKLN- 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 559 QHLGKCNAFQKPKPakgKAEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPVVEETgggkkg 638
Cdd:smart00242 468 QHHKKHPHFSKPKK---KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNA------ 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 639 gkKKGGSMQTVSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYA 718
Cdd:smart00242 539 --GSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFD 616
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 288856329 719 DFKQRYKVLNASVIPEGQFiDNKKASEKLLGSIDVNHDEYRFGHTKVFFKAGLLGTLEEMRD 780
Cdd:smart00242 617 EFLQRYRVLLPDTWPPWGG-DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
102-768 |
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: 965.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 102 SVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITGE 181
Cdd:cd14934 2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 182 SGAGKTVNTKRVIQYFATVAVQGpekkKEQASGKmqGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGK 261
Cdd:cd14934 82 SGAGKTENTKKVIQYFANIGGTG----KQSSDGK--GSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 262 LASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEMTLITTNPYDFPMCSQGQITVASIDDKEELVATDTAID 341
Cdd:cd14934 156 LAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 342 ILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKGQTV 421
Cdd:cd14934 236 VLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 422 PQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMFVLE 501
Cdd:cd14934 316 EQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 502 QEEYKKEGIVWEFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKCNAFQKPKPAKGK-AEAH 580
Cdd:cd14934 396 QEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKgPEAH 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 581 FSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPpvvEETGGGKKGGKKKGGSMQTVSSQFRENLGKL 660
Cdd:cd14934 476 FELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFK---EEEAPAGSKKQKRGSSFMTVSNFYREQLNKL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 661 MTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASVIPEGqFIDN 740
Cdd:cd14934 553 MTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-FVDN 631
|
650 660
....*....|....*....|....*...
gi 288856329 741 KKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd14934 632 KKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
101-768 |
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: 939.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITG 180
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 181 ESGAGKTVNTKRVIQYFATVavqGPEKKKEQASGKmQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSG 260
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATV---GASKKTDEAAKS-KGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 261 KLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEMTLITTNPYDFPMCSQGQITVASIDDKEELVATDTAI 340
Cdd:cd14909 157 KLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 341 DILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKGQT 420
Cdd:cd14909 237 DILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 421 VPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMFVL 500
Cdd:cd14909 317 VQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 501 EQEEYKKEGIVWEFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKCNAFQKPKPAK-GKAEA 579
Cdd:cd14909 397 EQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpGQQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 580 HFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLY---PPVVEETGGGKKGGKKKGGSMQTVSSQFREN 656
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFadhAGQSGGGEQAKGGRGKKGGGFATVSSAYKEQ 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 657 LGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASVIPEGQ 736
Cdd:cd14909 557 LNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEE 636
|
650 660 670
....*....|....*....|....*....|..
gi 288856329 737 fiDNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd14909 637 --DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
101-768 |
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: 811.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKR-MEAPPHIFSVSDNAYQFMLTDRENQSVLIT 179
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 180 GESGAGKTVNTKRVIQYFATVAVQGPEKKKEQASgkmqgSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTS 259
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSAS-----SIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 260 GKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEMTLITTNPYDFPM----CSQGQITVASIDDKEELVA 335
Cdd:cd00124 156 GRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylNSSGCDRIDGVDDAEEFQE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 336 TDTAIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREE--QAEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNE 413
Cdd:cd00124 236 LLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 414 FVTKGQTVPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNF--FIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQ 491
Cdd:cd00124 316 TITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEStsFIGILDIFGFENFEVNSFEQLCINYANEKLQQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 492 FFNHHMFVLEQEEYKKEGIVWEFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKCNAFQKP 570
Cdd:cd00124 396 FFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 571 KpakgKAEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKssvkllatlyppvveetgggkkggkkkggsmqtvS 650
Cdd:cd00124 475 R----KAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRS----------------------------------G 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 651 SQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAS 730
Cdd:cd00124 517 SQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPG 596
|
650 660 670
....*....|....*....|....*....|....*...
gi 288856329 731 vIPEGQFIDNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd00124 597 -ATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
32-1114 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 809.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 32 FDAKTACYVVDDKELYVKGTIKSKD--GGKVTV------ITLDTKEEKVVKEDDvhpMNPPKFDKIEDMAMMTHLNEPSV 103
Cdd:COG5022 6 AEVGSGCWIPDEEKGWIWAEIIKEAfnKGKVTEegkkedGESVSVKKKVLGNDR---IKLPKFDGVDDLTELSYLNEPAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 104 LYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITGESG 183
Cdd:COG5022 83 LHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 184 AGKTVNTKRVIQYFATVavqgpekkkEQASGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGKLA 263
Cdd:COG5022 163 AGKTENAKRIMQYLASV---------TSSSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEIC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 264 SADIETYLLEKSRVTFQLPDERGYHIFYQMMTNhKPELIEMTLITTNPYDFPMCSQG-QITVASIDDKEELVATDTAIDI 342
Cdd:COG5022 234 GAKIETYLLEKSRVVHQNKNERNYHIFYQLLAG-DPEELKKLLLLQNPKDYIYLSQGgCDKIDGIDDAKEFKITLDALKT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 343 LGFNNEEKMGIYKFTGAVLHHGNMKFKqKQREEQAEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKGQTVP 422
Cdd:COG5022 313 IGIDEEEQDQIFKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 423 QVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMFVLEQ 502
Cdd:COG5022 392 QALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQ 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 503 EEYKKEGIVWEFIDFgMDLAACIELIEK--PLGIFSILEEECMFPKATDTSFKNKLYDQ-HLGKCNAFQKPKPAKGKaea 579
Cdd:COG5022 472 EEYVKEGIEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNK--- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 580 hFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPVVEetgggkkggKKKGGSMQTVSSQFRENLGK 659
Cdd:COG5022 548 -FVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEEN---------IESKGRFPTLGSRFKESLNS 617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 660 LMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASVIPEGQFI- 738
Cdd:COG5022 618 LMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTw 697
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 739 --DNKKASEKLLGSIDVNHDEYRFGHTKVFFKAGLLGTLEEMRDEKLASLVTMTQALCRAYLMRREFVKMMERRDAIYTI 816
Cdd:COG5022 698 keDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVI 777
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 817 QYNVRSFMNVKHWPWMKVYYKIKPLLKSAETEKELatmkEDFVKCKEDLAKAEAKKKELEEKMVALLQEKNDLQLAVASE 896
Cdd:COG5022 778 QHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEY----RSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGR 853
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 897 SENLS---DAEERCEGLIKSKIQLEAKLKETTERLEDEEEINaELTAKKRKLEDECSELKKDID-----DLELTLAKVEK 968
Cdd:COG5022 854 SLKAKkrfSLLKKETIYLQSAQRVELAERQLQELKIDVKSIS-SLKLVNLELESEIIELKKSLSsdlieNLEFKTELIAR 932
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 969 EKHATEN-KVKNLTEEMAAQDESIGKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQekklR 1047
Cdd:COG5022 933 LKKLLNNiDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQ----Y 1008
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 288856329 1048 MDLERAKRKLEgdlklaqesIMDLENDKQQSEEKLKKKDFETSQLLSKIEDEQSL----GAQLQKKIKELQ 1114
Cdd:COG5022 1009 GALQESTKQLK---------ELPVEVAELQSASKIISSESTELSILKPLQKLKGLllleNNQLQARYKALK 1070
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
102-768 |
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: 767.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 102 SVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITGE 181
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 182 SGAGKTVNTKRVIQYFATVAVQGPEK-----KKEQASGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHF 256
Cdd:cd14911 82 SGAGKTENTKKVIQFLAYVAASKPKGsgavpHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 257 GTSGKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEmTLITTNPYDFPMCSQGQITVASIDDKEELVAT 336
Cdd:cd14911 162 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQRE-KFILDDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 337 DTAIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAE-PDGTEeADKIGYLLGLNSADMLKALCYPRVKVGNEFV 415
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNTV-AQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 416 TKGQTVPQVYNSVSALSKSIYERMFLWMVVRINQMLD-TKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFN 494
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 495 HHMFVLEQEEYKKEGIVWEFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHlgkcNAFQKPKPAK 574
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH----SMHPKFMKTD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 575 GKAEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPP-----VVEETGGGKKGGKKKGGSM-QT 648
Cdd:cd14911 476 FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDaeivgMAQQALTDTQFGARTRKGMfRT 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 649 VSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 728
Cdd:cd14911 556 VSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLT 635
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 288856329 729 ASVIPEGqFIDNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd14911 636 PNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
102-768 |
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: 742.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 102 SVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITGE 181
Cdd:cd14920 2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 182 SGAGKTVNTKRVIQYFATVAvqgpEKKKEQASGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGK 261
Cdd:cd14920 82 SGAGKTENTKKVIQYLAHVA----SSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 262 LASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPEL-IEMTLITTNPYDFpmCSQGQITVASIDDKEELVATDTAI 340
Cdd:cd14920 158 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFNNYRF--LSNGYIPIPGQQDKDNFQETMEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 341 DILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAE-PDGTeEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKGQ 419
Cdd:cd14920 236 HIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASmPENT-VAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 420 TVPQVYNSVSALSKSIYERMFLWMVVRINQMLD-TKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMF 498
Cdd:cd14920 315 TKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 499 VLEQEEYKKEGIVWEFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLyDQHLGKCNAFQKPKPAKG 575
Cdd:cd14920 395 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKL-VQEQGSHSKFQKPRQLKD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 576 KAEahFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPVVE---------ETGGGKKGGKKKGGSM 646
Cdd:cd14920 474 KAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRivgldqvtgMTETAFGSAYKTKKGM 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 647 -QTVSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 725
Cdd:cd14920 552 fRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 288856329 726 VLNASVIPEGqFIDNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd14920 632 ILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
102-768 |
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: 702.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 102 SVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITGE 181
Cdd:cd14932 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 182 SGAGKTVNTKRVIQYFATVAVQGPEKKKEQASGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGK 261
Cdd:cd14932 82 SGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 262 LASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPEL-IEMTLITTNPYDFpmCSQGQITVASIDDKEELVATDTAI 340
Cdd:cd14932 162 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLrSELCLEDYSKYRF--LSNGNVTIPGQQDKELFAETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 341 DILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAE-PDGTeEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKGQ 419
Cdd:cd14932 240 RIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDT-AAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 420 TVPQVYNSVSALSKSIYERMFLWMVVRINQMLD-TKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMF 498
Cdd:cd14932 319 TQEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 499 VLEQEEYKKEGIVWEFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKCNAFQKPKpaKG 575
Cdd:cd14932 399 ILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QEQGNNPKFQKPK--KL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 576 KAEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPV--------VEETGGGKKGGKKKGGSM- 646
Cdd:cd14932 476 KDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVdrivgldkVAGMGESLHGAFKTRKGMf 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 647 QTVSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 726
Cdd:cd14932 556 RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 288856329 727 LNASVIPEGqFIDNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd14932 636 LTPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
101-768 |
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: 690.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYA-AWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLIT 179
Cdd:cd01380 1 PAVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 180 GESGAGKTVNTKRVIQYFATVavqgpekkkeQASGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTS 259
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFATV----------GGSSSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 260 GKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTN-HKPELIEMTLiTTNPYDFPMCSQGQITVASIDDKEELVATDT 338
Cdd:cd01380 151 YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAaSLPELKELHL-GSAEDFFYTNQGGSPVIDGVDDAAEFEETRK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 339 AIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKG 418
Cdd:cd01380 230 ALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 419 QTVPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQ--QRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHH 496
Cdd:cd01380 310 LTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVkeKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 497 MFVLEQEEYKKEGIVWEFIDFgMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKCNA-FQKPKPAKG 575
Cdd:cd01380 390 VFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNKhFKKPRFSNT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 576 KaeahFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLlatlyppvveetgggkkggkkkggsmQTVSSQFRE 655
Cdd:cd01380 469 A----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNRK--------------------------KTVGSQFRD 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 656 NLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASviPEG 735
Cdd:cd01380 519 SLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPS--KEW 596
|
650 660 670
....*....|....*....|....*....|...
gi 288856329 736 QFIDNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd01380 597 LRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
102-768 |
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: 673.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 102 SVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITGE 181
Cdd:cd14921 2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 182 SGAGKTVNTKRVIQYFATVAVQGPEKKKEQASGKmqgsLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGK 261
Cdd:cd14921 82 SGAGKTENTKKVIQYLAVVASSHKGKKDTSITGE----LEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 262 LASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEMTLITT-NPYDFpmCSQGQITVASIDDKEELVATDTAI 340
Cdd:cd14921 158 IVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGfNNYTF--LSNGFVPIPAAQDDEMFQETLEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 341 DILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAE-PDGTeEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKGQ 419
Cdd:cd14921 236 SIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 420 TVPQVYNSVSALSKSIYERMFLWMVVRINQMLD-TKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMF 498
Cdd:cd14921 315 TKEQADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 499 VLEQEEYKKEGIVWEFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKCNAFQKPKPAKG 575
Cdd:cd14921 395 ILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLC-TEQGNHPKFQKPKQLKD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 576 KAEahFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPV---------VEETGGGKKGGKKKGGSM 646
Cdd:cd14921 474 KTE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldqmAKMTESSLPSASKTKKGM 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 647 -QTVSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 725
Cdd:cd14921 552 fRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 288856329 726 VLNASVIPEGqFIDNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd14921 632 ILAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
102-768 |
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: 654.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 102 SVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITGE 181
Cdd:cd15896 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 182 SGAGKTVNTKRVIQYFATVAVQGPEKKKEQASGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGK 261
Cdd:cd15896 82 SGAGKTENTKKVIQYLAHVASSHKTKKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 262 LASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPEL-IEMTLITTNPYDFpmCSQGQITVASIDDKEELVATDTAI 340
Cdd:cd15896 162 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLrSELLLENYNNYRF--LSNGNVTIPGQQDKDLFTETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 341 DILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKGQT 420
Cdd:cd15896 240 RIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 421 VPQVYNSVSALSKSIYERMFLWMVVRINQMLD-TKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMFV 499
Cdd:cd15896 320 QEQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 500 LEQEEYKKEGIVWEFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKCNAFQKPKpaKGK 576
Cdd:cd15896 400 LEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVL-QEQGTHPKFFKPK--KLK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 577 AEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPV--------VEETGGGKKGGKKKGGSMQT 648
Cdd:cd15896 477 DEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVdrivgldkVSGMSEMPGAFKTRKGMFRT 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 649 VSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 728
Cdd:cd15896 557 VGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 636
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 288856329 729 ASVIPEGqFIDNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd15896 637 PNAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
102-768 |
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: 652.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 102 SVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITGE 181
Cdd:cd14919 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 182 SGAGKTVNTKRVIQYFATVAVQGPEKKKeqasgkmQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGK 261
Cdd:cd14919 82 SGAGKTENTKKVIQYLAHVASSHKSKKD-------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 262 LASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPEL-IEMTLITTNPYDFpmCSQGQITVASIDDKEELVATDTAI 340
Cdd:cd14919 155 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLkTDLLLEPYNKYRF--LSNGHVTIPGQQDKDMFQETMEAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 341 DILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAE-PDGTeEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKGQ 419
Cdd:cd14919 233 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 420 TVPQVYNSVSALSKSIYERMFLWMVVRINQMLD-TKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMF 498
Cdd:cd14919 312 TKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 499 VLEQEEYKKEGIVWEFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKCNAFQKPKPAKG 575
Cdd:cd14919 392 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVV-QEQGTHPKFQKPKQLKD 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 576 KAEahFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPV-----------VEETGGGKKGGKKKGG 644
Cdd:cd14919 471 KAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldqvagMSETALPGAFKTRKGM 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 645 sMQTVSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 724
Cdd:cd14919 549 -FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 288856329 725 KVLNASVIPEGqFIDNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd14919 628 EILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
102-768 |
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: 635.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 102 SVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITGE 181
Cdd:cd14930 2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 182 SGAGKTVNTKRVIQYFATVAvQGPEKKKEQAsgkMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGK 261
Cdd:cd14930 82 SGAGKTENTKKVIQYLAHVA-SSPKGRKEPG---VPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 262 LASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPEL-IEMTLITTNPYDF----PMCSQGQitvasidDKEELVAT 336
Cdd:cd14930 158 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLkADLLLEPCSHYRFltngPSSSPGQ-------ERELFQET 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 337 DTAIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAE-PDGTeEADKIGYLLGLNSADMLKALCYPRVKVGNEFV 415
Cdd:cd14930 231 LESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 416 TKGQTVPQVYNSVSALSKSIYERMFLWMVVRINQMLD-TKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFN 494
Cdd:cd14930 310 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 495 HHMFVLEQEEYKKEGIVWEFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLyDQHLGKCNAFQKPK 571
Cdd:cd14930 390 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGGHPKFQRPR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 572 PAKGKAEahFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPV--------VEETGGGKKGGKKKG 643
Cdd:cd14930 469 HLRDQAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVegivgleqVSSLGDGPPGGRPRR 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 644 GSMQTVSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQR 723
Cdd:cd14930 547 GMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQR 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 288856329 724 YKVLNASVIPEGqFIDNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd14930 627 YEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
102-768 |
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: 616.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 102 SVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITGE 181
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 182 SGAGKTVNTKRVIQYFATVavqgpekkkeqaSGKmQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGK 261
Cdd:cd01381 82 SGAGKTESTKLILQYLAAI------------SGQ-HSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 262 LASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEMtLITTNPYDFPMCSQGQ-ITVASIDDKEELVATDTAI 340
Cdd:cd01381 149 IEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKK-LELGDASDYYYLTQGNcLTCEGRDDAAEFADIRSAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 341 DILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQRE--EQAEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKG 418
Cdd:cd01381 228 KVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 419 QTVPQVYNSVSALSKSIYERMFLWMVVRIN----QMLDTKQQRNfFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFN 494
Cdd:cd01381 308 LSAEQALDVRDAFVKGIYGRLFIWIVNKINsaiyKPRGTDSSRT-SIGVLDIFGFENFEVNSFEQLCINFANENLQQFFV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 495 HHMFVLEQEEYKKEGIVWEFIDFgMDLAACIELI-EKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKCNaFQKPkpa 573
Cdd:cd01381 387 RHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKN-YLKP--- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 574 KGKAEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPVVEETGGGKKGGkkkggsmQTVSSQF 653
Cdd:cd01381 462 KSDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGSETRKKS-------PTLSSQF 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 654 RENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLnASVIP 733
Cdd:cd01381 535 RKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVL-VPGIP 613
|
650 660 670
....*....|....*....|....*....|....*
gi 288856329 734 EGQFIDNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd01381 614 PAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
102-768 |
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: 606.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 102 SVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITGE 181
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 182 SGAGKTVNTKRVIQYFATVavqgpekkkeqaSGKMQGSLE---DQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGT 258
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAV------------SGGSESEVErvkDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 259 SGKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEMTLITTNPYDFPMCSQGQITVASIDDKEELVATDT 338
Cdd:cd01378 150 KGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 339 AIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDgTEEADKIGYLLGLNSADMLKALCYPRVKVGNEF---V 415
Cdd:cd01378 230 AMKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 416 TKGQTVPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQR-NFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFN 494
Cdd:cd01378 309 EVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGkKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 495 HhmFVL--EQEEYKKEGIVWEFIDFgMDLAACIELIE-KPLGIFSILEEECMFP-KATDTSFKNKLyDQHLGKCNAFQKP 570
Cdd:cd01378 389 E--LTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 571 KPAKGKAEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPVVEETGGGKKGgkkkggsmqTVS 650
Cdd:cd01378 465 SGHFELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDSKKRPP---------TAG 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 651 SQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAS 730
Cdd:cd01378 536 TKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPK 615
|
650 660 670
....*....|....*....|....*....|....*...
gi 288856329 731 VIPEGQFIDnKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd01378 616 TWPAWDGTW-QGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
101-768 |
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: 605.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRgKKRMEaPPHIFSVSDNAYQFMLTDRENQSVLITG 180
Cdd:cd01383 1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR-QKLLD-SPHVYAVADTAYREMMRDEINQSIIISG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 181 ESGAGKTVNTKRVIQYFATVavqgpekkkeqasGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSG 260
Cdd:cd01383 79 ESGAGKTETAKIAMQYLAAL-------------GGGSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 261 KLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEmTLITTNPYDFPMCSQGQ-ITVASIDDKEELVATDTA 339
Cdd:cd01383 146 KICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALRE-KLNLKSASEYKYLNQSNcLTIDGVDDAKKFHELKEA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 340 IDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKGQ 419
Cdd:cd01383 225 LDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 420 TVPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNF-FIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMF 498
Cdd:cd01383 305 TLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGrSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 499 VLEQEEYKKEGIVWEFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLyDQHLGKCNAFqkpkpaKGKA 577
Cdd:cd01383 385 KLEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCF------KGER 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 578 EAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPVVEE-TGGGKKGGKKKGGSM-QTVSSQFRE 655
Cdd:cd01383 457 GGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFASKMLDAsRKALPLTKASGSDSQkQSVATKFKG 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 656 NLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLnasvIPEG 735
Cdd:cd01383 537 QLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFL----LPED 612
|
650 660 670
....*....|....*....|....*....|....*
gi 288856329 736 QFIDNKKASEK--LLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd01383 613 VSASQDPLSTSvaILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
102-768 |
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: 590.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 102 SVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITGE 181
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 182 SGAGKTVNTKRVIQYFATVAVQgpekkkeqasgkmQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGK 261
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNN-------------HSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 262 LASADIETYLLEKSRVTFQLPDERGYHIFYQMMT--NHKPELIEmTLITTNPYDFPMCSQ-GQITVASIDDKEELVATDT 338
Cdd:cd14883 149 IKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAgaKHSKELKE-KLKLGEPEDYHYLNQsGCIRIDNINDKKDFDHLRL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 339 AIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAE-PDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTK 417
Cdd:cd14883 228 AMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 418 GQTVPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHM 497
Cdd:cd14883 308 PLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 498 FVLEQEEYKKEGIVWEFIDFgMDLAACIELIEK-PLGIFSILEEECMFPKATDTSFKNKLYDQHlGKCNAFQkpKPAKGK 576
Cdd:cd14883 388 FKLEQEEYEKEGINWSHIVF-TDNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYE--KPDRRR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 577 AEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLY-PPVVEETGGGKKGGKKKGGSMQ------TV 649
Cdd:cd14883 464 WKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFtYPDLLALTGLSISLGGDTTSRGtskgkpTV 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 650 SSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNa 729
Cdd:cd14883 544 GDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLD- 622
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 288856329 730 sviPEGQFIDNKKASE---KLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd14883 623 ---PRARSADHKETCGavrALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
101-768 |
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: 576.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLP-VYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLIT 179
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 180 GESGAGKTVNTKRVIQYFATVAvqgpekKKEQASGKmqgSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTS 259
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG------GRAVTEGR---SVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 260 GKLASADIETYLLEKSRVTfQLPD-ERGYHIFYQMMTNHKPELIEmTLITTNPYDFPMCSQGQ-ITVASIDDKEELVATD 337
Cdd:cd01384 152 GRISGAAIRTYLLERSRVV-QVSDpERNYHCFYQLCAGAPPEDRE-KYKLKDPKQFHYLNQSKcFELDGVDDAEEYRATR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 338 TAIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEP--DGTEEADKI-GYLLGLNSADMLKALCYPRVKVGNEF 414
Cdd:cd01384 230 RAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPkdEKSEFHLKAaAELLMCDEKALEDALCKRVIVTPDGI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 415 VTKGQTVPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFN 494
Cdd:cd01384 310 ITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 495 HHMFVLEQEEYKKEGIVWEFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYDQhlGKCNA-FQKPKp 572
Cdd:cd01384 390 QHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT--LKDHKrFSKPK- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 573 akgKAEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPVVEEtgggkkgGKKKGGSMQTVSSQ 652
Cdd:cd01384 466 ---LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPRE-------GTSSSSKFSSIGSR 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 653 FRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLnASVI 732
Cdd:cd01384 536 FKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLL-APEV 614
|
650 660 670
....*....|....*....|....*....|....*.
gi 288856329 733 PEGQFiDNKKASEKLLGSIDVNhdEYRFGHTKVFFK 768
Cdd:cd01384 615 LKGSD-DEKAACKKILEKAGLK--GYQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
101-768 |
4.45e-165 |
|
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: 519.88 E-value: 4.45e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLP-VYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLIT 179
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 180 GESGAGKTVNTKRVIQYFATVAvqgpekkkeqasGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTS 259
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESW------------GSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 260 GKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEMTLittnpydfpmcsqgqiTVASIDDKEELVATDTA 339
Cdd:cd01382 149 SSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL----------------KDPLLDDVGDFIRMDKA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 340 IDILGFNNEEKMGIYKFTGAVLHHGNMKFkqkqrEEQAE--------PDGTEEADKI-GYLLGLNSADMLKALCYpRVKV 410
Cdd:cd01382 213 MKKIGLSDEEKLDIFRVVAAVLHLGNIEF-----EENGSdsgggcnvKPKSEQSLEYaAELLGLDQDELRVSLTT-RVMQ 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 411 GNEFVTKGQ--TVP----QVYNSVSALSKSIYERMFLWMVVRINQMLDTkQQRNFFIGVLDIAGFEIFDFNSMEQLCINF 484
Cdd:cd01382 287 TTRGGAKGTviKVPlkveEANNARDALAKAIYSKLFDHIVNRINQCIPF-ETSSYFIGVLDIAGFEYFEVNSFEQFCINY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 485 TNEKLQQFFNHHMFVLEQEEYKKEGIVWEFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYDQHLgk 563
Cdd:cd01382 366 CNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK-- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 564 cNAFQKPKPAKGKAEAH--------FSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPvvEETGGG 635
Cdd:cd01382 443 -NHFRLSIPRKSKLKIHrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFES--STNNNK 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 636 KKGGKKKGGSMQTVSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRI 715
Cdd:cd01382 520 DSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRT 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 288856329 716 LYADFKQRYKvlnaSVIPEG-QFIDNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd01382 600 SFHDLYNMYK----KYLPPKlARLDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
102-768 |
2.57e-164 |
|
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: 518.18 E-value: 2.57e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 102 SVLYNLKERYAAWMIYTYSGLFCATVNPYKWLP-VYDAEVVAAYRGKKRMEAPPHIFSVSDNAY-QFM---LTDRENQSV 176
Cdd:cd14890 2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYtQLIqsgVLDPSNQSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 177 LITGESGAGKTVNTKRVIQYFATV----AVQGPEKKKEQASGKMQ--GSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGK 250
Cdd:cd14890 82 IISGESGAGKTEATKIIMQYLARItsgfAQGASGEGEAASEAIEQtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 251 FIRIHFGTSGKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEmTLITTNPYDFPMCSQGQITVASIDDK 330
Cdd:cd14890 162 FIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRE-RLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 331 EELVATDTAIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGTEEA-DKIGYLLGLNSADMLKALCYPRVK 409
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTLQSlKLAAELLGVNEDALEKALLTRQLF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 410 VGNEFVTKGQTVPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKL 489
Cdd:cd14890 321 VGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEKL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 490 QQFFNHHMFVLEQEEYKKEGIVWEFIDFgMDLAACIELIE-----KPlGIFSILEEECMFPKA-TDTSFKNKLYDQHLGK 563
Cdd:cd14890 401 QRHFNQHMFEVEQVEYSNEGIDWQYITF-NDNQACLELIEgkvngKP-GIFITLDDCWRFKGEeANKKFVSQLHASFGRK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 564 CNAFQKPKPAKGK---------AEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATlyppvveetgg 634
Cdd:cd14890 479 SGSGGTRRGSSQHphfvhpkfdADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSIREV----------- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 635 gkkggkkkggsmqTVSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSR 714
Cdd:cd14890 548 -------------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALR 614
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 288856329 715 ILYADFKQRYKVLNASVipegqfiDNKKASEKLLGSI-DVNHDEYRFGHTKVFFK 768
Cdd:cd14890 615 EEHDSFFYDFQVLLPTA-------ENIEQLVAVLSKMlGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
101-768 |
3.53e-163 |
|
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: 515.10 E-value: 3.53e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLP-VYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLIT 179
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 180 GESGAGKTVNTKRVIQYFATVAvqgpekkkeqasGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTS 259
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA------------GGLNDSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 260 GKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELiEMTLITTNPYDFPmcsqGQITVASID---DKEELVAT 336
Cdd:cd14903 149 GTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEE-RLFLDSANECAYT----GANKTIKIEgmsDRKHFART 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 337 DTAIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAE--PDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEF 414
Cdd:cd14903 224 KEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 415 VTKGQTVPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFN 494
Cdd:cd14903 304 YTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFT 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 495 HHMFVLEQEEYKKEGIVWEFIDFgMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKCNAFQKPKPAK 574
Cdd:cd14903 384 QDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 575 gkaeAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPVVEETGGGKKGGKKKGG-------SMQ 647
Cdd:cd14903 463 ----TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARrrrggalTTT 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 648 TVSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 727
Cdd:cd14903 539 TVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLF 618
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 288856329 728 nasvIPEGQFIDNKKAS--EKLLGSIDVNH-DEYRFGHTKVFFK 768
Cdd:cd14903 619 ----LPEGRNTDVPVAErcEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
101-768 |
6.84e-163 |
|
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: 513.94 E-value: 6.84e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITG 180
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 181 ESGAGKTVNTKRVIQYFATVAvqgpekkkeqasgKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSG 260
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVA-------------GSTNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 261 KLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTnhKPELIEMTLITTNPyDFPMCSQGQ-ITVASIDDKEELVATDTA 339
Cdd:cd14872 148 RICGASTENYLLEKSRVVYQIKGERNFHIFYQLLA--SPDPASRGGWGSSA-AYGYLSLSGcIEVEGVDDVADFEEVVLA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 340 IDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGT---EEADKIGYLLGLNSADMLKALCYPRVKVGNefvT 416
Cdd:cd14872 225 MEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVanrDVLKEVATLLGVDAATLEEALTSRLMEIKG---C 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 417 KGQTVP----QVYNSVSALSKSIYERMFLWMVVRINQ-MLDTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQ 491
Cdd:cd14872 302 DPTRIPltpaQATDACDALAKAAYSRLFDWLVKKINEsMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 492 FFNHHMFVLEQEEYKKEGIVWEFIDFgMDLAACIELIEK-PLGIFSILEEECMFPKATDTSFKNKLYDQHLGKcnAFQKP 570
Cdd:cd14872 382 HFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAK--STFVY 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 571 KPAKGkAEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPVveetgggkkgGKKKGGSMQTVS 650
Cdd:cd14872 459 AEVRT-SRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPS----------EGDQKTSKVTLG 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 651 SQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAS 730
Cdd:cd14872 528 GQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVKT 607
|
650 660 670
....*....|....*....|....*....|....*...
gi 288856329 731 vIPEGQFIDNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd14872 608 -IAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
848-1925 |
4.49e-162 |
|
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: 526.67 E-value: 4.49e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 848 EKELATMKEDFVKCKEDLAKAEAKKKELEEKMVALLQEKNDLQLAVASESENLSDAEERCEGLIKSKIQLEAKLKETTER 927
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 928 LEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAQDESIGKLTKEKKALQEAHQQ 1007
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1008 TLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSEEKLKKKDF 1087
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1088 ETSQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQIEMNK 1167
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1168 KREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEYKMEIDDLSSNMEAVAKAKANL 1247
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1248 EKMCRTLEDQLSEIKSKNDENLRQINDLSAQRARLQTENGEFGRQLEEKEALVSQLTRGKQAFTQQIEELKRQIEEEVKA 1327
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1328 KNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRTKYETDAiQRTEELEESKKKLAQRLQEAEEQIE 1407
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1408 AVNSKCASLEKTKQRLQGEVEDLMIDVERANALAANLDKKQRNFDKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMK 1487
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1488 NSYEETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAVETEKAEIQTALEEAEGTLEHEESKILRVQLEL 1567
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNM 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1568 NQVKSEIDRKLAEKDEEIEQIKRNSQRITDSMQSTLDSEVRSRNDALRIKKKMEGDLNEMEIQLSHANRQAAEAQKQLRN 1647
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1648 VQAQLKDAQLHLDDAVRGQEDMKEQVAMVERRNTLMQSEIEELRAALEQTERGRKVAEQELVDASERVGLLHSQNTSLLN 1727
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1728 TKKKLEADLVQIQSEVEDTVQEARNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENLAM 1807
Cdd:pfam01576 883 EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1808 KGGKKQLQKLESRVRELESEVEAEQRRGADAVKGVRKYERRVKELTYQTEEDKKNVNRLQDLVDKLQLKVKAYKRQSEEA 1887
Cdd:pfam01576 963 SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 288856329 1888 EEQANSHLSKLRKVQHELEEAEERADIAESQVNKLRAK 1925
Cdd:pfam01576 1043 EEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
101-768 |
3.37e-161 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 510.00 E-value: 3.37e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLP-VYDAEVVAAYRgKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLIT 179
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 180 GESGAGKTVNTKRVIQYfatVAVQGPEKKKeqasgkMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHF--- 256
Cdd:cd14888 80 GESGAGKTESTKYVMKF---LACAGSEDIK------KRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFskl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 257 ------GTSGKLASADIETYLLEKSRVTFQLPDERGYHIFYQ--------------MMTNH---------KPELIEMTLi 307
Cdd:cd14888 151 kskrmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQlcaaareakntglsYEENDeklakgadaKPISIDMSS- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 308 ttnpyDFPMCSQGQITVASI------DDKEELVATDTAIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQA---E 378
Cdd:cd14888 230 -----FEPHLKFRYLTKSSChelpdvDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 379 PDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKGQTVPQVYNSVSALSKSIYERMFLWMVVRINQMLD-TKQQR 457
Cdd:cd14888 305 ASCTDDLEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 458 NFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGmDLAACIELI-EKPLGIFS 536
Cdd:cd14888 385 LLFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFC 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 537 ILEEECMFPKATDTSFKNKLYDQHLGKcNAFQKPKpakgKAEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKS 616
Cdd:cd14888 464 MLDEECFVPGGKDQGLCNKLCQKHKGH-KRFDVVK----TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNS 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 617 SVKLLATLYPPVVEETGGGKKGGKKKggsmQTVSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLR 696
Cdd:cd14888 539 KNPFISNLFSAYLRRGTDGNTKKKKF----VTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLK 614
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 288856329 697 CNGVLEGIRICRKGFPSRILYADFKQRYKVLnasvipegqfidnkkasekLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd14888 615 YGGVLQAVQVSRAGYPVRLSHAEFYNDYRIL-------------------LNGEGKKQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
102-768 |
8.92e-158 |
|
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: 500.43 E-value: 8.92e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 102 SVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITGE 181
Cdd:cd01387 2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 182 SGAGKTVNTKRVIQYFATVAVQGPEKKKEQasgkmqgsledqIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFgTSGK 261
Cdd:cd01387 82 SGSGKTEATKLIMQYLAAVNQRRNNLVTEQ------------ILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 262 LASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIE-MTLITTNPYdFPMCSQGQITVASIDDKEELVATDTAI 340
Cdd:cd01387 149 IVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQkYGLQEAEKY-FYLNQGGNCEIAGKSDADDFRRLLAAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 341 DILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQRE---EQAEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTK 417
Cdd:cd01387 228 QVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRhgqEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 418 GQTVPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHM 497
Cdd:cd01387 308 PLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 498 FVLEQEEYKKEGIVWEFIDFgMDLAACIELI-EKPLGIFSILEEECMFPKATDTSFKNKLYDQHlGKCNAFQKPKpaKGK 576
Cdd:cd01387 388 FKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPR--MPL 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 577 AEahFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPVVEETGGGKKGGKK-KGGSMQ----TVSS 651
Cdd:cd01387 464 PE--FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDKAPPRLGKgRFVTMKprtpTVAA 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 652 QFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASV 731
Cdd:cd01387 542 RFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALK 621
|
650 660 670
....*....|....*....|....*....|....*..
gi 288856329 732 IPEGQFIDNKKASEKLLGSIdVNHDEYRFGHTKVFFK 768
Cdd:cd01387 622 LPRPAPGDMCVSLLSRLCTV-TPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
101-766 |
2.60e-154 |
|
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: 490.84 E-value: 2.60e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAY--RGKKRM----EAPPHIFSVSDNAYQFMLTDRE-- 172
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyeHGERRAagerKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 173 --NQSVLITGESGAGKTVNTKRVIQYFATVAvqgpEKKKEQASGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGK 250
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVS----SATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 251 FIRIHFGTSGKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKP-ELIEMTLITTNPYDFPMCSQGQITVASIDD 329
Cdd:cd14901 157 FIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSdELHALGLTHVEEYKYLNSSQCYDRRDGVDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 330 KEELVATDTAIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGTE-EADKIGYLLGLNSADMLKALCYPRV 408
Cdd:cd14901 237 SVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLaNVRAACDLLGLDMDVLEKTLCTREI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 409 KVGNEFVTKGQTVPQVYNSVSALSKSIYERMFLWMVVRINQML----DTKQQRnfFIGVLDIAGFEIFDFNSMEQLCINF 484
Cdd:cd14901 317 RAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIayseSTGASR--FIGIVDIFGFEIFATNSLEQLCINF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 485 TNEKLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGMDlAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYDQhLGK 563
Cdd:cd14901 395 ANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 564 CNAFQKPKPAKGKAEahFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATlyppvveetgggkkggkkkg 643
Cdd:cd14901 473 HASFSVSKLQQGKRQ--FVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS-------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 644 gsmqTVSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQR 723
Cdd:cd14901 531 ----TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHT 606
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 288856329 724 YKVLNASVIPEGQFIDNKKASEKLLGSIDV----NHDEYRFGHTKVF 766
Cdd:cd14901 607 YSCLAPDGASDTWKVNELAERLMSQLQHSElnieHLPPFQVGKTKVF 653
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
102-768 |
4.63e-154 |
|
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: 490.08 E-value: 4.63e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 102 SVLYNLKERYAAWMIYTYSGLFCATVNPYKWLP-VYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITG 180
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 181 ESGAGKTVNTKRVIQYFATVAVQGPEKKkeqaSGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSG 260
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVISQQSLELS----LKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 261 KLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEMtLITTNPYDFPMCSQ-GQITVASIDDKEELVATDTA 339
Cdd:cd14873 158 NIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREE-FYLSTPENYHYLNQsGCVEDKTISDQESFREVITA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 340 IDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGTEEADKigyLLGLNSADMLKALCYPRVKVGNEFVTKGQ 419
Cdd:cd14873 237 MEVMQFSKEEVREVSRLLAGILHLGNIEFITAGGAQVSFKTALGRSAE---LLGLDPTQLTDALTQRSMFLRGEEILTPL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 420 TVPQVYNSVSALSKSIYERMFLWMVVRINQMLdtKQQRNF-FIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMF 498
Cdd:cd14873 314 NVQQAVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFkSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 499 VLEQEEYKKEGIVWEFIDFgMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHlGKCNAFQKPKpakgKAE 578
Cdd:cd14873 392 SLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH-ANNHFYVKPR----VAV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 579 AHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPVVEETGGGKKGGKKKGGSmQTVSSQFRENLG 658
Cdd:cd14873 466 NNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRR-PTVSSQFKDSLH 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 659 KLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL-NASVIPEgqf 737
Cdd:cd14873 545 SLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLmRNLALPE--- 621
|
650 660 670
....*....|....*....|....*....|.
gi 288856329 738 iDNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd14873 622 -DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
101-768 |
9.01e-152 |
|
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: 482.93 E-value: 9.01e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITG 180
Cdd:cd01379 1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 181 ESGAGKTVNTKRVIQYFATVavqgpekkkeqasGKMQ-GSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTS 259
Cdd:cd01379 81 ESGAGKTESANLLVQQLTVL-------------GKANnRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTST 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 260 GKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMT--NHKPELIEMTLITTNP----YDFPMCSQGQITVASIDDKEEL 333
Cdd:cd01379 148 GAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAglAEDKKLAKYKLPENKPprylQNDGLTVQDIVNNSGNREKFEE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 334 VatDTAIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQ----AEPDGTEEADKIGYLLGLNSADMLKALCYPRVK 409
Cdd:cd01379 228 I--EQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 410 VGNEFVTKGQTVPQVYNSVSALSKSIYERMFLWMVVRINQMLdtKQQRNFF-----IGVLDIAGFEIFDFNSMEQLCINF 484
Cdd:cd01379 306 TRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLL--KPDRSASdeplsIGILDIFGFENFQKNSFEQLCINI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 485 TNEKLQQFFNHHMFVLEQEEYKKEGIVWEFIDFG-----MDLaacieLIEKPLGIFSILEEECMFPKATDTSFKNKLYDQ 559
Cdd:cd01379 384 ANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKFHNN 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 560 HlgKCNAFQKPKpakgKAEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLatlyppvveetgggkkgg 639
Cdd:cd01379 459 I--KSKYYWRPK----SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV------------------ 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 640 kkkggsMQTVSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYAD 719
Cdd:cd01379 515 ------RQTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFAD 588
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 288856329 720 FKQRYKVL--NASVIPEGqfidNKKASEKLLgsIDVNHDEYRFGHTKVFFK 768
Cdd:cd01379 589 FLKRYYFLafKWNEEVVA----NRENCRLIL--ERLKLDNWALGKTKVFLK 633
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
102-768 |
1.48e-151 |
|
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: 484.57 E-value: 1.48e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 102 SVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITGE 181
Cdd:cd01385 2 TLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 182 SGAGKTVNTKRVIQYFATVAVQGpekkkeQASGkmqgsLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGK 261
Cdd:cd01385 82 SGSGKTESTNFLLHHLTALSQKG------YGSG-----VEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 262 LASADIETYLLEKSRVTFQLPDERGYHIFYQMMTN-HKPELIEMTLITTNPYDFPMCSQGqITVASIDDKEELVATDTAI 340
Cdd:cd01385 151 VRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGaSEEERKELHLKQPEDYHYLNQSDC-YTLEGEDEKYEFERLKQAM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 341 DILGFNNEEKMGIYKFTGAVLHHGNMKFKQK--QREEQAEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKG 418
Cdd:cd01385 230 EMVGFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 419 QTVPQVYNSVSALSKSIYERMFLWMVVRINQML----DTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFN 494
Cdd:cd01385 310 YKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 495 HHMFVLEQEEYKKEGIVWEFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKlYDQHLGKCNAFQKPKpa 573
Cdd:cd01385 390 QHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQ-- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 574 kgKAEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSS---VKLLATLYPPVV--------------------- 629
Cdd:cd01385 466 --VMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSsafVRELIGIDPVAVfrwavlrafframaafreagr 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 630 ---EETGGGKKGGKKKGGSM----------QTVSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLR 696
Cdd:cd01385 544 rraQRTAGHSLTLHDRTTKSllhlhkkkkpPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLR 623
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 288856329 697 CNGVLEGIRICRKGFPSRILYADFKQRYKVLnasvIPEGQfIDNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd01385 624 YTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGL-ISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
107-768 |
6.62e-151 |
|
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: 481.57 E-value: 6.62e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 107 LKERYAAWMIYTYSGLFCATVNPYKWLP-VYDAEVVAAYRGKKRME--APPHIFSVSDNAYQFMLTDR----ENQSVLIT 179
Cdd:cd14892 7 LRRRYERDAIYTFTADILISINPYKSIPlLYDVPGFDSQRKEEATAssPPPHVFSIAERAYRAMKGVGkgqgTPQSIVVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 180 GESGAGKTVNTKRVIQYFATVAVQGPEKKKEQASGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTS 259
Cdd:cd14892 87 GESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNSD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 260 GKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNhKPELIEMTLITTNPYDFPMCSQGQ-ITVASIDDKEELVATDT 338
Cdd:cd14892 167 GRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAG-LDANENAALELTPAESFLFLNQGNcVEVDGVDDATEFKQLRD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 339 AIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQ--KQREEQAEPDGTEEADKIGYLLGLNSADMLKALCYpRVKVGnefvT 416
Cdd:cd14892 246 AMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEEnaDDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLVT-QTTST----A 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 417 KGQ------TVPQVYNSVSALSKSIYERMFLWMVVRINQMldTKQQ------------RNFFIGVLDIAGFEIFDFNSME 478
Cdd:cd14892 321 RGSvleiklTAREAKNALDALCKYLYGELFDWLISRINAC--HKQQtsgvtggaasptFSPFIGILDIFGFEIMPTNSFE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 479 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIVWEFIDFgMDLAACIELIEK-PLGIFSILEEECMFP-KATDTSFKNKL 556
Cdd:cd14892 399 QLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEF-QDNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLLTIY 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 557 YDQHLGKCNAFQKPKpakgKAEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKssvkllatlyppvveetgggk 636
Cdd:cd14892 478 HQTHLDKHPHYAKPR----FECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRS--------------------- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 637 kggkkkggsmqtvSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRIL 716
Cdd:cd14892 533 -------------SSKFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQ 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 288856329 717 YADFKQRYKVLNASVIPEGQFIDNKKASE--KLLGSIDVNH---DEYRFGHTKVFFK 768
Cdd:cd14892 600 FEEFYEKFWPLARNKAGVAASPDACDATTarKKCEEIVARAlerENFQLGRTKVFLR 656
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
102-768 |
1.23e-139 |
|
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: 449.53 E-value: 1.23e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 102 SVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKK-RMEAPPHIFSVSDNAYQFMLTDRENQSVLITG 180
Cdd:cd14897 2 TIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 181 ESGAGKTVNTKRVIQYFATVavqgpekkkeqaSGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSG 260
Cdd:cd14897 82 ESGAGKTESTKYMIKHLMKL------------SPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 261 KLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIeMTLITTNPYDFPMCSQGQITVASIDDKEEL----VAT 336
Cdd:cd14897 150 QLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRL-LYYFLEDPDCHRILRDDNRNRPVFNDSEELeyyrQMF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 337 DTAIDIL---GFNNEEKMGIYKFTGAVLHHGNMKFkqkqrEEQAEPDGTEEADK-----IGYLLGLNSADMLKALCYPRV 408
Cdd:cd14897 229 HDLTNIMkliGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALISNVN 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 409 KVGNEFVTKGQTVPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQ-----RNFFIGVLDIAGFEIFDFNSMEQLCIN 483
Cdd:cd14897 304 TIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDfqimtRGPSIGILDMSGFENFKINSFDQLCIN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 484 FTNEKLQQFFNHHMFVLEQEEYKKEGIVWEFIDFgMDLAACIELI-EKPLGIFSILEEECMFPKATDTSFKNKLYDqhlg 562
Cdd:cd14897 384 LSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEY-HDNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKLNK---- 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 563 KCNAFQKPKPAKGKaEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYppvveetgggkkggkkk 642
Cdd:cd14897 459 YCGESPRYVASPGN-RVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF----------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 643 ggsmqtvSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQ 722
Cdd:cd14897 521 -------TSYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVK 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 288856329 723 RYKVL-----NASVIPEGQFIDNKKasekllgsiDVNHDEYRFGHTKVFFK 768
Cdd:cd14897 594 RYKEIcdfsnKVRSDDLGKCQKILK---------TAGIKGYQFGKTKVFLK 635
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
101-768 |
1.71e-139 |
|
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: 449.78 E-value: 1.71e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLP-VYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLIT 179
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 180 GESGAGKTVNTKRVIQYFATVAvqgpekkkeqasGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTS 259
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVA------------GGRKDKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 260 GKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTN-HKPELIEMTLITTNPYDFPMCSQGQITVASIDDKEELVATDT 338
Cdd:cd14904 149 GKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 339 AIDILGFNNEEKMGIYKFTGAVLHHGNMKFkQKQREEQAEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKG 418
Cdd:cd14904 229 SLSLIGLDNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 419 QTVPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNF-FIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHM 497
Cdd:cd14904 308 LAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 498 FVLEQEEYKKEGIVWEFIDFgMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQH--LGKCNAFQKPKPAKg 575
Cdd:cd14904 388 FKTVEEEYIREGLQWDHIEY-QDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKVKR- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 576 kaeAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPVVEETGGGKKGGKKKGGSMQTVSSQFRE 655
Cdd:cd14904 466 ---TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEAPSETKEGKSGKGTKAPKSLGSQFKT 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 656 NLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLnasVIPEG 735
Cdd:cd14904 543 SLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIM---FPPSM 619
|
650 660 670
....*....|....*....|....*....|....
gi 288856329 736 QFIDNKKASEKLLGSIDVNHD-EYRFGHTKVFFK 768
Cdd:cd14904 620 HSKDVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
102-727 |
2.09e-139 |
|
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: 448.60 E-value: 2.09e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 102 SVLYNLKERYAAWMIYTYSGLFCATVNPYKWLP-VYDAEVVAAY-----------RGKKRMEAPPHIFSVSDNAYQFM-- 167
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 168 --LTDRENQSVLITGESGAGKTVNTKRVIQYFATVAvqGPEKKKEQASGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNS 245
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAG--DNNLAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 246 SRFGKFIRIHFGTSGKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEMTLITtnpydfpmcsqgQITva 325
Cdd:cd14900 160 SRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARKRDMYR------------RVM-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 326 siddkeelvatdTAIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGTEEA-------DKIGYLLGLNSAD 398
Cdd:cd14900 226 ------------DAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLLSVDATK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 399 MLKALCYPRVKVGNEFVTKGQTVPQVYNSVSALSKSIYERMFLWMVVRINQML-----DTKQQRNFFIGVLDIAGFEIFD 473
Cdd:cd14900 294 LEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEVFP 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 474 FNSMEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIVWEFIDFgMDLAACIELI-EKPLGIFSILEEECMFPKATDTSF 552
Cdd:cd14900 374 KNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEF-CDNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 553 KNKLYdQHLGKCNAFQKPKPAKGKaeAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKssvkllatlyppvveet 632
Cdd:cd14900 453 ASKLY-RACGSHPRFSASRIQRAR--GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVY----------------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 633 gggkkggkkkggsmqtvSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFP 712
Cdd:cd14900 513 -----------------GLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFP 575
|
650
....*....|....*
gi 288856329 713 SRILYADFKQRYKVL 727
Cdd:cd14900 576 IRLLHDEFVARYFSL 590
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
101-768 |
4.12e-137 |
|
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: 443.70 E-value: 4.12e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLP-VYDAEVVAAYRGK--------KRMEAPPHIFSVSDNAYQFMLTDR 171
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 172 ENQSVLITGESGAGKTVNTKRVIQYFATVAVQGPE-------KKKEQASGKMQGSLEDQIIAANPLLEAYGNAKTVRNDN 244
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNseevltlTSSIRATSKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 245 SSRFGKFIRIHFG-TSGKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIE-MTLITTNPYDFPMC-SQGQ 321
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQqLGLKNQLSGDRYDYlKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 322 -ITVASIDDKEELVATDTAIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQ--REEQAEPDGTEEADKIGYLLGLNSAD 398
Cdd:cd14907 241 cYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 399 MLKALCYPRVKVGNEFVTKGQTVPQVYNSVSALSKSIYERMFLWMVVRINQML--------DTKQQRNFFIGVLDIAGFE 470
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 471 IFDFNSMEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIVWEF--IDFgMDLAACIELIEK-PLGIFSILEEECMFPKA 547
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 548 TDTSFKNKLYDQHlgkcNAFQKPKPAKGKAEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPP 627
Cdd:cd14907 480 TDEKLLNKIKKQH----KNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSG 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 628 VVEETGGGKKGGKKKGGSMQTVSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRIC 707
Cdd:cd14907 556 EDGSQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVR 635
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 288856329 708 RKGFPSRILYADFKQRYKVLNASVIpegqfidnkkasekllgsidvnhdeyrFGHTKVFFK 768
Cdd:cd14907 636 KQGYPYRKSYEDFYKQYSLLKKNVL---------------------------FGKTKIFMK 669
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
103-768 |
3.97e-135 |
|
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: 437.80 E-value: 3.97e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 103 VLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFML----TDRENQSVLI 178
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 179 TGESGAGKTVNTKRVIQYFAtvavqgpekkkEQASGKMQgsLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFgT 258
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIM-----------ELCRGNSQ--LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-R 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 259 SGKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEM-TLITTNPYDFPMCSQGQITVASIDDKE--ELVa 335
Cdd:cd14889 149 NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENyGLLDPGKYRYLNNGAGCKREVQYWKKKydEVC- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 336 tdTAIDILGFNNEEKMGIYKFTGAVLHHGNMKFkqkqreeqaEPDGTE----EADKIGYL------LGLNSADMLKALCY 405
Cdd:cd14889 228 --NAMDMVGFTEQEEVDMFTILAGILSLGNITF---------EMDDDEalkvENDSNGWLkaaagqFGVSEEDLLKTLTC 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 406 PRVKVGNEFVTKGQTVPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNF---FIGVLDIAGFEIFDFNSMEQLCI 482
Cdd:cd14889 297 TVTFTRGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSVelrEIGILDIFGFENFAVNRFEQACI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 483 NFTNEKLQQFFNHHMFVLEQEEYKKEGIVWEFIDFgMDLAACIEL-IEKPLGIFSILEEECMFPKATDTSFKNKLyDQHL 561
Cdd:cd14889 377 NLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHF 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 562 GKCNAFQKPKPAKGKaeahFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPVVEETGGGKKGGKK 641
Cdd:cd14889 455 KGNSYYGKSRSKSPK----FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKL 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 642 KGGS--------MQTVSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPS 713
Cdd:cd14889 531 PQAGsdnfnstrKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSW 610
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 288856329 714 RILYADFKQRYKVLnasvIPEGQFIDNKKASEKLLGSIDVNhdEYRFGHTKVFFK 768
Cdd:cd14889 611 RPSFAEFAERYKIL----LCEPALPGTKQSCLRILKATKLV--GWKCGKTRLFFK 659
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
56-827 |
6.92e-132 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 434.46 E-value: 6.92e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 56 DGGKVTVITLD--TKEEKVVKEDDV----HPMNPPKFDkieDMAMMTHLNEPSVLYNLKERYAAWMIYTYSGLFCATVNP 129
Cdd:PTZ00014 62 TGEKLTLKQIDppTNSTFEVKPEHAfnanSQIDPMTYG---DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 130 YKWLPVYDAEVVAAYR-GKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITGESGAGKTVNTKRVIQYFATvavqgpekk 208
Cdd:PTZ00014 139 FKDLGNTTNDWIRRYRdAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAS--------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 209 keQASGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGKLASADIETYLLEKSRVTFQLPDERGYH 288
Cdd:PTZ00014 210 --SKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYH 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 289 IFYQMMTNHKPELIE-MTLITTNPYDF--PMCsqgqITVASIDDKEELVATDTAIDILGFNNEEKMGIYKFTGAVLHHGN 365
Cdd:PTZ00014 288 IFYQLLKGANDEMKEkYKLKSLEEYKYinPKC----LDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGN 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 366 MKFKQKQREEQAE-----PDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKGQTVPQVYNSVSALSKSIYERMF 440
Cdd:PTZ00014 364 VEIEGKEEGGLTDaaaisDESLEVFNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLF 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 441 LWMVVRINQMLDTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGMD 520
Cdd:PTZ00014 444 LWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSN 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 521 LAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQhLGKCNAFqkpKPAKGKAEAHFSLVHYAGTVDYNISGWLDK 600
Cdd:PTZ00014 524 ESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTN-LKNNPKY---KPAKVDSNKNFVIKHTIGDIQYCASGFLFK 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 601 NKDPLNESVVQLYQKSSVKLLATLYPPVVEETGGGKKGgkkkggsmQTVSSQFRENLGKLMTNLRSTHPHFVRCLIPNES 680
Cdd:PTZ00014 600 NKDVLRPELVEVVKASPNPLVRDLFEGVEVEKGKLAKG--------QLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNEN 671
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 681 KTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASVIpEGQFIDNKKASEKLLGSIDVNHDEYRF 760
Cdd:PTZ00014 672 KKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVS-NDSSLDPKEKAEKLLERSGLPKDSYAI 750
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 761 GHTKVFFKAGLLGTLEEMRDEKLAS---LVTMTQALCRAYLMRRefvKMMERRDAIYTIQYNVRSFMNVK 827
Cdd:PTZ00014 751 GKTMVFLKKDAAKELTQIQREKLAAwepLVSVLEALILKIKKKR---KVRKNIKSLVRIQAHLRRHLVIA 817
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
101-734 |
1.17e-127 |
|
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: 417.77 E-value: 1.17e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRG-----KKRMEAP----PHIFSVSDNAYQFMLTD- 170
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRQegllrSQGIESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 171 RENQSVLITGESGAGKTVNTKRVIQYFATVAVQGPEKKKEQASGKmQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGK 250
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELG-KLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 251 FIRIHFGTSGKLASADIETYLLEKSRVTFQLPDERGYHIFYQMM------TNHKPELIE-MTLITTNPYDFPMCSQGQI- 322
Cdd:cd14908 160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLrggdeeEHEKYEFHDgITGGLQLPNEFHYTGQGGAp 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 323 TVASIDDKEELVATDTAIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGTEEADKIGY---LLGLNSADM 399
Cdd:cd14908 240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARvakLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 400 LKALCYPRVKVGNEFVTKGQTVPQVYNSVSALSKSIYERMFLWMVVRINQML--DTKQQRNFFIGVLDIAGFEIFDFNSM 477
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 478 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGmDLAACIELIE-KPLGIFSILEEECMFP-KATDTSFKNK 555
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 556 LYDQHLGKCN-----AFQKPKPAKGKAEAHFSLVHYAGTVDYNI-SGWLDKNKDPLnesvvqlyQKSSVKLLATlyppvv 629
Cdd:cd14908 479 LYETYLPEKNqthseNTRFEATSIQKTKLIFAVRHFAGQVQYTVeTTFCEKNKDEI--------PLTADSLFES------ 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 630 eetgggkkggkkkggsmqtvSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRK 709
Cdd:cd14908 545 --------------------GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARS 604
|
650 660
....*....|....*....|....*
gi 288856329 710 GFPSRILYADFKQRYKVLnASVIPE 734
Cdd:cd14908 605 GYPVRLPHKDFFKRYRML-LPLIPE 628
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
103-768 |
3.23e-127 |
|
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: 414.83 E-value: 3.23e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 103 VLYNLKERYAA--WMIYTYSGLFCATVNPYKWLPVYDaevVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRE---NQSVL 177
Cdd:cd14891 3 ILHNLEERSKLdnQRPYTFMANVLIAVNPLRRLPEPD---KSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQSIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 178 ITGESGAGKTVNTKRVIQYFATVAVQGPEKKKEQASGKMQG------SLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKF 251
Cdd:cd14891 80 ISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKKrklsvtSLDERLMDTNPILESFGNAKTLRNHNSSRFGKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 252 IRIHFGTSG-KLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEmTLITTNPYDFPMCSQ-GQITVASIDD 329
Cdd:cd14891 160 MKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLK-ELLLLSPEDFIYLNQsGCVSDDNIDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 330 KEELVATDTAIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREE----QAEPDGTEEADKIGYLLGLNSADMLKALCY 405
Cdd:cd14891 239 AANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEgeaeIASESDKEALATAAELLGVDEEALEKVITQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 406 PRVKVGNEFVTKGQTVPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNFFIGVLDIAGFEIFD-FNSMEQLCINF 484
Cdd:cd14891 319 REIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLINY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 485 TNEKLQQFFNHHMFVLEQEEYKKEGI-----VWEfidfgmDLAACIELI-EKPLGIFSILEEECMFPKATDTSFKNKLYD 558
Cdd:cd14891 399 ANEALQATFNQQVFIAEQELYKSEGIdvgviTWP------DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 559 QHlGKCNAFQKPKPaKGKAEAhFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYqKSSVKLLAtlyppvveetgggkkg 638
Cdd:cd14891 473 TH-KRHPCFPRPHP-KDMREM-FIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLL-ASSAKFSD---------------- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 639 gkkkggSMQTvssqfrenlgkLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYA 718
Cdd:cd14891 533 ------QMQE-----------LVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYA 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 288856329 719 DFKQRYK-VLNASVIPegQFIDNKKA-SEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd14891 596 ELVDVYKpVLPPSVTR--LFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
101-725 |
6.06e-127 |
|
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: 416.99 E-value: 6.06e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLP-VYDAEVVAAYR--------GKKRMEAPPHIFSVSDNAYQFML-TD 170
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 171 RENQSVLITGESGAGKTVNTKRVIQYFATVAvqgpekkKEQASGKMQGS----LEDQIIAANPLLEAYGNAKTVRNDNSS 246
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVG-------RDQSSTEQEGSdaveIGKRILQTNPILESFGNAQTIRNDNSS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 247 RFGKFIRIHFGTSGKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEmTLITTNPYDFPM-----CSQGQ 321
Cdd:cd14902 154 RFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLD-LLGLQKGGKYELlnsygPSFAR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 322 ITVASIDDKEELVATDTAIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGTEEA---DKIGYLLGLNSAD 398
Cdd:cd14902 233 KRAVADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRfhlAKCAELMGVDVDK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 399 MLKALCYPRVKVGNEFVTKGQTVPQVYNSVSALSKSIYERMFLWMVVRINQMLD-------TKQQRNFF--IGVLDIAGF 469
Cdd:cd14902 313 LETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsISDEDEELatIGILDIFGF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 470 EIFDFNSMEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGmDLAACIELIE-KPLGIFSILEEECMFPKAT 548
Cdd:cd14902 393 ESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 549 DTSFKNKLYDQHLGkcnafqkpkpakgkaEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLL-ATLYPP 627
Cdd:cd14902 472 NQALSTKFYRYHGG---------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVvAIGADE 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 628 VVEETGGGKKGGKKKGGSM---QTVSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGI 704
Cdd:cd14902 537 NRDSPGADNGAAGRRRYSMlraPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAV 616
|
650 660
....*....|....*....|.
gi 288856329 705 RICRKGFPSRILYADFKQRYK 725
Cdd:cd14902 617 RIARHGYSVRLAHASFIELFS 637
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
101-768 |
5.45e-123 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 405.11 E-value: 5.45e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLP-VYDaevVAAYRGK--KRMEAPPHIFSVSDNAYQFMLT-------D 170
Cdd:cd14895 1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEmpGWTALPPHVFSIAEGAYRSLRRrlhepgaS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 171 RENQSVLITGESGAGKTVNTKRVIQYFATVAVqgpEKKKEQASGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGK 250
Cdd:cd14895 78 KKNQTILVSGESGAGKTETTKFIMNYLAESSK---HTTATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 251 FIRIHFG-----TSGKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPE-LIEMTLITTNPYDFPMCSQGQITV 324
Cdd:cd14895 155 FVRMFFEgheldTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDmKLELQLELLSAQEFQYISGGQCYQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 325 AS--IDDKEELVATDTAIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGT------------------EE 384
Cdd:cd14895 235 RNdgVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAasapcrlasaspssltvqQH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 385 ADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKGQTVPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNF----- 459
Cdd:cd14895 315 LDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALNpnkaa 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 460 ------FIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGmDLAACIELIE-KPL 532
Cdd:cd14895 395 nkdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYE-DNSVCLEMLEqRPS 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 533 GIFSILEEECMFPKATDTSFKNKLYdQHLGKCNAFQKPKpaKGKAEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQL 612
Cdd:cd14895 474 GIFSLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASR--TDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 613 YQKSSVKLLATLYPP--VVEETGGGKKGGKKKGGSMQTVS----SQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLM 686
Cdd:cd14895 551 LGKTSDAHLRELFEFfkASESAELSLGQPKLRRRSSVLSSvgigSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQF 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 687 ENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASvipegQFIDNKKASEkLLGSIDVNHDEyrFGHTKVF 766
Cdd:cd14895 631 DMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAA-----KNASDATASA-LIETLKVDHAE--LGKTRVF 702
|
..
gi 288856329 767 FK 768
Cdd:cd14895 703 LR 704
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
101-768 |
1.13e-119 |
|
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: 393.58 E-value: 1.13e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRG-KKRMEAPPHIFSVSDNAYQFMLTDRENQSVLIT 179
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 180 GESGAGKTVNTKRVIQYFATvavqgpekkkeQASGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTS 259
Cdd:cd14876 81 GESGAGKTEATKQIMRYFAS-----------AKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 260 GKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIE-MTLITTNPYDF--PMCsqgqITVASIDDKEELVAT 336
Cdd:cd14876 150 GGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSkYHLLGLKEYKFlnPKC----LDVPGIDDVADFEEV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 337 DTAIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQ-----AEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVG 411
Cdd:cd14876 226 LESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVddaaaISNESLEVFKEACSLLFLDPEALKRELTVKVTKAG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 412 NEFVTKGQTVPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQ 491
Cdd:cd14876 306 GQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 492 FFNHHMFVLEQEEYKKEGIVWEFIDFgMDLAACIE-LIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKcnafQKP 570
Cdd:cd14876 386 NFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSN----GKF 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 571 KPAKGKAEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPVVEETGGGKKGgkkkggsmQTVS 650
Cdd:cd14876 461 KPAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKGKIAKG--------SLIG 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 651 SQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAS 730
Cdd:cd14876 533 SQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLG 612
|
650 660 670
....*....|....*....|....*....|....*...
gi 288856329 731 vIPEGQFIDNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd14876 613 -IANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
101-768 |
3.85e-115 |
|
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: 380.66 E-value: 3.85e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITG 180
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 181 ESGAGKTVNTKRVIQYFATVAVQGPEKKKEQASGKMqgsledqiiaanPLLEAYGNAKTVRNDNSSRFGKFIRIHFgTSG 260
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQTEDRLRQPEDVL------------PILESFGHAKTILNANASRFGQVLRLHL-QHG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 261 KLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEMtLITTNPYDFPMCSQGQI-TVASIDDKEELVATDTA 339
Cdd:cd14896 148 VIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQ-LSLQGPETYYYLNQGGAcRLQGKEDAQDFEGLLKA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 340 IDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQRE--EQAEPDGTEEADKIGYLLGLnSADMLKALCYPRVKVGN-EFVT 416
Cdd:cd14896 227 LQGLGLCAEELTAIWAVLAAILQLGNICFSSSEREsqEVAAVSSWAEIHTAARLLQV-PPERLEGAVTHRVTETPyGRVS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 417 KGQTVPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNFF--IGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFN 494
Cdd:cd14896 306 RPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSS 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 495 HHMFVLEQEEYKKEGIVWEFIDfGMDLAACIELI-EKPLGIFSILEEECMFPKATDTSFKNKLYDQHlGKCNAFQKPK-- 571
Cdd:cd14896 386 QTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQlp 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 572 -PAkgkaeahFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYppvveetgGGKKGGKKKGGSMQTVS 650
Cdd:cd14896 464 lPV-------FTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLF--------QEAEPQYGLGQGKPTLA 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 651 SQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAs 730
Cdd:cd14896 529 SRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGS- 607
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 288856329 731 vipEGQ--FIDNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd14896 608 ---ERQeaLSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
102-730 |
8.20e-111 |
|
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: 370.85 E-value: 8.20e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 102 SVLYNLKERYAAWMIYTYSGLFCATVNPYKWLP-VYDAEVVAAYRGKKRM-EAPPHIFSVSDNAYQFMLTDRENQSVLIT 179
Cdd:cd14906 2 IILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQNkSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 180 GESGAGKTVNTKRVIQYFatVAVQGPEKKKEQASGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHF-GT 258
Cdd:cd14906 82 GESGSGKTEASKTILQYL--INTSSSNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFrSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 259 SGKLASADIETYLLEKSRVTFQlPDER--GYHIFYQMMTNHKPELIEMTLITTNPYDFPMCSQGQITVASI--------- 327
Cdd:cd14906 160 DGKIDGASIETYLLEKSRISHR-PDNInlSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFksqssnkns 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 328 ------DDKEELVATDTAIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQ---REEQAEPDGTEEADKIGYLLGLNSAD 398
Cdd:cd14906 239 nhnnktESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYIESV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 399 MLKALCYPRVKVGNE--FVTKGQTVPQVYNSVSALSKSIYERMFLWMVVRIN-QMLDTKQQR----------NFFIGVLD 465
Cdd:cd14906 319 FKQALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINrKFNQNTQSNdlaggsnkknNLFIGVLD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 466 IAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIVWEFIDFgMDLAACIELIE-KPLGIFSILEEECMF 544
Cdd:cd14906 399 IFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIM 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 545 PKATDTSFKNKlYDQHLGKCNAFQKPKPAKGKaeahFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATL 624
Cdd:cd14906 478 PKGSEQSLLEK-YNKQYHNTNQYYQRTLAKGT----LGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 625 YPPVVEETGGGKKGGKKKGgsmqTVSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGI 704
Cdd:cd14906 553 FQQQITSTTNTTKKQTQSN----TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTI 628
|
650 660
....*....|....*....|....*.
gi 288856329 705 RICRKGFPSRILYADFKQRYKVLNAS 730
Cdd:cd14906 629 KVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
102-727 |
1.17e-110 |
|
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: 368.41 E-value: 1.17e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 102 SVLYNLKERYAAWMIYTYSGLFCATVNPYKWLP-VYDAEVVAAYRGKKRMEA-PPHIFSVSDNAYQFMLTDRE--NQSVL 177
Cdd:cd14880 2 TVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQPQKlKPHIFTVGEQTYRNVKSLIEpvNQSIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 178 ITGESGAGKTVNTKRVIQYFATVAVQGPEKKkeqaSGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFG 257
Cdd:cd14880 82 VSGESGAGKTWTSRCLMKFYAVVAASPTSWE----SHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 258 TSGKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTN-HKPELIEMTLITTNPYDFPMCSQGQItvasidDKEELVAT 336
Cdd:cd14880 158 RAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGaSADERLQWHLPEGAAFSWLPNPERNL------EEDCFEVT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 337 DTAIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEP--DGTEEADKI-GYLLGLNSADMLKALCYPRVKVGne 413
Cdd:cd14880 232 REAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQpmDDTKESVRTsALLLKLPEDHLLETLQIRTIRAG-- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 414 fvtKGQTVPQVYNSVS-------ALSKSIYERMFLWMVVRINQMLDTKQQR-NFFIGVLDIAGFEIFDFNSMEQLCINFT 485
Cdd:cd14880 310 ---KQQQVFKKPCSRAecdtrrdCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 486 NEKLQQFFNHHMFVLEQEEYKKEGIVWEFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKC 564
Cdd:cd14880 387 NEKLQQHFVAHYLRAQQEEYAVEGLEWSFINY-QDNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALAGN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 565 NAFQKPKPAKgkaEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYpPVVEETGGGKKGGKKKGG 644
Cdd:cd14880 466 PCLGHNKLSR---EPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLF-PANPEEKTQEEPSGQSRA 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 645 SMQTVSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 724
Cdd:cd14880 542 PVLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERY 621
|
...
gi 288856329 725 KVL 727
Cdd:cd14880 622 KLL 624
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
107-768 |
4.32e-109 |
|
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: 363.44 E-value: 4.32e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 107 LKERYAAWMIYTYSGLFCATVNPYKWLP-VYDAEVVAAYRGKKRM-----EAPPHIFSVSDNAYQFMLTDRENQSVLITG 180
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 181 ESGAGKTVNTKRVIQYFATVAVQGPEKkkeqasgkmqgsLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSG 260
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAYGHSTSSTD------------VQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 261 KLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIE-MTLITTNPYDFPMCSQGqITVASIDDKEELVATDTA 339
Cdd:cd14886 155 GLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKsLGFKSLESYNFLNASKC-YDAPGIDDQKEFAPVRSQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 340 IDILgFNNEEKMGIYKFTGAVLHHGNMKFKQKQR---EEQAEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEFVT 416
Cdd:cd14886 234 LEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETII 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 417 KGQTVPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHH 496
Cdd:cd14886 313 SPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 497 MFVLEQEEYKKEGIVWEFIDFgMDLAACIELIEKP-LGIFSILEEECMFPKATDTSFKNklydqhlgKCNAFQKPK---P 572
Cdd:cd14886 393 VFKSEIQEYEIEGIDHSMITF-TDNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTS--------SCKSKIKNNsfiP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 573 AKGkAEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPVVEETGGGKKggkkkggsmQTVSSQ 652
Cdd:cd14886 464 GKG-SQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNMKG---------KFLGST 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 653 FRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL---NA 729
Cdd:cd14886 534 FQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILishNS 613
|
650 660 670
....*....|....*....|....*....|....*....
gi 288856329 730 SVIPEGQfiDNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd14886 614 SSQNAGE--DLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
102-725 |
1.47e-107 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 361.34 E-value: 1.47e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 102 SVLYNLKERYAAWMIYTYSGLFCATVNPYKWLP-VYDAEVVAAYR-------GKKRMEA---PPHIFSVSDNAYQFMLTD 170
Cdd:cd14899 2 SILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhnsqfGDRVTSTdprEPHLFAVARAAYIDIVQN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 171 RENQSVLITGESGAGKTVNTKRVIQYFATVAVQG-----PEKKKEQASGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNS 245
Cdd:cd14899 82 GRSQSILISGESGAGKTEATKIIMTYFAVHCGTGnnnltNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 246 SRFGKFIRIHF-GTSGKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNH----KPELIEMTLITTNPYDFPMCSQG 320
Cdd:cd14899 162 SRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 321 QITVA--SIDDKEELVATDTAIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQ--KQREEQAEPDGTEEA----------D 386
Cdd:cd14899 242 LCSKRrdGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhfT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 387 KIGYLLGLNSADMLKALCYPRVKVGNEFVTKGQTVPQVYNSVSALSKSIYERMFLWMVVRINQML--------------- 451
Cdd:cd14899 322 KAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesdv 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 452 DTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGMDlAACIELIE-K 530
Cdd:cd14899 402 DDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFEhR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 531 PLGIFSILEEECMFPKATDTSFKNKLYDQHLGKCNAFQKPKPAKGKAEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVV 610
Cdd:cd14899 481 PIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 611 QLYQKSSVKLLATLYPPVVEETGGGKKGGKKKGGSMQ----------TVSSQFRENLGKLMTNLRSTHPHFVRCLIPNES 680
Cdd:cd14899 561 QLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRrraksaiaavSVGTQFKIQLNELLSTVRATTPRYVRCIKPNDS 640
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 288856329 681 KTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 725
Cdd:cd14899 641 HVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
102-768 |
7.62e-102 |
|
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: 342.95 E-value: 7.62e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 102 SVLYNLKERYAAWMI-YTYSGLFCATVNPYKWLPVYDAEVVAAYRG--KKRMeAPPHIFSVSDNAY-QFMLTDRENQSVL 177
Cdd:cd14875 2 TLLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlpDPRL-LPPHIWQVAHKAFnAIFVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 178 ITGESGAGKTVNTKRVIQYFAtvavqgpEKKKEQASGKMQGSLEDQIIA----ANPLLEAYGNAKTVRNDNSSRFGKFIR 253
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLG-------QLSYMHSSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 254 IHF-GTSGKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEMTLITTNPYDFPMCSQGQITV------AS 326
Cdd:cd14875 154 LYFdPTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGNTFVrrgvdgKT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 327 IDDKEELVATDTAIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGTEEADKIGyLLGLNSADMLKalCYp 406
Cdd:cd14875 234 LDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFLTACR-LLQLDPAKLRE--CF- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 407 RVKVGNEFVTKGQTVPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNF--FIGVLDIAGFEIFDFNSMEQLCINF 484
Cdd:cd14875 310 LVKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDCSGckYIGLLDIFGFENFTRNSFEQLCINY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 485 TNEKLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGmDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYDQHLGK 563
Cdd:cd14875 390 ANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 564 CNAFQKPKPAkgkAEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPpvveetgggkkGGKKKG 643
Cdd:cd14875 469 SPYFVLPKST---IPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLS-----------TEKGLA 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 644 GSMQTVSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADF-KQ 722
Cdd:cd14875 535 RRKQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFcRY 614
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 288856329 723 RYKVLNASVIPEGQFIDNKKASEKLLGS----IDVNHDEYRFGHTKVFFK 768
Cdd:cd14875 615 FYLIMPRSTASLFKQEKYSEAAKDFLAYyqrlYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
102-768 |
1.30e-94 |
|
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: 322.72 E-value: 1.30e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 102 SVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITGE 181
Cdd:cd01386 2 SVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 182 SGAGKTVNTKRVIQYFATVAvqgpekkkeqASGKMQGSLEdQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGK 261
Cdd:cd01386 82 SGSGKTTNCRHILEYLVTAA----------GSVGGVLSVE-KLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 262 LASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPEL---IEMTLITTNPYDFPMCSQgqitvaSIDDKE----ELV 334
Cdd:cd01386 151 LASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALrteLHLNQLAESNSFGIVPLQ------KPEDKQkaaaAFS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 335 ATDTAIDILGFNNEEKMGIYKFTGAVLHHGN---MKFKQKQREEQAEPdgtEEADKIGYLLGLNSADMLKALCYPRVKVG 411
Cdd:cd01386 225 KLQAAMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFARP---EWAQRAAYLLGCTLEELSSAIFKHHLSGG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 412 NEFVTKGQTVPQVYNS------------VSALSKSIYERMFLWMVVRINQMLDTKQQRNFFIGVLDIAGFEIFDFN---- 475
Cdd:cd01386 302 PQQSTTSSGQESPARSssggpkltgveaLEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsqr 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 476 --SMEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGMDLAACIELIEKPL---------------GIFSIL 538
Cdd:cd01386 382 gaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPqqalvrsdlrdedrrGLLWLL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 539 EEECMFPKATDTSFKNKLYdQHLGKCNAFQKPKPAKgKAEA--HFSLVHYAGT--VDYNISGWLDKNK-DPLNESVVQLY 613
Cdd:cd01386 462 DEEALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLR-RSEGplQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLL 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 614 QKSSVKLLAtlyppvveetgggkkggkkkgGSMQTVSSQFRENLGKLMTNLRSTHPHFVRCLIPN-----------ESKT 682
Cdd:cd01386 540 QESQKETAA---------------------VKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQhnagkderstsSPAA 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 683 PGLMENF-LVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL----NASVIPEGQFIDNKKASEKLLGSIDVNHDE 757
Cdd:cd01386 599 GDELLDVpLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLapplTKKLGLNSEVADERKAVEELLEELDLEKSS 678
|
730
....*....|.
gi 288856329 758 YRFGHTKVFFK 768
Cdd:cd01386 679 YRIGLSQVFFR 689
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
102-736 |
3.81e-94 |
|
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: 320.22 E-value: 3.81e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 102 SVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYR---GKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLI 178
Cdd:cd14878 2 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 179 TGESGAGKTVNTKRVIQYFATvavqgpekkkeqASGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGT 258
Cdd:cd14878 82 SGERGSGKTEASKQIMKHLTC------------RASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 259 SGK-LASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELiEMTLITTNPYDFPMCSQGQ----ITVASIDDKEEL 333
Cdd:cd14878 150 RKKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEE-KYGLHLNNLCAHRYLNQTMredvSTAERSLNREKL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 334 VATDTAIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNE 413
Cdd:cd14878 229 AVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 414 FVTKGQTVPQVYNSVSALSKSIYERMFLWMVVRINQML----DTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKL 489
Cdd:cd14878 309 MIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 490 QQFFNHHMFVLEQEEYKKEGIVWEFI-DFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQ-HLGKCNAF 567
Cdd:cd14878 389 HHYINEVLFLQEQTECVQEGVTMETAySPGNQTGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLlESSNTNAV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 568 QKPK-------PAKGKAEAhFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYppvveetgggkkggk 640
Cdd:cd14878 469 YSPMkdgngnvALKDQGTA-FTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLF--------------- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 641 kkGGSMQTVSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADF 720
Cdd:cd14878 533 --QSKLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDF 610
|
650
....*....|....*.
gi 288856329 721 KQRYKVLnASVIPEGQ 736
Cdd:cd14878 611 LSRYKPL-ADTLLGEK 625
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
103-768 |
1.99e-87 |
|
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: 300.01 E-value: 1.99e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 103 VLYNLKERYAAWMIYTYSGLFCATVNPYKwlpVYDAEVvAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITGES 182
Cdd:cd14937 3 VLNMLALRYKKNYIYTIAEPMLISINPYQ---VIDVDI-NEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 183 GAGKTVNTKRVIQYFatvaVQGPEKKKEqasgkMQGSLEDqiiaANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGKL 262
Cdd:cd14937 79 GSGKTEASKLVIKYY----LSGVKEDNE-----ISNTLWD----SNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 263 ASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEMTLITTNPyDFPMCSQGQITVASIDDKEELVATDTAIDI 342
Cdd:cd14937 146 VSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSEN-EYKYIVNKNVVIPEIDDAKDFGNLMISFDK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 343 LGFNNEEKMGIYKFTGAVLhHGNMKFKQ-----KQREEQAEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTK 417
Cdd:cd14937 225 MNMHDMKDDLFLTLSGLLL-LGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 418 GQTVPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHM 497
Cdd:cd14937 304 PLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 498 FVLEQEEYKKEGIVWEFIDFGMDlAACIELIEKPLGIFSILEEECMFPKATDTSfknkLYDQHLGKCNAFQKPKPAKGKA 577
Cdd:cd14937 384 YEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDES----IVSVYTNKFSKHEKYASTKKDI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 578 EAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPV-VEETGGGKkggkkkggsmQTVSSQFREN 656
Cdd:cd14937 459 NKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVeVSESLGRK----------NLITFKYLKN 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 657 LGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRIcRKGFPSRILYADFKQRYKVLNASVIPEGQ 736
Cdd:cd14937 529 LNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDSS 607
|
650 660 670
....*....|....*....|....*....|..
gi 288856329 737 FIDNKKASEKLLGSIDvnHDEYRFGHTKVFFK 768
Cdd:cd14937 608 LTDKEKVSMILQNTVD--PDLYKVGKTMVFLK 637
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
101-768 |
7.88e-87 |
|
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: 301.18 E-value: 7.88e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAA--------WMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRE 172
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 173 NQSVLITGESGAGKTVNTKRVIQYFATVAvqgpekkkEQASGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFI 252
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVS--------DRRHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKML 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 253 RIHFGTSGKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNhkpELIEMTLITTNPYDFPMCSqgqitvasidDKEE 332
Cdd:cd14887 153 LLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNA---AVAAATQKSSAGEGDPEST----------DLRR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 333 LVATDTAIDILGFNNEEkmgIYKFTGAVLHHGNMKFKQKQREEQAEPD-------GTEE--------------------- 384
Cdd:cd14887 220 ITAAMKTVGIGGGEQAD---IFKLLAAILHLGNVEFTTDQEPETSKKRkltsvsvGCEEtaadrshssevkclssglkvt 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 385 ----------ADKIGYLLGLNSADMLK-ALCYPRVKVGNEFVTKGQTvpqVYNSvSALSKSIYERMFLWMVVRINQMLDT 453
Cdd:cd14887 297 easrkhlktvARLLGLPPGVEGEEMLRlALVSRSVRETRSFFDLDGA---AAAR-DAACKNLYSRAFDAVVARINAGLQR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 454 KQQRNF--------------FIGVLDIAGFEIF---DFNSMEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIVWEFI- 515
Cdd:cd14887 373 SAKPSEsdsdedtpsttgtqTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDc 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 516 ---DFGMDLAAC--------IELIEKP--------------LGIFSILEEE-CMFPKATDTSFKNKLYDQHLGKCNA--- 566
Cdd:cd14887 453 safPFSFPLASTltsspsstSPFSPTPsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKNIInsa 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 567 -FQKPKPAKGKAEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKllatlyppVVEETGGGKKGGKKKGGS 645
Cdd:cd14887 533 kYKNITPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLACSTY--------TRLVGSKKNSGVRAISSR 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 646 MQTVSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 725
Cdd:cd14887 605 RSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYE 684
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 288856329 726 vlnaSVIPEG--QFIDNKKASEKLLGSIDVNHDEYRFGHTKVFFK 768
Cdd:cd14887 685 ----TKLPMAlrEALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
102-731 |
6.38e-84 |
|
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: 287.95 E-value: 6.38e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 102 SVLYNLKERYAAWMIYTYSGLFCATVNPYKwlPVYDAEVVAAYRgKKRMEAPPHIFSVSDNAYQFMLTdRENQSVLITGE 181
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 182 SGAGKTVNTKRVIQYFAtvavqgpekkkEQASGKMqgSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFgtSGK 261
Cdd:cd14898 78 SGSGKTENAKLVIKYLV-----------ERTASTT--SIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--DGK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 262 LASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKpeliemtLITTNPYdFPMCSQGQITVASIDDKEELVATDTAID 341
Cdd:cd14898 143 ITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR-------LNIKNDF-IDTSSTAGNKESIVQLSEKYKMTCSAMK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 342 ILGFNNEEKmgIYKFTGAVLHHGNMKFKQkqrEEQAEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVGNEFVTKGQTV 421
Cdd:cd14898 215 SLGIANFKS--IEDCLLGILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 422 PQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNffIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMFVLE 501
Cdd:cd14898 290 KQARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAK 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 502 QEEYKKEGIVWEFIDFgMDLAACIELIEKPLGIFSILEEECMFPKAT--DTSFKNKLYDQHLGKCNAFQKPKpakgkaea 579
Cdd:cd14898 368 QGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNvkNLLVKIKKYLNGFINTKARDKIK-------- 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 580 hfsLVHYAGTVDYNISGWLDKNKdplnesvvqlyQKSSVKLLATlyPPVVEEtgggkkggkkkgGSMQTVSSQFRENLGK 659
Cdd:cd14898 439 ---VSHYAGDVEYDLRDFLDKNR-----------EKGQLLIFKN--LLINDE------------GSKEDLVKYFKDSMNK 490
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 288856329 660 LMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASV 731
Cdd:cd14898 491 LLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
107-767 |
6.17e-80 |
|
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: 278.66 E-value: 6.17e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 107 LKERYAAWMIYTY---SGLFCatVNPYKWLPVYDAEVVAAYR-------GKKRMEAPPHIFSVSDNAYQFMLTDRENQSV 176
Cdd:cd14879 10 LASRFRSDLPYTRlgsSALVA--VNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRRRSEDQAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 177 LITGESGAGKTVNTKRVIQYFATVAVQGPEKKKeqasgkmqgsLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHF 256
Cdd:cd14879 88 VFLGETGSGKSESRRLLLRQLLRLSSHSKKGTK----------LSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 257 GTSGKLASADIETYLLEKSRVTfQLP-DERGYHIFYQMMTNHKPELIEmTLITTNPYDFPM-----CSQGQITVASiDDK 330
Cdd:cd14879 158 NERGRLIGAKVLDYRLERSRVA-SVPtGERNFHVFYYLLAGASPEERQ-HLGLDDPSDYALlasygCHPLPLGPGS-DDA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 331 EELVATDTAIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQkqreeqaEPDGTEEA---------DKIGYLLGLNSADMLK 401
Cdd:cd14879 235 EGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTY-------DHEGGEESavvkntdvlDIVAAFLGVSPEDLET 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 402 ALCYPRVKVGNEFVTkgqtvpqVY-NSVSA------LSKSIYERMFLWMVVRINQML-DTKQQRNFFIGVLDIAGFEIFD 473
Cdd:cd14879 308 SLTYKTKLVRKELCT-------VFlDPEGAaaqrdeLARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQNRS 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 474 ---FNSMEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIVWEFIDFgMDLAACIELI-EKPLGIFSILEEEC-MFPKAT 548
Cdd:cd14879 381 stgGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQTrRMPKKT 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 549 DTSFKNKLYDQHLGKCNAFQKPKPAKGKAEAHFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLyqkssvkLLATlyppv 628
Cdd:cd14879 460 DEQMLEALRKRFGNHSSFIAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNL-------LRGA----- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 629 veetgggkkggkkkggsmqtvsSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICR 708
Cdd:cd14879 528 ----------------------TQLNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLR 585
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 288856329 709 KGFPSRILYADFKQRYKvlnasviPEGQFIDNKKASEKLLGSIDVNHDEYRFGHTKVFF 767
Cdd:cd14879 586 VEYVVSLEHAEFCERYK-------STLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
101-716 |
1.04e-70 |
|
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: 252.52 E-value: 1.04e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLP-VYDAEVVAAYRGKKRMEA-------PPHIFSVSDNAYQFMLTDRE 172
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 173 NQSVLITGESGAGKTVNTKRVIQYFATVAVQgpekkkeqasgKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFI 252
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTD-----------SQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRIN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 253 RIHFGT---------SGKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEMTLITTN--PYDFPMCSQGQ 321
Cdd:cd14884 150 LLIFEEventqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNcgVYGLLNPDESH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 322 ----------ITVASIDDKEELVATDTA-----IDILGFNNEEKMGIYKF---TGAVLHHGNMKFKQKQReeqaepdgte 383
Cdd:cd14884 230 qkrsvkgtlrLGSDSLDPSEEEKAKDEKnfvalLHGLHYIKYDERQINEFfdiIAGILHLGNRAYKAAAE---------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 384 eadkigyLLGLNSADMLKALCYPRVKVGNEFVTKGQTVPQVYNSVSALSKSIYERMFLWMVVRINQML------------ 451
Cdd:cd14884 300 -------CLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckekdesdne 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 452 DTKQQRNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIVW--EFIDFGMDLAACIELIE 529
Cdd:cd14884 373 DIYSINEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICcsDVAPSYSDTLIFIAKIF 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 530 KPLGIFSILEEECMfpKATDTSFKNKLYD----QHLGKCNAFQK--PKPAKGKAEAH------FSLVHYAGTVDYNISGW 597
Cdd:cd14884 453 RRLDDITKLKNQGQ--KKTDDHFFRYLLNnerqQQLEGKVSYGFvlNHDADGTAKKQnikkniFFIRHYAGLVTYRINNW 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 598 LDKNKDPLNESVVQLYQKSSVKLLatlyppvveetggGKKGGKKKGGSMQTVSSQFRENLGKLMTNLRSTHPHFVRCLIP 677
Cdd:cd14884 531 IDKNSDKIETSIETLISCSSNRFL-------------REANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFLP 597
|
650 660 670
....*....|....*....|....*....|....*....
gi 288856329 678 NESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRIL 716
Cdd:cd14884 598 NAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
174-757 |
7.10e-70 |
|
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: 248.49 E-value: 7.10e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 174 QSVLITGESGAGKTVNTKRVIQYFATVAVQGPEKK--KEQAsgkmqgsledqiiAANPLLEAYGNAKTVRNDNSSRFGKF 251
Cdd:cd14881 69 QAIILSGTSGSGKTYASMLLLRQLFDVAGGGPETDafKHLA-------------AAFTVLRSLGSAKTATNSESSRIGHF 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 252 IRIHFgTSGKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKP-ELIEMTLITTNPYDFPMCSQGQITVASIDDK 330
Cdd:cd14881 136 IEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQeERVKLHLDGYSPANLRYLSHGDTRQNEAEDA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 331 EELVATDTAIDILGFNNEEKMGIYkftGAVLHHGNMKFKQKQrEEQAEPDGTEEADKIGYLLGLNSADMLKALcYPRVKV 410
Cdd:cd14881 215 ARFQAWKACLGILGIPFLDVVRVL---AAVLLLGNVQFIDGG-GLEVDVKGETELKSVAALLGVSGAALFRGL-TTRTHN 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 411 gnefvTKGQTV-----PQVYNSV-SALSKSIYERMFLWMVVRINQMLD-----TKQQRNFFIGVLDIAGFEIFDFNSMEQ 479
Cdd:cd14881 290 -----ARGQLVksvcdANMSNMTrDALAKALYCRTVATIVRRANSLKRlgstlGTHATDGFIGILDMFGFEDPKPSQLEH 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 480 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIVWEF-IDFgMDLAACIELIEK-PLGIFSILEEECMfPKATDTSFKNKLY 557
Cdd:cd14881 365 LCINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIK 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 558 DQHLGKCNAFQkPKPAKGKAeahFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLlatlyppvveetgggkk 637
Cdd:cd14881 443 VQHRQNPRLFE-AKPQDDRM---FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNF----------------- 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 638 ggkkkggSMQTVSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILY 717
Cdd:cd14881 502 -------GFATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRF 574
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 288856329 718 ADFKQRYKVLnASVIPEGQFIDNKKASEKLLGSIDVNHDE 757
Cdd:cd14881 575 KAFNARYRLL-APFRLLRRVEEKALEDCALILQFLEAQPP 613
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
103-768 |
9.96e-63 |
|
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: 227.45 E-value: 9.96e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 103 VLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYrgkkrmeappHIFSVSDNAYQFMLTDREN-QSVLITGE 181
Cdd:cd14874 3 IAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFGGE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 182 SGAGKTVNTKRVIQYFATvavqgpeKKKEQASGKMQGSLEDqiiaanpLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGK 261
Cdd:cd14874 73 SGSGKSYNAFQVFKYLTS-------QPKSKVTTKHSSAIES-------VFKSFGCAKTLKNDEATRFGCSIDLLYKRNVL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 262 LASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEMTLITtNPYDFPMCSQGQITVASIDDKEELVATDTAID 341
Cdd:cd14874 139 TGLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIK-GLQKFFYINQGNSTENIQSDVNHFKHLEDALH 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 342 ILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQ----REEQAEPDGTEEADKIGYLLGLNsADMLKALCYPRVKVGNEFvtk 417
Cdd:cd14874 218 VLGFSDDHCISIYKIISTILHIGNIYFRTKRnpnvEQDVVEIGNMSEVKWVAFLLEVD-FDQLVNFLLPKSEDGTTI--- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 418 gqTVPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQrNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHM 497
Cdd:cd14874 294 --DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLH-TGVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHS 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 498 FVLEQEEYKKEGIVwefIDFGM----DLAACIELI-EKPLGIFSILEEECMFPKATDTSFknklydqhLGKCNAFQKPKP 572
Cdd:cd14874 371 FHDQLVDYAKDGIS---VDYKVpnsiENGKTVELLfKKPYGLLPLLTDECKFPKGSHESY--------LEHCNLNHTDRS 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 573 AKGKAEA----HFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLATLYPPVVEETGGGkkggkkkggsMQT 648
Cdd:cd14874 440 SYGKARNkerlEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSDM----------IVS 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 649 VSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 728
Cdd:cd14874 510 QAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLL 589
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 288856329 729 ASVIPEGQfiDNKKASEKLLGSIDVNHDE-YRFGHTKVFFK 768
Cdd:cd14874 590 PGDIAMCQ--NEKEIIQDILQGQGVKYENdFKIGTEYVFLR 628
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
104-725 |
1.49e-58 |
|
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: 217.53 E-value: 1.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 104 LYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRM----------EAPPHIFSVSDNAYQFMLTDREN 173
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQtplyekdtvnDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 174 QSVLITGESGAGKTVNTKRVIQYFATVAVQ-GPEKKKEQASGKMQgSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFI 252
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDEtEPRPDSEGASGVLH-PIGQQILHAFTILEAFGNAATRQNRNSSRFAKMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 253 RIHFGTSGKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMT--NHKPELIEMTLITTNPYDFPMCSQG--QITVASID 328
Cdd:cd14893 163 SVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAgvQHDPTLRDSLEMNKCVNEFVMLKQAdpLATNFALD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 329 --DKEELVATDTAIDIlgfNNEEKMGIYKFTGAVLHHGNMKF----KQKQREEQAEPDGTEEA------DKIGYLLGLNS 396
Cdd:cd14893 243 arDYRDLMSSFSALRI---RKNQRVEIVRIVAALLHLGNVDFvpdpEGGKSVGGANSTTVSDAqscalkDPAQILLAAKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 397 ADMLKALC--YPRV-----KVGNEFVT--KGQTVPQVYNSVSALSKSIYERMFLWMVVRINQML----DTKQQRNFFIG- 462
Cdd:cd14893 320 LEVEPVVLdnYFRTrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNIVINs 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 463 ----VLDIAGFEIFD--FNSMEQLCINFTNEKLQQFFNHHMFV-----LEQEEYKKEG--IVWEFIDFGMDLAACIELIE 529
Cdd:cd14893 400 qgvhVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVENrlTVNSNVDITSEQEKCLQLFE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 530 -KPLGIFSILEEECMFPKATDTSFKNKLYDQHlGKCNAFQKPKPAKGKAEAH----------FSLVHYAGTVDYNISGWL 598
Cdd:cd14893 480 dKPFGIFDLLTENCKVRLPNDEDFVNKLFSGN-EAVGGLSRPNMGADTTNEYlapskdwrllFIVQHHCGKVTYNGKGLS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 599 DKNKDPLNESVVQLYQKSSVKLL-----ATLYPPVVEETGGGKKGGKKKGGSMQTVSSQFRE--NLGK------------ 659
Cdd:cd14893 559 SKNMLSISSTCAAIMQSSKNAVLhavgaAQMAAASSEKAAKQTEERGSTSSKFRKSASSAREskNITDsaatdvynqada 638
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 288856329 660 LMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 725
Cdd:cd14893 639 LLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
102-727 |
2.17e-58 |
|
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: 214.60 E-value: 2.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 102 SVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITGE 181
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 182 SGAGKTVNTKRVIQYFATVavqgpekkkeqasGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGK 261
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYL-------------GDGNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 262 LASADIETYLLEKSRVTFQLPDERGYHIFYQMM--TNHKPELIEMTLITTNPYDF---PMCSQGQITVASIDDKEELVAT 336
Cdd:cd14882 149 MSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYdfIEAQNRLKEYNLKAGRNYRYlriPPEVPPSKLKYRRDDPEGNVER 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 337 ----DTAIDILGFNNEEKMGIYKFTGAVLHHGNMKFKQKQREeqAEPDGTEEADKIGYLLGLNSADMLKALCYPRVKVGN 412
Cdd:cd14882 229 ykefEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYCLIKGG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 413 EFVTKGQTVPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQ---RNFFIGVLDIAGFEIFDFNSMEQLCINFTNEKL 489
Cdd:cd14882 307 SAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPRAvfgDKYSISIHDMFGFECFHRNRLEQLMVNTLNEQM 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 490 QQFFNHHMFVLEQEEYKKEGIVWEFIDFGMDLAACIELIEKPLGIFSILEEecmfpKATDTSFKNKLYDQHLGKCNAFQK 569
Cdd:cd14882 387 QYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDD-----ASRSCQDQNYIMDRIKEKHSQFVK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 570 PkpakgkAEAH-FSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKSS---VKLLATlyppvveetgggkkggKKKGGS 645
Cdd:cd14882 462 K------HSAHeFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLdesVKLMFT----------------NSQVRN 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 646 MQTVSSQFR----ENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYADFK 721
Cdd:cd14882 520 MRTLAATFRatslELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFL 599
|
....*.
gi 288856329 722 QRYKVL 727
Cdd:cd14882 600 RRYQFL 605
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
107-768 |
1.08e-57 |
|
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: 213.42 E-value: 1.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 107 LKERYAAWMIYTYSGLFCATVNPYKWLP-VYDAEVVAAYRGKKRMeaPPHIFSVSDNAYQFMLTDRENQSVLITGESGAG 185
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYNQRRGL--PPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 186 KTVNTKRVIQYFATVAVQGPEkkkeqasgkmqgSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGKLASA 265
Cdd:cd14905 85 KSENTKIIIQYLLTTDLSRSK------------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 266 DIETYLLEKSRVTFQLPDERGYHIFYQMMTN-HKPELIEMTLITTNPYDFpMCSQGQITVASIDDKEELVATDTAIDILG 344
Cdd:cd14905 153 KLYSYFLDENRVTYQNKGERNFHIFYQFLKGiTDEEKAAYQLGDINSYHY-LNQGGSISVESIDDNRVFDRLKMSFVFFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 345 FNNEEKMGIYKFTGAVLHHGNMKFKQKQREEQAEPDGTEEAdkIGYLLGLNSADMLKALCYPRVKVGNEFVtkgqtvpqv 424
Cdd:cd14905 232 FPSEKIDLIFKTLSFIIILGNVTFFQKNGKTEVKDRTLIES--LSHNITFDSTKLENILISDRSMPVNEAV--------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 425 yNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNfFIGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMFVLEQEE 504
Cdd:cd14905 301 -ENRDSLARSLYSALFHWIIDFLNSKLKPTQYSH-TLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQRE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 505 YKKEGIVWEFIDFGMDLAACIELIEKplgIFSILEEECMFPKATDTSFKNKLYDqHLGKCNAFQKpKPAKgkaeahFSLV 584
Cdd:cd14905 379 YQTERIPWMTPISFKDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKLQN-FLSRHHLFGK-KPNK------FGIE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 585 HYAGTVDYNISGWLDKNKDPLNESVVQLYQKSSVKLLAT------LYPPVVEETGGGKKGGKKKGGSMQTVS------SQ 652
Cdd:cd14905 448 HYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLFSrdgvfnINATVAELNQMFDAKNTAKKSPLSIVKvllscgSN 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 653 FRENL-----------------------GKLMTNLRSTHP---------HFVRCLIPNESKTPGLMENFLVIHQLRCNGV 700
Cdd:cd14905 528 NPNNVnnpnnnsgggggggnsgggsgsgGSTYTTYSSTNKainnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQIKSLCL 607
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 288856329 701 LEGIRICRKGFPSRILYADFKQRYKVlnasvipegqFIDNKKASEKLLGSI---DVNHDE-----YRFGHTKVFFK 768
Cdd:cd14905 608 LETTRIQRFGYTIHYNNKIFFDRFSF----------FFQNQRNFQNLFEKLkenDINIDSilpppIQVGNTKIFLR 673
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
123-254 |
1.12e-57 |
|
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: 197.18 E-value: 1.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 123 FCATVNPYKWLPVY-DAEVVAAYRGKKRMEAPPHIFSVSDNAYQFMLTDRENQSVLITGESGAGKTVNTKRVIQYFATVA 201
Cdd:cd01363 1 VLVRVNPFKELPIYrDSKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 288856329 202 VQGPEKKKEQAS---GKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRFGKFIRI 254
Cdd:cd01363 81 FNGINKGETEGWvylTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
101-766 |
5.05e-47 |
|
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: 181.96 E-value: 5.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 101 PSVLYNLKERYAAWMIYTYSGLFCATVNPYKWLPVYDAEVVAAYRGKKRME-APPHIFSVSDNAYQFMLTDRENQSVLIT 179
Cdd:cd14938 1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEdLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 180 GESGAGKTVNTKRVIQYFA-----------TVAVQGPEKKKEQASGKMQGSLEDQIIAANPLLEAYGNAKTVRNDNSSRF 248
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAyqvkgsrrlptNLNDQEEDNIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 249 GKFIRIHFGTSgKLASADIETYLLEKSRVTFQLPDERGYHIFYQMMTNHKPELIEMTLItTNPYDFPMCSQGQITVASID 328
Cdd:cd14938 161 SKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFL-KNIENYSMLNNEKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 329 DKEELVATDTAIDILGFNNEEKMGIYKFTGAVLHHGN-------------MKFKQKQRE----------EQAEPDGTEEA 385
Cdd:cd14938 239 YSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNinyetilselENSEDIGLDEN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 386 DKIGYL----LGLNSADMLKALCYPRVkVGNEFVTKGQTVPQVYNSVSALSKSIYERMFLWMVVRINQMLDTKQQRNFF- 460
Cdd:cd14938 319 VKNLLLacklLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNININt 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 461 --IGVLDIAGFEIFDFNSMEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGMDLAACIELIEKPL--GIFS 536
Cdd:cd14938 398 nyINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 537 ILEEECMfPKATDTSFKNKLYDQHLGKCNAFQKPKPAKGKAEAhFSLVHYAGTVDYNISGWLDKNKDPLNESVVQLYQKS 616
Cdd:cd14938 478 LLENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT-FVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 617 SVKLLATL--------YPPVVEETGGGKKG------GKKKGGSMQTVSSQFRENLGKLMTNLRSTHPHFVRCLIPNESK- 681
Cdd:cd14938 556 ENEYMRQFcmfynydnSGNIVEEKRRYSIQsalklfKRRYDTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESKr 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 682 -TPGLMENfLVIHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAsvipegqfiDNKKASEKLLGSIDVNHDEYRF 760
Cdd:cd14938 636 eLCSFDAN-IVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEWMI 705
|
....*.
gi 288856329 761 GHTKVF 766
Cdd:cd14938 706 GNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1146-1928 |
1.13e-33 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 142.50 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1146 EEISERLEEAGGATaaqiemnkkreaefqKLRRDLEESTLQHEATAAALrKKQADSVAELGEQIDNLQRVKQKLEK---- 1221
Cdd:TIGR02168 155 EERRAIFEEAAGIS---------------KYKERRKETERKLERTRENL-DRLEDILNELERQLKSLERQAEKAERykel 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1222 -------EKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDENLRQINDLSAQRARLQTENGEFGRQLE 1294
Cdd:TIGR02168 219 kaelrelELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1295 EKEALV-------SQLTRGKQAFTQQIEELKRQIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKAN 1367
Cdd:TIGR02168 299 RLEQQKqilrerlANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1368 SEVAQWRTKYEtdaiqrteELEESKKKLAQRLQEAEEQIEavnskcaSLEKTKQRLQGEVEDLMIDVERAN--ALAANLD 1445
Cdd:TIGR02168 379 EQLETLRSKVA--------QLELQIASLNNEIERLEARLE-------RLEDRRERLQQEIEELLKKLEEAElkELQAELE 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1446 KKqrnfDKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEET---LDQLETLKRENKNLQQEI-------SDLT 1515
Cdd:TIGR02168 444 EL----EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLqarLDSLERLQENLEGFSEGVkallknqSGLS 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1516 EQLGETGKSIHELEKSKKAVETEKAEIQTAL-----EEAEGTLEH-EESKILRVQ-LELNQVKseiDRKLAEKDEEIEQI 1588
Cdd:TIGR02168 520 GILGVLSELISVDEGYEAAIEAALGGRLQAVvvenlNAAKKAIAFlKQNELGRVTfLPLDSIK---GTEIQGNDREILKN 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1589 KRNSQRITDSMQSTldsevrsrndALRIKKKMEGDLNEMEI--QLSHANRQAAEAQKQLRNVQaqlKDAQLHLDDAVRGQ 1666
Cdd:TIGR02168 597 IEGFLGVAKDLVKF----------DPKLRKALSYLLGGVLVvdDLDNALELAKKLRPGYRIVT---LDGDLVRPGGVITG 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1667 EDMKEQVAMVERRNtlmqsEIEELRAALEQTERGRKVAEQELVDASERVGLLHSQNTSLLNTKKKLEADLVQIQSEVEDT 1746
Cdd:TIGR02168 664 GSAKTNSSILERRR-----EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1747 VQEARNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENlamkggkkQLQKLESRVRELES 1826
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE--------ELKALREALDELRA 810
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1827 EVEAEQRRGADAVKGVRKYERRVKELTYQTEEDKKNVNRLQDLVDKLQLKVKAYKRQSEEAEEQANSHLSKLRKVQHELE 1906
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
810 820
....*....|....*....|..
gi 288856329 1907 EAEERADIAESQVNKLRAKSRD 1928
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSE 912
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
914-1796 |
1.69e-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: 138.65 E-value: 1.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 914 KIQLEAKLKETTERLEDEEEINAELTAKKRKLEDECS------ELKKDIDDLELTLAKVEKEKHAtenkvknltEEMAAQ 987
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLERQAEkaerykELKAELRELELALLVLRLEELR---------EELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 988 DESIGKLTKEKKALQEAhqqtlddLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEqekklrmDLERAKRKLEGDLKLAQES 1067
Cdd:TIGR02168 245 QEELKEAEEELEELTAE-------LQELEEKLEELRLEVSELEEEIEELQKELY-------ALANEISRLEQQKQILRER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1068 IMDLENDKQQSEEKLKkkdfetsQLLSKIEDEQSLGAQLQKKIKELQArieeleeeieaeraarakvekqradlsrELEE 1147
Cdd:TIGR02168 311 LANLERQLEELEAQLE-------ELESKLDELAEELAELEEKLEELKE----------------------------ELES 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1148 ISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEESTLQhEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEYK 1227
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ-IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1228 MEidDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDENLRQINDLSAQRARLQTENGEFGRQLEEKEAL---VSQLT 1304
Cdd:TIGR02168 435 LK--ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFsegVKALL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1305 RGKQAFTQQIEELKRQIEEEVKAKNALAHAVQSARHDcdLLREQFEEEQEAKAELqrgmskANSEVAQWrTKYETDAIqr 1384
Cdd:TIGR02168 513 KNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQA--VVVENLNAAKKAIAFL------KQNELGRV-TFLPLDSI-- 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1385 teeleeSKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLM------IDVERANALAANLDKKQRNF------- 1451
Cdd:TIGR02168 582 ------KGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLggvlvvDDLDNALELAKKLRPGYRIVtldgdlv 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1452 ---------------------------DKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLETLKREN 1504
Cdd:TIGR02168 656 rpggvitggsaktnssilerrreieelEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDL 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1505 KNLQQEISDLTEQLGETGKSIHELEKSKKAVETEKAEIQTALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEE 1584
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1585 IEQIKRNSQRItDSMQSTLDSEVRSRNDALRIKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAVR 1664
Cdd:TIGR02168 816 NEEAANLRERL-ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1665 GQEDMKEQVAMVERRNTLMQSEIEELRAALEQTERGRKVAEQELvdaservgllhSQNTSLLNTKKKLEADLV-QIQSEV 1743
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI-----------DNLQERLSEEYSLTLEEAeALENKI 963
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 288856329 1744 EDTVQEARNAEDKAKKAITD------AAMmaEELKKEQDTSAHLERMKKNLEVTVKDLQ 1796
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKIKElgpvnlAAI--EEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
910-1750 |
1.54e-31 |
|
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: 135.57 E-value: 1.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 910 LIKSKIQLEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAQDE 989
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 990 SIGKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIM 1069
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1070 DLENDKQQSEEKLkkkdfetSQLLSKIEDEQSLGAQLQKKIKELQARieeleeeieaeraaraKVEKQRADLSRELEEIS 1149
Cdd:TIGR02168 390 QLELQIASLNNEI-------ERLEARLERLEDRRERLQQEIEELLKK----------------LEEAELKELQAELEELE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1150 ERLEEAGGATAAQIEMNKKREAEFQKLRRDLEESTLQHEATAAALrkkqaDSVAELGEQIDNLQRVKQKLEKEKSEYKME 1229
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL-----DSLERLQENLEGFSEGVKALLKNQSGLSGI 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1230 IDDLSSNMEAVAKAKANLEKmcrTLEDQLSEIKSKNDENLRQINDLSAQ----RARLQTENGEFGRQLEEKEALVSQLTR 1305
Cdd:TIGR02168 522 LGVLSELISVDEGYEAAIEA---ALGGRLQAVVVENLNAAKKAIAFLKQnelgRVTFLPLDSIKGTEIQGNDREILKNIE 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1306 GKQAFTQQIEELKRQIEEEVKA-----------KNALAHAVQSARH------DCDLLReqfeeeqeAKAELQRGMSKANS 1368
Cdd:TIGR02168 599 GFLGVAKDLVKFDPKLRKALSYllggvlvvddlDNALELAKKLRPGyrivtlDGDLVR--------PGGVITGGSAKTNS 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1369 EVAQWRTKYEtDAIQRTEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANALAANLDKKQ 1448
Cdd:TIGR02168 671 SILERRREIE-ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1449 RNFDKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHEL 1528
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1529 EKSKKAVETEKAEIQTALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEEIEQIKrnsqritdSMQSTLDSEVR 1608
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA--------LLRSELEELSE 901
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1609 SRNDALRIKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQL-KDAQLHLDDAVRGQEDMKEQVAMVERRNTLMQSEI 1687
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 288856329 1688 EEL-RAALEqtergrkvAEQELVDASERVGLLHSQNTSLLNTKKKLEADLVQIQSEVEDTVQEA 1750
Cdd:TIGR02168 982 KELgPVNLA--------AIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDT 1037
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1134-1911 |
4.47e-28 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 124.02 E-value: 4.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1134 VEKQRAdlSRELEEISERLEEAggataaQIEMNKKREaEFQKLRRDLEEStlqhEATAAALRKKQADSVAELGEQIDNLQ 1213
Cdd:TIGR02169 170 RKKEKA--LEELEEVEENIERL------DLIIDEKRQ-QLERLRREREKA----ERYQALLKEKREYEGYELLKEKEALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1214 RVKQKLEKEKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSknDENLR---QINDLSAQRARLQTENGEFG 1290
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE--EEQLRvkeKIGELEAEIASLERSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1291 RQLEEKEALVSQLTRGKQAFTQQIEELKRQIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRgmskansEV 1370
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD-------EL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1371 AQWRTKYEtDAIQRTEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERAnalaanlDKKQRN 1450
Cdd:TIGR02169 388 KDYREKLE-KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ-------EWKLEQ 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1451 FDKVLAEWKQKYEEGQAELEGAQKEARSLSTELfkmknsyeetlDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEK 1530
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEYDRVEKELSKLQREL-----------AEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVA 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1531 SKKAVeteKAEIQTALEEAEG------TLEHE-----------ESKILRVQ-LELNQVKSE--------------IDRKL 1578
Cdd:TIGR02169 529 QLGSV---GERYATAIEVAAGnrlnnvVVEDDavakeaiellkRRKAGRATfLPLNKMRDErrdlsilsedgvigFAVDL 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1579 AEKDEEIEQIKRNSQRITDSMQS--------------TLDSEV-----------RSRNDALRIKKKMEGDLNEMEIQLSH 1633
Cdd:TIGR02169 606 VEFDPKYEPAFKYVFGDTLVVEDieaarrlmgkyrmvTLEGELfeksgamtggsRAPRGGILFSRSEPAELQRLRERLEG 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1634 ANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAMVERRNTLMQSEIEELRAALEQTERGRKVAEQELVDASE 1713
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1714 RVGLLHSQNTSLLNTKKKLEADLVQiqSEVEDTVQEARNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVK 1793
Cdd:TIGR02169 766 RIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1794 DLQHRL----DEAENLAMKGGKK--QLQKLESRVRELESEVEAEQRRGADAVKGVRKYERRVKELTYQTEEDKKNVNRLQ 1867
Cdd:TIGR02169 844 DLKEQIksieKEIENLNGKKEELeeELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 288856329 1868 DLVDKLQLKVKAYKRQSEEAEEQANSHLSkLRKVQHELEEAEER 1911
Cdd:TIGR02169 924 AKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEE 966
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
845-1595 |
3.87e-26 |
|
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: 117.85 E-value: 3.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 845 AETEKELATMKEDFVKCKEDLAKAEAKKKELEEKMVALLQEKNDLQLAVASESENLSDAEERCEGLIKSKIQLEAKLKET 924
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 925 TERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAQDESIgKLTKEKKALQEA 1004
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV-AQLELQIASLNN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1005 HQQTLddlqaeEDKVNTLTKSKTKLEQQVDDLEGSLEqekklrmdlERAKRKLEGDLKLAQESIMDLENDKQQSEEKLKK 1084
Cdd:TIGR02168 401 EIERL------EARLERLEDRRERLQQEIEELLKKLE---------EAELKELQAELEELEEELEELQEELERLEEALEE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1085 KDFETSQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISER------LEEAGGA 1158
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDegyeaaIEAALGG 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1159 TAAQIEMNKKREA--EFQKLRRDLEESTLQHEATAAALRKKQADSvAELGEQIDNLQRVKQKLEKEKSEYKMEIDDLSSN 1236
Cdd:TIGR02168 546 RLQAVVVENLNAAkkAIAFLKQNELGRVTFLPLDSIKGTEIQGND-REILKNIEGFLGVAKDLVKFDPKLRKALSYLLGG 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1237 MEAVAKAKANLEKmcRTLEDQLSEIKSKNDENLRQinDLSAQRARLQTENGEFGRQLEEKEAlvsqltrgkqafTQQIEE 1316
Cdd:TIGR02168 625 VLVVDDLDNALEL--AKKLRPGYRIVTLDGDLVRP--GGVITGGSAKTNSSILERRREIEEL------------EEKIEE 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1317 LKRQIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTeELEESKKKLA 1396
Cdd:TIGR02168 689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT-ELEAEIEELE 767
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1397 QRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDL--MIDVERA-----NALAANLDKKQRNFDKVLAEWKQKYEEGQAEL 1469
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALreALDELRAeltllNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1470 EGAQKEARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAVETEKAEIQTALEEA 1549
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 288856329 1550 EGTLEHEESKILRVQLELN-----------QVKSEIDRKLAEKDEEIEQIKRNSQRI 1595
Cdd:TIGR02168 928 ELRLEGLEVRIDNLQERLSeeysltleeaeALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
919-1805 |
3.04e-24 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 111.70 E-value: 3.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 919 AKLKETTERLEDEEEINAELTAKKRKLEDECSELKKdIDDLELTLAKVE-----KEKHATENKVKNLTEEMAAQDESIGK 993
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 994 LTKEKKALQEAHQQTLDDLQAEEDKVNTLTKSKT-KLEQQVDDLEGSLEQekklrmdlerakrkLEGDLKLAQESIMDLE 1072
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIGELEAEIAS--------------LERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1073 NDKQQSEEKLKKKDFETSQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERL 1152
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1153 EEAGGATAAQIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQadsvAELGEQIDNLQRVKQKLEKEKSEYKmeidd 1232
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA----LEIKKQEWKLEQLAADLSKYEQELY----- 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1233 lssnmeavakakaNLEKMCRTLEDQLSEIKskndenlRQINDLSAQRARLQTENGEFGRQLEEKEA-------LVSQLTR 1305
Cdd:TIGR02169 473 -------------DLKEEYDRVEKELSKLQ-------RELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLGS 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1306 GKQAFTQQIEELKRQ------IEEEVKAKNA--LAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRTKY 1377
Cdd:TIGR02169 533 VGERYATAIEVAAGNrlnnvvVEDDAVAKEAieLLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKY 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1378 ETD---AIQRT---EELEESKK--------KLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANALAAN 1443
Cdd:TIGR02169 613 EPAfkyVFGDTlvvEDIEAARRlmgkyrmvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSS 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1444 LDKKQRNFDKVLAEWKQKYEEGQAELEGAQKEArslstelfkmknsyEETLDQLETLKRENKNLQQEISDLTEQLGETGK 1523
Cdd:TIGR02169 693 LQSELRRIENRLDELSQELSDASRKIGEIEKEI--------------EQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1524 SIHELEKSKKAVETEKAEIQTALEEAEGTLEHEESKILRVQL-ELNQVKSEIDRKLAEKDEEIEQIKRNSQRITDSMQst 1602
Cdd:TIGR02169 759 ELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELsKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ-- 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1603 ldsEVRSRNDALRIKKKMEGD-LNEMEIQLSHANRQAAEAQKQLRNVQAQLKDaqlhlddavrgqedmkeqvamverrnt 1681
Cdd:TIGR02169 837 ---ELQEQRIDLKEQIKSIEKeIENLNGKKEELEEELEELEAALRDLESRLGD--------------------------- 886
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1682 lMQSEIEELRAALEQTERGRKVAEQELVDASERVGLLHSQNTSLLNTKKKLEADLVQIQSEVE-----DTVQEARNAEDK 1756
Cdd:TIGR02169 887 -LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEeelslEDVQAELQRVEE 965
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 288856329 1757 AKKAITDAAMMA-EELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENL 1805
Cdd:TIGR02169 966 EIRALEPVNMLAiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1141-1733 |
8.38e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 110.03 E-value: 8.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1141 LSRELEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQADsVAELGEQIDNLQRVKQKLE 1220
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE-EYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1221 KEKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDENLRQINDLSAQRARLQTENGEFGRQLEEKEALV 1300
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1301 SQLTRGKQAFTQQIEELKRQIEEEVKAKNALAHAVQSarhdcdlLREQFEEEQEAKAELQRGMSKANSEVAQWRTKYETD 1380
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEE-------LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1381 AIQRTEELEESKKKLAQRLQEAEEQIEAvnskcASLEKTKQRLQGEVEDLMIDVERANALAANLDKKQRnfDKVLAEWKQ 1460
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEA-----AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA--VAVLIGVEA 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1461 KYEEGQAELEGAQKEARSLST--------ELFKMKNSYEETLDQLETLKREN--KNLQQEISDLTEQLGETGKSIHELEK 1530
Cdd:COG1196 535 AYEAALEAALAAALQNIVVEDdevaaaaiEYLKAAKAGRATFLPLDKIRARAalAAALARGAIGAAVDLVASDLREADAR 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1531 SKKAVETEKAEIQTALEEAEG-----TLEHEESKILRVQLELNQVKSEIDRKLAEKDEEIEQIKRNSQRITDSMQSTLDS 1605
Cdd:COG1196 615 YYVLGDTLLGRTLVAARLEAAlrravTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1606 EVRSRNDALRIKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAMVERRntlmqs 1685
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE------ 768
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 288856329 1686 eIEELRAALEQTErgrKV---AEQELVDASERVGLLHSQNTSLLNTKKKLE 1733
Cdd:COG1196 769 -LERLEREIEALG---PVnllAIEEYEELEERYDFLSEQREDLEEARETLE 815
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
914-1514 |
1.76e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.87 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 914 KIQLEAKLKETTERLEDEEEINAELTAKKRKLEdecsELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAQDESIGK 993
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELE----ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 994 LTKEKKALQEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLEN 1073
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1074 DKQQSEEKLKKKDFETSQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLE 1153
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1154 EAGGATAAQIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEYKMEIDDL 1233
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1234 SSNMEAVAKAKAN---LEKMCRTLEDQLSEIkskndENLRQINDLSAQRARLQTENGEFGRQLEEKEALVSQLTRGKQAF 1310
Cdd:COG1196 533 EAAYEAALEAALAaalQNIVVEDDEVAAAAI-----EYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1311 TQQIEELKRQIEEEVKAKNALAHAVQSARHdcdlLREQFEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEELEE 1390
Cdd:COG1196 608 LREADARYYVLGDTLLGRTLVAARLEAALR----RAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1391 SKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANALAANLDKKQRNFDKVLAEWKQKYEEGQAELE 1470
Cdd:COG1196 684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 288856329 1471 GAQKEARSLSTELFKMKN-------SYEETLDQLETLKRENKNLQQEISDL 1514
Cdd:COG1196 764 ELERELERLEREIEALGPvnllaieEYEELEERYDFLSEQREDLEEARETL 814
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
841-1454 |
2.27e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.49 E-value: 2.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 841 LLKSAETEKELATMKEDFVKCKEDLAKAEAKKKELEEKMVALLQEKNDLQLAVASESENLSDAEERCEGLIKSKIQLEAK 920
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 921 LKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAQDESIGKLTKEKKA 1000
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1001 LQEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSEE 1080
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1081 KLKKKDFETSQLLSKIEDEQSLGAQLQKKIKELQARIE--ELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGA 1158
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEgvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQN 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1159 TAAQIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQIDnlqRVKQKLEKEKSEYKMEIDDLSSNME 1238
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD---LVASDLREADARYYVLGDTLLGRTL 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1239 AVAKAKANLEKMCRTLEDQLSEIKSKNDENLRQINDLSAQRARLQtengefgrQLEEKEALVSQLTRGKQAFTQQIEELK 1318
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA--------ALLEAEAELEELAERLAEEELELEEAL 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1319 RQIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAqwrtKYETDAIQRTEELEESKKKLAQR 1398
Cdd:COG1196 700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA----LEELPEPPDLEELERELERLERE 775
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1399 LQ--------------EAEEQIEAVNSKCASLEKTKQRLQGEVEDlmIDVERANALAANLDKKQRNFDKV 1454
Cdd:COG1196 776 IEalgpvnllaieeyeELEERYDFLSEQREDLEEARETLEEAIEE--IDRETRERFLETFDAVNENFQEL 843
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1218-1925 |
2.43e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.49 E-value: 2.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1218 KLEKEKSEYKMEiddlssnmeavaKAKANLEKmcrtLEDQLSEIKskndenlRQINDLSAQRAR------LQTEngefgr 1291
Cdd:COG1196 171 KERKEEAERKLE------------ATEENLER----LEDILGELE-------RQLEPLERQAEKaeryreLKEE------ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1292 qLEEKEALVSQLTRgkQAFTQQIEELKRQIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVA 1371
Cdd:COG1196 222 -LKELEAELLLLKL--RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1372 QwrtkyetdAIQRTEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANALAANLDKKQRNF 1451
Cdd:COG1196 299 R--------LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1452 DKVLAEWKQKYEEGQAELEGAQKEARSLSTELfkmknsyEETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEKS 1531
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQL-------EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1532 KKAVETEKAEIQTALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEEIEQIKRNSQRITDSMQSTLDSEVRSRN 1611
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1612 DALRIkkkmegdlnemEIQLSHANRQAAEAQKQLRNVQAQLKDAQlhldDAVRGQEDMKEQVAmvERRNTLMQSEIEELR 1691
Cdd:COG1196 524 GAVAV-----------LIGVEAAYEAALEAALAAALQNIVVEDDE----VAAAAIEYLKAAKA--GRATFLPLDKIRARA 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1692 AALEQTERGRKVAEQELVDAservgllhsqntsllntkkkLEADLVQIQSEVEDTVQEARNAEDKAKKAITDAAMMAEEL 1771
Cdd:COG1196 587 ALAAALARGAIGAAVDLVAS--------------------DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRL 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1772 KKEQDTSAHLERMKKNLEVTVKDLQHRLDEAEnlamkggkKQLQKLESRVRELESEVEAEQRRGADAvkgvrkyERRVKE 1851
Cdd:COG1196 647 REVTLEGEGGSAGGSLTGGSRRELLAALLEAE--------AELEELAERLAEEELELEEALLAEEEE-------ERELAE 711
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 288856329 1852 LTYQTEEDKKNVNRLQDLVDKLQLKVKAYKRQSEEAEEQAnshlsklrkvQHELEEAEERADIAESQVNKLRAK 1925
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE----------ALEELPEPPDLEELERELERLERE 775
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
881-1592 |
3.17e-23 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 108.23 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 881 ALLQEKNDLQLAVASESENLSDAEERCEGLIKSKIQLEAKLKETTERLED--EEEINA------ELTAKKRKLEDECSEL 952
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgEEEQLRvkekigELEAEIASLERSIAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 953 KKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAQDESIGKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQ 1032
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1033 VDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSEEKLKKKDFETSQLLSKIEDEQSLGAQLQKKIKE 1112
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1113 LQARIEELEEEIEAERAARAKVEKQR----------------------------ADLSRELEEISERLEEAGG------- 1157
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAEAQAraseervrggraveevlkasiqgvhgtvAQLGSVGERYATAIEVAAGnrlnnvv 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1158 ----ATAAQ-IEMNKKREA------EFQKLRRDLEESTLQHEATAAALrkkqADSVAELGEQIDNLQR-------VKQKL 1219
Cdd:TIGR02169 554 veddAVAKEaIELLKRRKAgratflPLNKMRDERRDLSILSEDGVIGF----AVDLVEFDPKYEPAFKyvfgdtlVVEDI 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1220 EKEKS---EYKM-----EIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDENLRQINDLSAQRARLQTENGEF-- 1289
Cdd:TIGR02169 630 EAARRlmgKYRMvtlegELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELsq 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1290 -----GRQLEEKEALVSQLTRGKQAFTQQIEELKRQIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRgmS 1364
Cdd:TIGR02169 710 elsdaSRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA--R 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1365 KANSEVAQWRTKYetdaiqrtEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANALAANL 1444
Cdd:TIGR02169 788 LSHSRIPEIQAEL--------SKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1445 DKKQRNFDKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGETGKS 1524
Cdd:TIGR02169 860 NGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDP 939
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1525 IHELEKSKKAV---ETEKAEIQtALEEAEGTL---------EHEESKILRVQLELNQVKSEIDRK-LAEKDEEIEQIKRN 1591
Cdd:TIGR02169 940 KGEDEEIPEEElslEDVQAELQ-RVEEEIRALepvnmlaiqEYEEVLKRLDELKEKRAKLEEERKaILERIEEYEKKKRE 1018
|
.
gi 288856329 1592 S 1592
Cdd:TIGR02169 1019 V 1019
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
911-1590 |
3.46e-22 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 104.76 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 911 IKSKIQLEAKLKETTERLEDEEEINAELTAKKRKLEDecseLKKDIDDLELTLAKVEKEKHATENKVKNLTE-EMAAQDE 989
Cdd:TIGR02169 219 EKREYEGYELLKEKEALERQKEAIERQLASLEEELEK----LTEEISELEKRLEEIEQLLEELNKKIKDLGEeEQLRVKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 990 SIGKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIM 1069
Cdd:TIGR02169 295 KIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1070 DLENDKQQSEEKLKKKDFETSQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEIS 1149
Cdd:TIGR02169 375 EVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1150 ERLEEAGGATAAQIEMNKKREAEFQKLRRDLEESTLQH---EATAAALRKKQADSVA---ELGEQIDNLQRVKQKLEKEK 1223
Cdd:TIGR02169 455 WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELaeaEAQARASEERVRGGRAveeVLKASIQGVHGTVAQLGSVG 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1224 SEYKMEIDDLSSNM--------EAVAKAKANL---EKMCRTLEDQLSEIKSKNdenlrqiNDLSAQRarlqtENGEFGRQ 1292
Cdd:TIGR02169 535 ERYATAIEVAAGNRlnnvvvedDAVAKEAIELlkrRKAGRATFLPLNKMRDER-------RDLSILS-----EDGVIGFA 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1293 L-----EEKEALVSQLTRGKQAFTQQIEELKRQ--------IEEEVKAK--------NALAHAVQSARHDCDLLREQFEE 1351
Cdd:TIGR02169 603 VdlvefDPKYEPAFKYVFGDTLVVEDIEAARRLmgkyrmvtLEGELFEKsgamtggsRAPRGGILFSRSEPAELQRLRER 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1352 EQEAKAELQRGMSKAN---SEVAQWRTKYEtDAIQRTEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVE 1428
Cdd:TIGR02169 683 LEGLKRELSSLQSELRrieNRLDELSQELS-DASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1429 DLMIDVERANALAANLDKKQRNFDKVLAEwkQKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLETLKRENKNLQ 1508
Cdd:TIGR02169 762 ELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1509 QEISDLTEQLGETGKSIHELEKSKKAVETEKAEIQTALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEEIEQI 1588
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRL 919
|
..
gi 288856329 1589 KR 1590
Cdd:TIGR02169 920 SE 921
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1195-1925 |
9.96e-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: 103.22 E-value: 9.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1195 RKKQADSVAELGEQIDNLQRVKQKLEK-EKSEYKME--IDDLSSNMEAVAKAKANLEKMcRTLEDQLSEIKSKndENLRQ 1271
Cdd:TIGR02169 155 RRKIIDEIAGVAEFDRKKEKALEELEEvEENIERLDliIDEKRQQLERLRREREKAERY-QALLKEKREYEGY--ELLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1272 INDLSAQRARLQtengefgRQLEEKEALVSQLTRGKQAFTQQIEELKRQIEEEVKAKNALAhavqsarhdcdllreqfEE 1351
Cdd:TIGR02169 232 KEALERQKEAIE-------RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG-----------------EE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1352 EQeakAELQRGMSKANSEVAQWRtkyetDAIqrtEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLM 1431
Cdd:TIGR02169 288 EQ---LRVKEKIGELEAEIASLE-----RSI---AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1432 IDVERANALAANLDKKQRNFDKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMknsyeetLDQLETLKRENKNLQQEI 1511
Cdd:TIGR02169 357 EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRL-------QEELQRLSEELADLNAAI 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1512 SDLTEQLGETGKSIHELEKSKKAVETEKAEIQTALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKD---EEIEQI 1588
Cdd:TIGR02169 430 AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARaseERVRGG 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1589 KRNSQRITDSMQSTLDS-----EVRSR------------------------NDALRIKKKMEGD------LNEMEIQLSH 1633
Cdd:TIGR02169 510 RAVEEVLKASIQGVHGTvaqlgSVGERyataievaagnrlnnvvveddavaKEAIELLKRRKAGratflpLNKMRDERRD 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1634 ANRQA-----------AEAQKQLRNVQAQLKDAQLHLDDAVRGQEDM--------------------------------- 1669
Cdd:TIGR02169 590 LSILSedgvigfavdlVEFDPKYEPAFKYVFGDTLVVEDIEAARRLMgkyrmvtlegelfeksgamtggsraprggilfs 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1670 ---KEQVAMVERRNTLMQSEIEELRAALEQTERGRKVAEQELVDASERVGLLHSQNTSLLNTKKKLEADLVQIQSEVEDT 1746
Cdd:TIGR02169 670 rsePAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1747 VQEARNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMkknlevtvkDLQHRLDEAENLAMKgGKKQLQKLESRVRELES 1826
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR---------LSHSRIPEIQAELSK-LEEEVSRIEARLREIEQ 819
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1827 EVEAEQRRGA-------DAVKGVRKYERRVKELTYQTEEDKKNVNRLQDLVDKLQLKVKAYKRQSEEAEEQANSHLSKLR 1899
Cdd:TIGR02169 820 KLNRLTLEKEylekeiqELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
810 820
....*....|....*....|....*.
gi 288856329 1900 KVQHELEEAEERADIAESQVNKLRAK 1925
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1003-1796 |
6.30e-21 |
|
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: 100.58 E-value: 6.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1003 EAHQQTLDDLQAEEDKVNTL-TKSKTKLEQQVDDLEGSLEQ---EKKLRMDLERAKRKLEGDLK-LAQESIMDLENDKQQ 1077
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNELhEKQKFYLRQSVIDLQTKLQEmqmERDAMADIRRRESQSQEDLRnQLQNTVHELEAAKCL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1078 SEEKLKKKDFETSQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAK-----VEKQRADLSRELEEISERL 1152
Cdd:pfam15921 161 KEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRslgsaISKILRELDTEISYLKGRI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1153 EEAGGATAA-QIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEYKMEID 1231
Cdd:pfam15921 241 FPVEDQLEAlKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLS 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1232 DLSSNmeaVAKAKANLEKMCRTLEDQLSEIKSKNDENLRQINDLSAQRARLQTENGEFGRQLEEkeaLVSQLTRGKQAFT 1311
Cdd:pfam15921 321 DLEST---VSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQK---LLADLHKREKELS 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1312 QQIEELKRQIEEEVKAKNALAHavqsarhdcdlLREQFEEEQeakAELQR--GMSKANSEVAQWRTKYETDAIQRTEELE 1389
Cdd:pfam15921 395 LEKEQNKRLWDRDTGNSITIDH-----------LRRELDDRN---MEVQRleALLKAMKSECQGQMERQMAAIQGKNESL 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1390 ESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDV---ERA-NALAANLDKKQRNFDKVLAEWKQKYEEG 1465
Cdd:pfam15921 461 EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLqekERAiEATNAEITKLRSRVDLKLQELQHLKNEG 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1466 QaELEGAQKEARSLSTELFKMKNSYEEtldqletlkrenknLQQEISDLTEQLGETGKSIHELEKSKKAVETEKAEIQTA 1545
Cdd:pfam15921 541 D-HLRNVQTECEALKLQMAEKDKVIEI--------------LRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLE 605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1546 LEEAEGTLEHEESKILRVQ-----LELNQVK-----SEIDRKLAEKDEEIEQIKRNSQRITDSMQS-TLDSEVRSRNdal 1614
Cdd:pfam15921 606 LQEFKILKDKKDAKIRELEarvsdLELEKVKlvnagSERLRAVKDIKQERDQLLNEVKTSRNELNSlSEDYEVLKRN--- 682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1615 rIKKKMEgdlnEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAMVERRNTLMQSEIEELRAAL 1694
Cdd:pfam15921 683 -FRNKSE----EMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAM 757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1695 EQTERGRKVAEQELVDASERVgllhsqnTSLLNTKKKLEADLVQIQSEVEDTVQEARNAEDKAKKAITDAAMMAEELKKE 1774
Cdd:pfam15921 758 TNANKEKHFLKEEKNKLSQEL-------STVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQ 830
|
810 820
....*....|....*....|..
gi 288856329 1775 QDTSAhleRMKKNLEVTVKDLQ 1796
Cdd:pfam15921 831 EQESV---RLKLQHTLDVKELQ 849
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
224-713 |
1.26e-20 |
|
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: 99.43 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 224 IIAANPLLEAYGNAKTVRNDNSSRFGKF--IRIHFGTSG---KLASADIETYLLEKSRVTFQLPDERG------YHIFYQ 292
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERGRESGdqnelnFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 293 MMT--NHKPEL----IEMTLITTNPYDFPMCSQGQITVASIDDKEELVATDT--------AIDILGFNNEEKMGIYKFTG 358
Cdd:cd14894 329 MVAgvNAFPFMrllaKELHLDGIDCSALTYLGRSDHKLAGFVSKEDTWKKDVerwqqvidGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 359 AVLHHGNMKFKQKQREEQAEPDGT---EEADKIGYLLGLNSADMLKALCYPR---VKVGNEFVTKGQTVPQVYNSVSALS 432
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsvsLQSTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 433 KSIYERMFLWMVVRINQM-----LDTKQQRN------------FFIGVLDIAGFEIFDFNSMEQLCINFTNEKLqqfFNH 495
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEAtkmsaLSTDGNKHqmdsnasapeavSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL---YAR 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 496 HMFVLEQEEYKKEGIVWEfiDFGMDLaacIELIEKPLGIFSILEEECMFPKATDTSF-----KNKLYDQHLGKCNAFQKP 570
Cdd:cd14894 566 EEQVIAVAYSSRPHLTAR--DSEKDV---LFIYEHPLGVFASLEELTILHQSENMNAqqeekRNKLFVRNIYDRNSSRLP 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 571 KPAK--GKAEAH---------FSLVHYAGTVDYNISGWLDKNKDPLNES-VVQLYQKSSVKLLATL-------YPPVVEE 631
Cdd:cd14894 641 EPPRvlSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANlLVGLKTSNSSHFCRMLnessqlgWSPNTNR 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 632 TggGKKGGKKKGGSMQTVSSQFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGF 711
Cdd:cd14894 721 S--MLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICRNSS 798
|
..
gi 288856329 712 PS 713
Cdd:cd14894 799 SS 800
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
893-1623 |
1.81e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 99.45 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 893 VASESENLSDAEERCEGLIKSKIQLEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKdiddleltlaKVEKEKHA 972
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKK----------KAEEAKKA 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 973 TENKVKnlTEEMAAQDESIGKLTKEKKALQEAhqqtlddlqaeedkvntltkSKTKLEQQVDDLEGSLEQEKKLRMDLER 1052
Cdd:PTZ00121 1318 DEAKKK--AEEAKKKADAAKKKAEEAKKAAEA--------------------AKAEAEAAADEAEAAEEKAEAAEKKKEE 1375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1053 AKRKLEGDLKLAQESIMDLENDKQQSEEKLKKKDFETSQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAeraara 1132
Cdd:PTZ00121 1376 AKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA------ 1449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1133 kveKQRADLSRELEEISERLEEAGGATAAQIEMNKKREAEfqKLRRDLEESTLQ-HEATAAALRKKQADSVAELGEQidn 1211
Cdd:PTZ00121 1450 ---KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD--EAKKKAEEAKKKaDEAKKAAEAKKKADEAKKAEEA--- 1521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1212 lqrvKQKLEKEKSEYKMEIDDLSSnmeavAKAKANLEKMCRTLEDQLSEIKSKNDENLRQindlsAQRARLQTENGEFGR 1291
Cdd:PTZ00121 1522 ----KKADEAKKAEEAKKADEAKK-----AEEKKKADELKKAEELKKAEEKKKAEEAKKA-----EEDKNMALRKAEEAK 1587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1292 QLEEKEaLVSQLTRGKQAFTQQIEELKRQIEEEVKAKNalAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVA 1371
Cdd:PTZ00121 1588 KAEEAR-IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE--LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAA 1664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1372 QWRTKYETDAiQRTEEL----EESKKKLAQRLQEAEE--QIEAVNSKCASLEKTKQRLQGEVEDLMIDVERAnalaanld 1445
Cdd:PTZ00121 1665 EEAKKAEEDK-KKAEEAkkaeEDEKKAAEALKKEAEEakKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA-------- 1735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1446 KKQRNFDKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEEtldqlETLKRENKNLQQEISDLTEQLGETGKSI 1525
Cdd:PTZ00121 1736 KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE-----EELDEEDEKRRMEVDKKIKDIFDNFANI 1810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1526 HELEKSKKAV-----ETEKAEIQTALEEAEGTLEhEESKILRVQLELNQVKSEIDRKLA----EKD------EEIEQIKR 1590
Cdd:PTZ00121 1811 IEGGKEGNLVindskEMEDSAIKEVADSKNMQLE-EADAFEKHKFNKNNENGEDGNKEAdfnkEKDlkeddeEEIEEADE 1889
|
730 740 750
....*....|....*....|....*....|...
gi 288856329 1591 NSQRITDSMQSTLDSEVRSRNDALRIKKKMEGD 1623
Cdd:PTZ00121 1890 IEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKD 1922
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1255-1936 |
4.16e-19 |
|
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: 94.86 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1255 EDQLSEIKSKNDENLRQINDLSAQRARLQTENGEFGRQLE-------EKEALVSQLTRGKQAFTQQIEELKRQIEEEVKA 1327
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQaetelcaEAEEMRARLAARKQELEEILHELESRLEEEEER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1328 KNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEeLEESKKKLAQRLQEAEEQIE 1407
Cdd:pfam01576 91 SQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSK-LSKERKLLEERISEFTSNLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1408 AVNSKCASLEKTKQRLQGEVEDLMIDVERANALAANLDKKQRNFDKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMK 1487
Cdd:pfam01576 170 EEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAAL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1488 NSYEETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAVETEKAEIQTALEEAEGTLEHEESKILRVQLEL 1567
Cdd:pfam01576 250 ARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1568 NQVKSEIDRKLAEKDEEIEQIKRNSQRITDSMQSTLDSEVRSRNDALRIKKKMEGDLNEMEIQLSHANRQAAEAQKQLRN 1647
Cdd:pfam01576 330 TELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKK 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1648 VQAQLKDAQLHLDDAVRGQEDMKEQVAMverrntlMQSEIEELRAALEQTErgrkvaeqelvdaservgllhSQNTslln 1727
Cdd:pfam01576 410 LEGQLQELQARLSESERQRAELAEKLSK-------LQSELESVSSLLNEAE---------------------GKNI---- 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1728 tkkKLEADLVQIQSEVEDTvQEARNAEDKAKKAIT--------DAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRL 1799
Cdd:pfam01576 458 ---KLSKDVSSLESQLQDT-QELLQEETRQKLNLStrlrqledERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKL 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1800 DE-AENL-AMKGGKKQLQK-LESRVRELESEVEAEQRrgadAVKGVRKYERRVKELTYQTEEDKKNVNRL---QDLVDKL 1873
Cdd:pfam01576 534 EEdAGTLeALEEGKKRLQReLEALTQQLEEKAAAYDK----LEKTKNRLQQELDDLLVDLDHQRQLVSNLekkQKKFDQM 609
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 288856329 1874 QLKVKA----YKRQSEEAEEQANSHLSKLRKVQHELEEAEERADIAESQVNKLRAKSRDSGKGKDAA 1936
Cdd:pfam01576 610 LAEEKAisarYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDV 676
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1416-1925 |
4.69e-19 |
|
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: 94.41 E-value: 4.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1416 LEKTKQRLQGEVEDLMIDVERANALAanlDKKQRNFDKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLD 1495
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNELH---EKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1496 QLETLKRENKNLQQEISDLTEQLgetgksiHELEKSKKAVETEKAEIQTALEEAEGTLEHEESKIlrVQLELNQVKSEID 1575
Cdd:pfam15921 153 ELEAAKCLKEDMLEDSNTQIEQL-------RKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSM--STMHFRSLGSAIS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1576 RKLAEKDEEIEQIKRNSQRITDSMQsTLDSEVRSRNDAL--RIKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLK 1653
Cdd:pfam15921 224 KILRELDTEISYLKGRIFPVEDQLE-ALKSESQNKIELLlqQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1654 DAQlhlddavrgqEDMKEQVAMVERRNTLMQSEIEELRAALEQTERgrkVAEQELVDASERVGLLHSQntsllntkkkle 1733
Cdd:pfam15921 303 IIQ----------EQARNQNSMYMRQLSDLESTVSQLRSELREAKR---MYEDKIEELEKQLVLANSE------------ 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1734 adLVQIQSEVEDTVQEARNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAenlamkggKKQ 1813
Cdd:pfam15921 358 --LTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDR--------NME 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1814 LQKLESRVRELESEVEAEQRRGADAVKGVRKYERRVKELTYQTEEDKKnvnRLQDLVDKLqlkvkAYKRQSEEAEEQANS 1893
Cdd:pfam15921 428 VQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKE---MLRKVVEEL-----TAKKMTLESSERTVS 499
|
490 500 510
....*....|....*....|....*....|..
gi 288856329 1894 HLSKlrkvqhELEEAEERADIAESQVNKLRAK 1925
Cdd:pfam15921 500 DLTA------SLQEKERAIEATNAEITKLRSR 525
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1169-1913 |
7.21e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 94.44 E-value: 7.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1169 REAEFQKLRRDLEESTLQHEATAAALRKKQADSVAElgEQIDNLQRVKQKLEKEKSEYKMEIDDLSSNMEAVAKAKANLE 1248
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAE--EARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRV 1154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1249 KMCRTLEDQLSEIKSKNDENLRQIndlSAQRARLQTENGEFGRQLEEkealVSQLTRGKQAFTQQIEELKRQIEEEVKAK 1328
Cdd:PTZ00121 1155 EIARKAEDARKAEEARKAEDAKKA---EAARKAEEVRKAEELRKAED----ARKAEAARKAEEERKAEEARKAEDAKKAE 1227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1329 NAlaHAVQSARHDcdllreqfeEEQEAKAELQRGmskaNSEVAQWRTKYETDAIQRTEELEESKKKLAQRLQEAEEQIEA 1408
Cdd:PTZ00121 1228 AV--KKAEEAKKD---------AEEAKKAEEERN----NEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA 1292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1409 VNSKCASLEKTKQRLQGEVEDlmidveraNALAANLDKKQRNFDKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMKN 1488
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEE--------AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1489 SYEEtlDQLETLKRENKnlqqeisdlTEQLGETGKSIHELEKSKKAVETEKAEIQTALEEAEGTLEHEESKILRVQLEln 1568
Cdd:PTZ00121 1365 KAEA--AEKKKEEAKKK---------ADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK-- 1431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1569 qvKSEIDRKLAEKDEEIEQIKRNSQRITDSMQSTLDSEVRSRNDALRIKKKMEGDLNEMEIQLSHANRQAAEAQKQlrnV 1648
Cdd:PTZ00121 1432 --KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA---A 1506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1649 QAQLKDAQLHLDDAVRGQEDMK---EQVAMVERRNTLMQSEIEELRAA--LEQTERGRKVaEQELVDASERVGLLHSQNT 1723
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKkaeEAKKADEAKKAEEKKKADELKKAeeLKKAEEKKKA-EEAKKAEEDKNMALRKAEE 1585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1724 SLLNTKKKLEADLVQIQSEVEDTVQEARNAEDKAKKAitdaammaEELKKEQDTSAHLERMKKNLEVTVKDLQH-RLDEA 1802
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA--------EELKKAEEEKKKVEQLKKKEAEEKKKAEElKKAEE 1657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1803 ENLAMKGGKKQLQKLESRVRELESEVEAEQRRGADAVKGVRKYERRVKELTYQTEEDKKNVNRLQDL-------VDKLQL 1875
Cdd:PTZ00121 1658 ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAeeenkikAEEAKK 1737
|
730 740 750
....*....|....*....|....*....|....*...
gi 288856329 1876 KVKAYKRQSEEAEEQANSHlsklRKVQHELEEAEERAD 1913
Cdd:PTZ00121 1738 EAEEDKKKAEEAKKDEEEK----KKIAHLKKEEEKKAE 1771
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1302-1907 |
2.51e-18 |
|
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: 92.10 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1302 QLTRGKQAFTQQIEELKRQIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVaqwrtkyeTDA 1381
Cdd:pfam15921 75 HIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDL--------RNQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1382 IQRT-EELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQrlqgEVEDLMIDVERANAlaanldkkqrnfdkvlaewKQ 1460
Cdd:pfam15921 147 LQNTvHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQ----EIRSILVDFEEASG-------------------KK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1461 KYEEGQAEL-------EGAQKEARSLSTELFKMKNSYEETLDQLETLKRENKN----LQQEISDLTEQL-GETGKSIHEL 1528
Cdd:pfam15921 204 IYEHDSMSTmhfrslgSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNkielLLQQHQDRIEQLiSEHEVEITGL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1529 EKSKKAVETEKAEIQTALEEAEGTLEHEESKILRVQLEL----NQVKSEI---DRKLAEKDEEIE--------------- 1586
Cdd:pfam15921 284 TEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLestvSQLRSELreaKRMYEDKIEELEkqlvlanselteart 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1587 ---QIKRNSQRITDSMQSTLdSEVRSRNDALRIKKKMEGDLNEME----IQLSHANRQAAEAQKQLRNVQAQLKDaqlhL 1659
Cdd:pfam15921 364 erdQFSQESGNLDDQLQKLL-ADLHKREKELSLEKEQNKRLWDRDtgnsITIDHLRRELDDRNMEVQRLEALLKA----M 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1660 DDAVRGQedMKEQVAMVERRNTLMQsEIEELRAALEQT-ERGRKVAEQ-----ELVDASERVglLHSQNTSLLNTKKKLE 1733
Cdd:pfam15921 439 KSECQGQ--MERQMAAIQGKNESLE-KVSSLTAQLESTkEMLRKVVEEltakkMTLESSERT--VSDLTASLQEKERAIE 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1734 A---DLVQIQSEVEDTVQEA---RNAEDKAKKAITDAA----MMAEELKKEQDTSAHLERM-----------------KK 1786
Cdd:pfam15921 514 AtnaEITKLRSRVDLKLQELqhlKNEGDHLRNVQTECEalklQMAEKDKVIEILRQQIENMtqlvgqhgrtagamqveKA 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1787 NLEVTVKDLQHRLDEAENLAMKGGKKqLQKLESRVRELESEVEAEQRRGADAVKGVRKYERRVKELTyqtEEDKKNVNRL 1866
Cdd:pfam15921 594 QLEKEINDRRLELQEFKILKDKKDAK-IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLL---NEVKTSRNEL 669
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 288856329 1867 QDLVDKLQLKVKAYKRQSEEAEEQANSHLSKLRKVQHELEE 1907
Cdd:pfam15921 670 NSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
957-1589 |
2.53e-18 |
|
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: 91.62 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 957 DDLELTLAKVEKEKHATENKVKNLTEEMAAQDESIGKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKS----------- 1025
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDlskinseiknd 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1026 ---KTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSEEKLKKKDFETSQLLSKIEDEQSL 1102
Cdd:TIGR04523 116 keqKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1103 GAQLQKKIKELQarieELEEEIEAERAARAKVEKQRADLSRELEEISERLEEaggataaqiemnkkREAEFQKLRRDLEE 1182
Cdd:TIGR04523 196 LLKLELLLSNLK----KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINE--------------KTTEISNTQTQLNQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1183 STLQHEATAAALRKKQadsvaelgEQIDNLQRVKQKLEKEKSEYKMEIDDLSSNMEA-----VAKAKANLEKMCRTLEDQ 1257
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQ--------KELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkeLKSELKNQEKKLEEIQNQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1258 LSEIKSKNDENLRQINDLSAQRARLQTENGEFGRQLEEKEALVSQLTRGKQAFTQQIEELKRQIeeevkakNALAHAVQS 1337
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI-------NDLESKIQN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1338 ARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRTKYEtDAIQRTEELEESKKKLAQRLQEAEEQIEAVNSKCASLE 1417
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK-DLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1418 KTKQRLQGEVEDLMIDVERANALAANLDKKQRNFDKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMKnsYEETLDQL 1497
Cdd:TIGR04523 482 QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDD--FELKKENL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1498 ETLKRENknlQQEISDLTEQLGETGKSIHELEKSKKAVETEKAEIQTALEEAE---GTLEHEESKILRVQLELNQVKSEI 1574
Cdd:TIGR04523 560 EKEIDEK---NKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEkkiSSLEKELEKAKKENEKLSSIIKNI 636
|
650
....*....|....*
gi 288856329 1575 DRKLAEKDEEIEQIK 1589
Cdd:TIGR04523 637 KSKKNKLKQEVKQIK 651
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
845-1516 |
3.56e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 91.66 E-value: 3.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 845 AETEKELATMKEDFVKCKEDLAKAEAKKKELEEKMVALLQEKNDLQLAVASESENLSDAEERCEGLIKSKIQLEAKLKET 924
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 925 TERLEDEEEINAEltAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAQDESIgkltKEKKALQEA 1004
Cdd:TIGR02168 420 QQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL----AQLQARLDS 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1005 HQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEKKLRMDLERAkrkLEGDLklaQESIMDLENDKQQSEEKLKK 1084
Cdd:TIGR02168 494 LERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAA---LGGRL---QAVVVENLNAAKKAIAFLKQ 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1085 KDFETSQLLskiEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADL----------------------- 1141
Cdd:TIGR02168 568 NELGRVTFL---PLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvvddldnalelakklrpg 644
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1142 -------------------------------SRELEEISERLEEAGG-ATAAQIEMNKKR------EAEFQKLRRDLEES 1183
Cdd:TIGR02168 645 yrivtldgdlvrpggvitggsaktnssilerRREIEELEEKIEELEEkIAELEKALAELRkeleelEEELEQLRKELEEL 724
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1184 TLQHEATAAALRKKQAdSVAELGEQIDNLQRVKQKLEKEKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKS 1263
Cdd:TIGR02168 725 SRQISALRKDLARLEA-EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1264 KndenlrqindLSAQRARLQTENGEFGRQLEEKEalvsQLTRGKQAFTQQIEELKRQIEEEVKAKNALAHAVQSARHDCD 1343
Cdd:TIGR02168 804 A----------LDELRAELTLLNEEAANLRERLE----SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1344 LLREQFEEEQEAKAELQRGMSKANSEvaqwrtkyETDAIQRTEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRL 1423
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSE--------LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1424 QgevedlmidvERANALAanldkkQRNFDKVLAewkqKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLETLKRE 1503
Cdd:TIGR02168 942 Q----------ERLSEEY------SLTLEEAEA----LENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKER 1001
|
730
....*....|...
gi 288856329 1504 NKNLQQEISDLTE 1516
Cdd:TIGR02168 1002 YDFLTAQKEDLTE 1014
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
896-1761 |
4.33e-18 |
|
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: 91.65 E-value: 4.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 896 ESENLSDAEERCEGLIKSKIQLEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDdleltlakvekekHATEN 975
Cdd:TIGR00606 246 ELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLY-------------HNHQR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 976 KVKNLTEEMAAQDESIGKLTKEKKALQEAH-----QQTLDDLQAEEDKVNTLTKSKTKLEQQ----VDDLEGSLEQEKKL 1046
Cdd:TIGR00606 313 TVREKERELVDCQRELEKLNKERRLLNQEKtellvEQGRLQLQADRHQEHIRARDSLIQSLAtrleLDGFERGPFSERQI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1047 RMDLERAKRKLEGDLKLAQESIMDLENDKQQSEEKLKKKDFETSQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEA 1126
Cdd:TIGR00606 393 KNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDR 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1127 ERAARAKVEKQRADLSRELEEiserleeaggataAQIEMNKKREAEFQKLRRDLEEStlqheataaalRKKQADSVAELG 1206
Cdd:TIGR00606 473 ILELDQELRKAERELSKAEKN-------------SLTETLKKEVKSLQNEKADLDRK-----------LRKLDQEMEQLN 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1207 EQIDNLQRVkQKLEKEKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDENLRQINDLSAQRARLQTEN 1286
Cdd:TIGR00606 529 HHTTTRTQM-EMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNK 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1287 GEFGRQLEEKEALVSQLTR------GKQAFTQQIEELKRQIEEEVKAKNALAHAvqSARHDcDLLREQFEEEQEAKAELQ 1360
Cdd:TIGR00606 608 NHINNELESKEEQLSSYEDklfdvcGSQDEESDLERLKEEIEKSSKQRAMLAGA--TAVYS-QFITQLTDENQSCCPVCQ 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1361 RgmskansevaqwrtkyetdAIQRTEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANAL 1440
Cdd:TIGR00606 685 R-------------------VFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKE 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1441 AANLDKKQRNFDKVLAEWKQKYEEGQAELE---GAQKEARSLSTELFKMKNSYEETldqletlKRENKNLQQEISDLteQ 1517
Cdd:TIGR00606 746 IPELRNKLQKVNRDIQRLKNDIEEQETLLGtimPEEESAKVCLTDVTIMERFQMEL-------KDVERKIAQQAAKL--Q 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1518 LGETGKSIHELEKSKKAVETEKAEIQTALEEAEGTLEHEESKILRVQLELNQVKSEiDRKLAEKDEEIEQIKRNSQRITD 1597
Cdd:TIGR00606 817 GSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE-KLQIGTNLQRRQQFEEQLVELST 895
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1598 SMQSTLDSEVRSRNDALRIKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAMVE 1677
Cdd:TIGR00606 896 EVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQK 975
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1678 rrntlmQSEIEELRAALEQTERGRKVAEQELVDASERVGLLHSQNTSLLN--TKKKLEADLVQIQSEV--------EDTV 1747
Cdd:TIGR00606 976 ------ETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDnlTLRKRENELKEVEEELkqhlkemgQMQV 1049
|
890
....*....|....
gi 288856329 1748 QEARNAEDKAKKAI 1761
Cdd:TIGR00606 1050 LQMKQEHQKLEENI 1063
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
956-1550 |
8.82e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 90.12 E-value: 8.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 956 IDDLELTLAKVEKEKHATENKVKNLtEEMAAQDESIGKLTKEKKalqeahqqtlDDLQAEEDKVNTLTKSKTKLEQQVDD 1035
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERL-EKFIKRTENIEELIKEKE----------KELEEVLREINEISSELPELREELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1036 LEGSLEQEKKLRMDLERAKRKLEGDLKlaqeSIMDLENDKQQSEEKLKKKDFETSQLLSKIEDeqslgaqlQKKIKELQA 1115
Cdd:PRK03918 226 LEKEVKELEELKEEIEELEKELESLEG----SKRKLEEKIRELEERIEELKKEIEELEEKVKE--------LKELKEKAE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1116 RIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQIEMNKKREaefqKLRRDLEESTLQHEATAAALR 1195
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK----ELEKRLEELEERHELYEEAKA 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1196 KKqadsvaelgeqiDNLQRVKQKLEKEkseykmEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDENLRQINDL 1275
Cdd:PRK03918 370 KK------------EELERLKKRLTGL------TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1276 SAQRA------RLQTENGEfGRQLEEKEALVSQLTRGKQAFTQQIEELKRQiEEEVKAKNALAHAVQSARHDCDLLREQF 1349
Cdd:PRK03918 432 KKAKGkcpvcgRELTEEHR-KELLEEYTAELKRIEKELKEIEEKERKLRKE-LRELEKVLKKESELIKLKELAEQLKELE 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1350 E-------EEQEAKAELQRGMSKANSEVAQwRTKYETDAIQRTEELEESKKKLAQRLQEAEEQIEAVNSKCASLE-KTKQ 1421
Cdd:PRK03918 510 EklkkynlEELEKKAEEYEKLKEKLIKLKG-EIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVE 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1422 RLQGEVEDLMIDVERANALAaNLDKKQRNFDKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEEtlDQLETLK 1501
Cdd:PRK03918 589 ELEERLKELEPFYNEYLELK-DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELR 665
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 288856329 1502 RENKNLQQEISDLTEQLGETGKSIHELEKSKKAVETEKAEIQTALEEAE 1550
Cdd:PRK03918 666 EEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE 714
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1210-1898 |
9.85e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 90.12 E-value: 9.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1210 DNLQRVKQKLEKEKSEYKMEIddlssnmeavaKAKANLEKMCRTLEDQLSEIkskndenLRQINDLSAQRARLQTENGEF 1289
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFI-----------KRTENIEELIKEKEKELEEV-------LREINEISSELPELREELEKL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1290 GRQLEEKEALVSQltrgkqaftqqIEELKRQIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQ--RGMSKAN 1367
Cdd:PRK03918 227 EKEVKELEELKEE-----------IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEEY 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1368 SEVAQWRTKYEtdaiQRTEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMidveranalaanldkk 1447
Cdd:PRK03918 296 IKLSEFYEEYL----DELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE---------------- 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1448 qrnfdkVLAEWKQKYEEGQAELEgaqkEARSLSTELfkMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHE 1527
Cdd:PRK03918 356 ------ELEERHELYEEAKAKKE----ELERLKKRL--TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1528 LEKSkkAVETEKAEIQTALEEAEGTLEHEESKILRVQLELNQVKSEidrkLAEKDEEIEQIKRNsqritdsmqstldsev 1607
Cdd:PRK03918 424 LKKA--IEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKE----LKEIEEKERKLRKE---------------- 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1608 rsrndalriKKKMEGDLNEMEIQLShaNRQAAEaqkQLRNVQAQLKDAQLH-LDDAVRGQEDMKEQVAMVERRNTLMQSE 1686
Cdd:PRK03918 482 ---------LRELEKVLKKESELIK--LKELAE---QLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1687 IEELraalEQTERGRKVAEQELVDASERVGLLHsqntsllntkKKLEADLVQIQSEVEDTVQEARNAEDK---AKKAITD 1763
Cdd:PRK03918 548 LEKL----EELKKKLAELEKKLDELEEELAELL----------KELEELGFESVEELEERLKELEPFYNEyleLKDAEKE 613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1764 AAMMAEELKKEQDTsahLERMKKNLEVTVKDLQHRLDEAENLAMKGGKKQLQKLESRVRELESEVEAEQRRGADAVKGVR 1843
Cdd:PRK03918 614 LEREEKELKKLEEE---LDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRRE 690
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 288856329 1844 KYERRVKELTYQTEEDKKNVNRLQDL------VDKLQLKVKAYKrqsEEAEEQANSHLSKL 1898
Cdd:PRK03918 691 EIKKTLEKLKEELEEREKAKKELEKLekalerVEELREKVKKYK---ALLKERALSKVGEI 748
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
966-1834 |
1.53e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 89.82 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 966 VEKEKHATENKVKNLTEEMAAQDESIGKLTKEKKALQEAHQQTLDDLQAEEdkvnTLTKSKTKLEQQVDDLEGSLEQEKK 1045
Cdd:PTZ00121 1041 VLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADE----ATEEAFGKAEEAKKTETGKAEEARK 1116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1046 LrmdlERAKRKLEgDLKLAQESimDLENDKQQSEEKLKKKDFETSQLLSKIED----EQSLGAQLQKKIKELQARIEELE 1121
Cdd:PTZ00121 1117 A----EEAKKKAE-DARKAEEA--RKAEDARKAEEARKAEDAKRVEIARKAEDarkaEEARKAEDAKKAEAARKAEEVRK 1189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1122 EEIEAERAARAKVEK-QRADLSRELEEISERLEEAGGATAAQIEMNKKREAEFQKLR--RDLEESTLQHEATAAALRKKQ 1198
Cdd:PTZ00121 1190 AEELRKAEDARKAEAaRKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEeeRNNEEIRKFEEARMAHFARRQ 1269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1199 ADSVAELGEQIDNLQR---VKQKLEKEKSEYKMEIDDLSSNMEAVAKAKaNLEKMCRTLEDQLSEIKSKNDENLRQIndl 1275
Cdd:PTZ00121 1270 AAIKAEEARKADELKKaeeKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADAAKKKAEEAKKAA--- 1345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1276 SAQRARLQTENGEFGRQLEEKEALVSQLTRGKQaftqQIEELKRQIEEEVKAKNALAHAvqsarhdcdllreqfeEEQEA 1355
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK----KADAAKKKAEEKKKADEAKKKA----------------EEDKK 1405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1356 KAELQRGMSKANSEVAQWRTKYETdaIQRTEELE---ESKKKLAQRLQEAEEQIEAVNSKCASLEKTKqrlqgevedlmi 1432
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKAEE--KKKADEAKkkaEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK------------ 1471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1433 dveranalAANLDKKqrnfdkvlAEWKQKYEEGQAELEGAQKEARSLstelfkmKNSYEETLDQLETLKRENKNLQQEIS 1512
Cdd:PTZ00121 1472 --------ADEAKKK--------AEEAKKADEAKKKAEEAKKKADEA-------KKAAEAKKKADEAKKAEEAKKADEAK 1528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1513 DLTEQlgETGKSIHELEKSKKAVETEKAEiqtALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEEIEQIKRNS 1592
Cdd:PTZ00121 1529 KAEEA--KKADEAKKAEEKKKADELKKAE---ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE 1603
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1593 QRITDSMQSTLDSEVRSRNDALRIKKKMEGDLNEMEIQLSHANRQAAEAQKQlrnvqaqlkdaqlhlddavrgQEDMKEQ 1672
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA---------------------EEENKIK 1662
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1673 VAMVERRNTLMQSEIEELRAALEQTergRKVAEQELVDASErvgllhsqntsllntKKKLEadlvqiqsEVEDTVQEARN 1752
Cdd:PTZ00121 1663 AAEEAKKAEEDKKKAEEAKKAEEDE---KKAAEALKKEAEE---------------AKKAE--------ELKKKEAEEKK 1716
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1753 AEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENLAMKGGKKQLQKLESRVRELESEVEAEQ 1832
Cdd:PTZ00121 1717 KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEV 1796
|
..
gi 288856329 1833 RR 1834
Cdd:PTZ00121 1797 DK 1798
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1084-1763 |
2.99e-17 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 88.15 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1084 KKDFETSQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGAT---A 1160
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLskiN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1161 AQIEMNK----KREAEFQKLRRDLEESTLQHEATAAALRKKQADsVAELGEQIDNLQRVKQKLEKEKSEYKMEIDDLSSN 1236
Cdd:TIGR04523 110 SEIKNDKeqknKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE-LEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1237 MeavakakANLEKMCRTLEDQLSEIKSKNDENlrqiNDLSAQRARLQTENGEFGRQLEEKEALVSQLTRGKQAFTQQIEE 1316
Cdd:TIGR04523 189 I-------DKIKNKLLKLELLLSNLKKKIQKN----KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1317 LKrqiEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELqrgmSKANSEVAQ-WRTKYETDAIQRTEELEESKKKL 1395
Cdd:TIGR04523 258 LK---DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEI----SDLNNQKEQdWNKELKSELKNQEKKLEEIQNQI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1396 AQrlqeAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANALAANLDKKQRNFDKVLAEWKQKYEEGQAELEGAQKE 1475
Cdd:TIGR04523 331 SQ----NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1476 ARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAVET-------EKAEIQTALEE 1548
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETqlkvlsrSINKIKQNLEQ 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1549 AEGTLEHEESKILrvqlELNQVKSEIDRKLAEKDEEIEQIKrNSQRITDSMQSTLDSEVRSRNDALrIKKKMEGDLNEME 1628
Cdd:TIGR04523 487 KQKELKSKEKELK----KLNEEKKELEEKVKDLTKKISSLK-EKIEKLESEKKEKESKISDLEDEL-NKDDFELKKENLE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1629 IQLSHANRQAaeaqKQLRNVQAQLKDAQLHLDDAVRGQEDmkeqvamverrntlmqsEIEELRAALEQTERGRKVAEQEL 1708
Cdd:TIGR04523 561 KEIDEKNKEI----EELKQTQKSLKKKQEEKQELIDQKEK-----------------EKKDLIKEIEEKEKKISSLEKEL 619
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 288856329 1709 VDASERVGLLHSQNTSLLNTKKKLEADLVQIQSEVEDTVQEARNAEDKAKKAITD 1763
Cdd:TIGR04523 620 EKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTK 674
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
843-1457 |
5.30e-17 |
|
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: 87.82 E-value: 5.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 843 KSAETEKELATMKEDFVKCKEDLAKAEAKKKELEEKMVALLQEKNDLQLAVASESENLSDAEERCEGLIKSKIQLEAKLK 922
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 923 ETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAQDESIGKLTKEK---- 998
Cdd:TIGR02169 459 QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGerya 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 999 KALQEAHQQTLDDLQAEED--------------------------KVNTLTKSKTKLEQQVDDLEGSLEQEKKLR----- 1047
Cdd:TIGR02169 539 TAIEVAAGNRLNNVVVEDDavakeaiellkrrkagratflplnkmRDERRDLSILSEDGVIGFAVDLVEFDPKYEpafky 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1048 --------MDLERAKR--------KLEGDL--------------KLAQESIMDLENDKQQSEEKLKKKDFETSQLLSKIE 1097
Cdd:TIGR02169 619 vfgdtlvvEDIEAARRlmgkyrmvTLEGELfeksgamtggsrapRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELR 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1098 DEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAggataaqiemnkkrEAEFQKLR 1177
Cdd:TIGR02169 699 RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV--------------KSELKELE 764
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1178 RDLEEstlqHEATAAALRKKQADSVAELG-EQIDNLQRVKQKLEKEKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLED 1256
Cdd:TIGR02169 765 ARIEE----LEEDLHKLEEALNDLEARLShSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE 840
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1257 QLSEIKSKNDENLRQINDLSAQRARLQTEngefgrqLEEKEALVSQLTRGKQAFTQQIEELKRQIEEEVKAKNALAHAVQ 1336
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEE-------LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE 913
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1337 SARHDCDLLREQFEEEQEAKAELqrgmskansEVAQWRTKYETDAIQRTEELEESKKKLAQRLQE-------AEEQIEAV 1409
Cdd:TIGR02169 914 KKRKRLSELKAKLEALEEELSEI---------EDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAlepvnmlAIQEYEEV 984
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 288856329 1410 NSKCASLEKTKQRLQGEVEDL-----MIDVERANALAANLDKKQRNFDKVLAE 1457
Cdd:TIGR02169 985 LKRLDELKEKRAKLEEERKAIlerieEYEKKKREVFMEAFEAINENFNEIFAE 1037
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
902-1551 |
5.80e-17 |
|
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: 87.72 E-value: 5.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 902 DAEERCEGLIKSKIQLEAKLKETTERLEDEEEINAELTAK------KRKLEDECSELKKDIDDLELTLAKVEKEKHATE- 974
Cdd:TIGR00618 209 CTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKreaqeeQLKKQQLLKQLRARIEELRAQEAVLEETQERINr 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 975 -NKVKNLTEEMAA------QDESIGKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEKKLR 1047
Cdd:TIGR00618 289 aRKAAPLAAHIKAvtqieqQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIR 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1048 MDLERAKRKLEGDLKLAQesimDLENDKQQSEEKLKKKDFETSQ------LLSKIEDEQSLGAQLQKKIKELQARIEELE 1121
Cdd:TIGR00618 369 EISCQQHTLTQHIHTLQQ----QKTTLTQKLQSLCKELDILQREqatidtRTSAFRDLQGQLAHAKKQQELQQRYAELCA 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1122 EEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQIEMNKKREA---EFQKLRRDLEESTLQHEATAAALRKKQ 1198
Cdd:TIGR00618 445 AAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLArllELQEEPCPLCGSCIHPNPARQDIDNPG 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1199 ADS---------VAELGEQIDNLQRVKQKLEKEKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDENL 1269
Cdd:TIGR00618 525 PLTrrmqrgeqtYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1270 RqindlsaQRARLQTENGEFGRQLEEKEALVS-QLTRGKQAFTQQIEELKRQIEEEVKAKNALAHAVQSARHDCDLLREQ 1348
Cdd:TIGR00618 605 E-------AEDMLACEQHALLRKLQPEQDLQDvRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLAS 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1349 FEEEQEAKAELQRGMSKANSEVAQWRTKyetdaiqrTEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVE 1428
Cdd:TIGR00618 678 RQLALQKMQSEKEQLTYWKEMLAQCQTL--------LRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELM 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1429 DlmidvERANALAANLDKKQRNFDKVLAEWK--QKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLD--------QLE 1498
Cdd:TIGR00618 750 H-----QARTVLKARTEAHFNNNEEVTAALQtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPsdedilnlQCE 824
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 288856329 1499 TLKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAVET---EKAEIQTALEEAEG 1551
Cdd:TIGR00618 825 TLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQltqEQAKIIQLSDKLNG 880
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
832-1513 |
3.59e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 85.58 E-value: 3.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 832 MKVYYKIKPLLKSAETEKELATMKEDFVKCKEDLAKAEAKKKELEEKMVALLQEKNDLQLAVASESENLSDAeerceglI 911
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA-------A 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 912 KSKIQLEAKLKETTERLEDEEEINAELTAKKRKL-EDECSELKKDIDDLEltlAKVEKEKHATENKVKnlTEEMAAQDES 990
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaEKKKEEAKKKADAAK---KKAEEKKKADEAKKK--AEEDKKKADE 1409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 991 IGKLTKEKKALQEAHQqtlddlQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGD-LKLAQESIM 1069
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKK------KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADeAKKKAEEAK 1483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1070 DLENDKQQSEEKLKKKDFETSQLLSKIEDEQSLGAQLQKKIKELQARIeeleeeieaeraarakvEKQRADLSRELEEIs 1149
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE-----------------EAKKADEAKKAEEK- 1545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1150 ERLEEAGGATaaqiEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEYKME 1229
Cdd:PTZ00121 1546 KKADELKKAE----ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1230 IDDLSSNmEAVAKAKANLEKMCRTLEDQLSEIKSKNDENLRQINDLsAQRARLQTENGEFGRQLEEKEALVSQLTRGKQA 1309
Cdd:PTZ00121 1622 AEELKKA-EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE-AKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE 1699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1310 FTQQIEELKRQIEEEVKAKNALAHAVQSARHDCDLLREQfEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEEL- 1388
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE-AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKe 1778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1389 ----EESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANALAANLDKKQRNFDKVLAewKQKYEE 1464
Cdd:PTZ00121 1779 avieEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFE--KHKFNK 1856
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 288856329 1465 GQAELEGAQKEARSlSTELFKMKNSYEETLDQLETLKRENKNLQQEISD 1513
Cdd:PTZ00121 1857 NNENGEDGNKEADF-NKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPN 1904
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1445-1926 |
4.04e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 84.71 E-value: 4.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1445 DKKQRNFDKVLAEWKQKYEEGQAELE--GAQKE-ARSLSTELFKMKNSYEETLDQLETLKrenknlqQEISDLTEQLGET 1521
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIEryEEQREqARETRDEADEVLEEHEERREELETLE-------AEIEDLRETIAET 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1522 GKsihELEKSKKAVETEKAEIQTALEEAEGTLEH------EESKILRVQLELNQVKSEIDRKLAEKDEEIEQIKRNSQRI 1595
Cdd:PRK02224 271 ER---EREELAEEVRDLRERLEELEEERDDLLAEaglddaDAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1596 TDSMQstldsEVRSRNDALRIK-KKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVA 1674
Cdd:PRK02224 348 REDAD-----DLEERAEELREEaAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1675 MVERRNTLMQSEIEELRAALEQTER----------GRKVAEQELVDASERVGllhsqntsllNTKKKLEADLVQIQSEVE 1744
Cdd:PRK02224 423 ELREREAELEATLRTARERVEEAEAlleagkcpecGQPVEGSPHVETIEEDR----------ERVEELEAELEDLEEEVE 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1745 DTvqEARNAEdkakkaitdaammAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAEnlamkggkKQLQKLESRVREL 1824
Cdd:PRK02224 493 EV--EERLER-------------AEDLVEAEDRIERLEERREDLEELIAERRETIEEKR--------ERAEELRERAAEL 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1825 ESEVEAEQRRGADAVKGVRKYERRVKELTYQTEEDKKNVNRLQDLVDKLQLKVKAYKRQSE---------EAEEQANSHL 1895
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERlrekrealaELNDERRERL 629
|
490 500 510
....*....|....*....|....*....|.
gi 288856329 1896 SKLRKVQHELEEAEERADIAESQVNKLRAKS 1926
Cdd:PRK02224 630 AEKRERKRELEAEFDEARIEEAREDKERAEE 660
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
917-1588 |
5.51e-16 |
|
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: 83.92 E-value: 5.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 917 LEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATE-------NKVKNLTEEMAAQDE 989
Cdd:TIGR04523 80 LEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKknidkflTEIKKKEKELEKLNN 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 990 SIGKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEKKLRMDLErakrKLEGDLKLAQESIM 1069
Cdd:TIGR04523 160 KYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQIS----ELKKQNNQLKDNIE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1070 DLENDKQQSEEKLKKKDFETSQLLSKIEDEQSlgaQLQKKIKELQARIEELEEEIEAERAARAKVE----KQRADLSREL 1145
Cdd:TIGR04523 236 KKQQEINEKTTEISNTQTQLNQLKDEQNKIKK---QLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnnQKEQDWNKEL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1146 EEISERLEEAGGATAAQIEMNKKREAEF----QKLRRDLEESTLQHEataaalrkkqadsvaELGEQIDNLQRVKQKLEK 1221
Cdd:TIGR04523 313 KSELKNQEKKLEEIQNQISQNNKIISQLneqiSQLKKELTNSESENS---------------EKQRELEEKQNEIEKLKK 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1222 EKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDENLRQINDLSAQRARLQTENGEFGRQLEEKEALVS 1301
Cdd:TIGR04523 378 ENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1302 QLTRGKQAFTQQIEELKRQIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVaqwrtkyetda 1381
Cdd:TIGR04523 458 NLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKI----------- 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1382 iqrtEELEESKKKLAQRLQEAEEQIEAVNS--KCASLEKTKQRLQGEVEDLMIDVEranalaaNLDKKQRNFDKVLAEWK 1459
Cdd:TIGR04523 527 ----EKLESEKKEKESKISDLEDELNKDDFelKKENLEKEIDEKNKEIEELKQTQK-------SLKKKQEEKQELIDQKE 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1460 QKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAVETEK 1539
Cdd:TIGR04523 596 KEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI 675
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 288856329 1540 AE-IQTALEEAEGTLEHEESKIlrvqleLNQVKSEIDRKLAEKDEEIEQI 1588
Cdd:TIGR04523 676 DDiIELMKDWLKELSLHYKKYI------TRMIRIKDLPKLEEKYKEIEKE 719
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1210-1905 |
6.37e-16 |
|
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: 84.25 E-value: 6.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1210 DNLQRVKQKLEKEKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKsKNDENLRQINDLSAQRARLQTENGEF 1289
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQ-QSHAYLTQKREAQEEQLKKQQLLKQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1290 GRQLEEKEALVSQLtrgkqAFTQQIEELKRQIEEEVKAKNALAHAVQSArhdcdllreqfeeeQEAKAELQRGMSKANSE 1369
Cdd:TIGR00618 266 RARIEELRAQEAVL-----EETQERINRARKAAPLAAHIKAVTQIEQQA--------------QRIHTELQSKMRSRAKL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1370 VAQWRtkyetdAIQRTEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTK-------QRLQGEVEDLMIDVERANALAA 1442
Cdd:TIGR00618 327 LMKRA------AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIScqqhtltQHIHTLQQQKTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1443 NLDKKQRNFDKVLAEwKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGeTG 1522
Cdd:TIGR00618 401 ELDILQREQATIDTR-TSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ-TK 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1523 KSIHELEKSKKAVETEKAEIQTALE-EAEGTLEHEE-------------SKILRVQLELNQVKSEIDRKLAEKDEEIEQI 1588
Cdd:TIGR00618 479 EQIHLQETRKKAVVLARLLELQEEPcPLCGSCIHPNparqdidnpgpltRRMQRGEQTYAQLETSEEDVYHQLTSERKQR 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1589 KRNSQRITDSMQSTLDSEV---RSRNDALRIKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRG 1665
Cdd:TIGR00618 559 ASLKEQMQEIQQSFSILTQcdnRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCS 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1666 QEDMKEQVAMVERRNTLMQSEIEELRAALEQTERGRKVAEQELVDASErvgllhSQNTSLLNTKKKLEadlvQIQSeved 1745
Cdd:TIGR00618 639 QELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQ------SEKEQLTYWKEMLA----QCQT---- 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1746 tvqearnaedkakkaitdaaMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLD---EAENLAMKGGKKQLQKLESRVR 1822
Cdd:TIGR00618 705 --------------------LLRELETHIEEYDREFNEIENASSSLGSDLAAREDalnQSLKELMHQARTVLKARTEAHF 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1823 ELESEVEAEQRRGADAVKGVRKYERRVKELTYQTEEDKKNVNRLQDLVDKLQLKVKAYKRQSEEAEEQANSHLSKLRKVQ 1902
Cdd:TIGR00618 765 NNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATL 844
|
...
gi 288856329 1903 HEL 1905
Cdd:TIGR00618 845 GEI 847
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
880-1274 |
1.51e-15 |
|
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: 83.18 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 880 VALLQEK-NDLQLAVASESENLSDAEERCEGLIKSKIQLEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDD 958
Cdd:TIGR02168 686 IEELEEKiAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 959 LELTLAKVEKEKHATENKVKNLTEEMAAQDESIGKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEG 1038
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1039 SLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSEEKLKKKDFETSQLLSKIEDEQSLGAQLQKKIKELQARie 1118
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK-- 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1119 eleeeieaeraaRAKVEKQRADLSRELEEISERLEEAGGATA-AQIEMNKKREAEFQKLRRdleestlqheataaalrkk 1197
Cdd:TIGR02168 924 ------------LAQLELRLEGLEVRIDNLQERLSEEYSLTLeEAEALENKIEDDEEEARR------------------- 972
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 288856329 1198 qadSVAELGEQIDNLQRVKQKLEKEKSEYKMEIDDLSSNMEAVAKAKANLEKmcrTLEDQLSEIKSKNDENLRQIND 1274
Cdd:TIGR02168 973 ---RLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEE---AIEEIDREARERFKDTFDQVNE 1043
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
918-1784 |
1.98e-15 |
|
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: 82.71 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 918 EAKLKETTERL-----EDEEEINAEL-TAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAQDEsi 991
Cdd:pfam02463 175 LKKLIEETENLaeliiDLEELKLQELkLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEE-- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 992 gklTKEKKALQEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEK-KLRMDLERAKRKLEGDLKLAQESIMD 1070
Cdd:pfam02463 253 ---IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELlKLERRKVDDEEKLKESEKEKKKAEKE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1071 LENDKQQSEEKLKKKDFETSQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISE 1150
Cdd:pfam02463 330 LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1151 RLEeaggataaqIEMNKKREAEFQKLRRDLEESTLQHEATAaalrkkqadsvAELGEQIDNLQRVKQKLEKEKSEYKMEI 1230
Cdd:pfam02463 410 LLE---------LARQLEDLLKEEKKEELEILEEEEESIEL-----------KQGKLTEEKEELEKQELKLLKDELELKK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1231 DDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDENLRQINDLSAQRARLQTENGEFGRQLEEKEALVSQLTRGKQAF 1310
Cdd:pfam02463 470 SEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1311 TQQIEELKRQIEEEVKAKNAL----------AHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRTKYETD 1380
Cdd:pfam02463 550 IVEVSATADEVEERQKLVRALtelplgarklRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGIL 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1381 AIQRTEELEESKKKLAQRLQEAEEQIEAVNSKC---ASLEKTKQRLQGEVEDLMID--VERANALAANLDKKQRNFDKVL 1455
Cdd:pfam02463 630 KDTELTKLKESAKAKESGLRKGVSLEEGLAEKSevkASLSELTKELLEIQELQEKAesELAKEEILRRQLEIKKKEQREK 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1456 AEWKQKYEEGQAELEGAQKEARSLSTELFKMKNSyEETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAV 1535
Cdd:pfam02463 710 EELKKLKLEAEELLADRVQEAQDKINEELKLLKQ-KIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKV 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1536 ETEKAEIQTALEEAegtlehEESKILRVQLELNQVKSEIDRKLAEKDEEIEQIKRNSQRITDSMQSTLDSEVRSRNDALR 1615
Cdd:pfam02463 789 EEEKEEKLKAQEEE------LRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEE 862
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1616 IKKK--------MEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHlDDAVRGQEDMKEQVAMVERRNTLMQSEI 1687
Cdd:pfam02463 863 ITKEellqelllKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLE-EKENEIEERIKEEAEILLKYEEEPEELL 941
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1688 EELRAALEQTERGRKVAEQELVDASERVGLLHSQNTSLLNTKKKLEADLVQIQSEVEDTVQEarNAEDKAKKAITDAAMM 1767
Cdd:pfam02463 942 LEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE--KKKLIRAIIEETCQRL 1019
|
890
....*....|....*..
gi 288856329 1768 AEELKKEQDTSAHLERM 1784
Cdd:pfam02463 1020 KEFLELFVSINKGWNKV 1036
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
885-1430 |
2.28e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.40 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 885 EKNDLQLAVASESENLSDAEERCEGLIKSKIQLEAKLKETTERLEDEEEINAELTakkrkledecsELKKDIDDLELTLA 964
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE-----------TLEAEIEDLRETIA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 965 KVEKEKHAtenkvknLTEEMAAQDESIGKLTKEKKALQEahQQTLDDLQAE--EDKVNTLTKSKTKLEQQVDDLEGSLEQ 1042
Cdd:PRK02224 269 ETEREREE-------LAEEVRDLRERLEELEEERDDLLA--EAGLDDADAEavEARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1043 EKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSEEKLKKKDFETSQLLSKIEDeqslgaqLQKKIKELQARIEELEE 1122
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE-------LRERFGDAPVDLGNAED 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1123 EIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAA--------------QIEMNKKREAEFQKLRRDLEESTLQHE 1188
Cdd:PRK02224 413 FLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVE 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1189 ATAAALrkKQADSVAELGEQIDNLQRVKQKLEKEKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDEN 1268
Cdd:PRK02224 493 EVEERL--ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEA 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1269 LRQINDLSAQRARLQTEngefgrqLEEKEALVSQLTRgkqaftqqIEELKRQIEEEVKAKNALAHAVqsarhdcDLLREQ 1348
Cdd:PRK02224 571 REEVAELNSKLAELKER-------IESLERIRTLLAA--------IADAEDEIERLREKREALAELN-------DERRER 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1349 FEEEQEAKAELQRGMSKANSEVAQWR----TKYETDAIQRTEELEESKKKLAQRLQEAEEQIEAVNS---KCASLEKTKQ 1421
Cdd:PRK02224 629 LAEKRERKRELEAEFDEARIEEAREDkeraEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEElreRREALENRVE 708
|
570
....*....|..
gi 288856329 1422 RLQ---GEVEDL 1430
Cdd:PRK02224 709 ALEalyDEAEEL 720
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1075-1928 |
2.97e-15 |
|
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: 81.94 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1075 KQQSEEKLKKKDFETSQLLSK-------IEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEE 1147
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELiidleelKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1148 ISERLEEAGGATAAQIEMNKKREAEFQKLrrDLEESTLQHEataaaLRKKQADSVAELGEQIDNLQRVKQKLEKEKSEYK 1227
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEEKLAQVLKENKE--EEKEKKLQEE-----ELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1228 MEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDENLRQINDLSAQRARLQTENGE----FGRQLEEKEALVSQL 1303
Cdd:pfam02463 321 KEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLeserLSSAAKLKEEELELK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1304 TRGKQAFTQQIEELKRQIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKaELQRGMSKANSEVAqwrtKYETDAIQ 1383
Cdd:pfam02463 401 SEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEEL-EKQELKLLKDELEL----KKSEDLLK 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1384 RTEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANALAANLDKKQRNFDKVLAEWKQKYE 1463
Cdd:pfam02463 476 ETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSA 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1464 EGQAELEGAQKEARSLSTELFKMKNSYEETLDQLE---TLKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAVETEKA 1540
Cdd:pfam02463 556 TADEVEERQKLVRALTELPLGARKLRLLIPKLKLPlksIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELT 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1541 EIQTALEEAEGTLEH--EESKILRVQLELNQVKSEIDRKLAEKDEEIEQIKRNSQRITDSMQSTLDSEVRSRNDALRIKK 1618
Cdd:pfam02463 636 KLKESAKAKESGLRKgvSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKL 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1619 KMEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAMvERRNTLMQSEIEELRAALEQTE 1698
Cdd:pfam02463 716 KLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLK-EKELAEEREKTEKLKVEEEKEE 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1699 RgRKVAEQELVDASERVGLLHSQNTSLLNTKKKLEADLVQIQSEVEDTVQEARNAEDKAKKAITDAAMMAEELKKEQDTS 1778
Cdd:pfam02463 795 K-LKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELL 873
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1779 AHLERMKKNLEVTVKDLQHRLDEAENLAMKGGKKQLQKLESRVRELESEVEAEQrrgadavKGVRKYERRVKELtyqTEE 1858
Cdd:pfam02463 874 LKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEA-------EILLKYEEEPEEL---LLE 943
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1859 DKKNVNRLQDLVDKLQLKVKAYKRQSEEAEEQANSHLSklrkvqhELEEAEERADIAESQVNKLRAKSRD 1928
Cdd:pfam02463 944 EADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIE-------EFEEKEERYNKDELEKERLEEEKKK 1006
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1292-1826 |
3.38e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 81.62 E-value: 3.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1292 QLEEKEA--LVSQLTRGKQAFTQQIEELKRQIEEEVKAKnalahavqSARHDCDLLREQFEEEQEAKAELQRGMSKANSE 1369
Cdd:PRK02224 195 QIEEKEEkdLHERLNGLESELAELDEEIERYEEQREQAR--------ETRDEADEVLEEHEERREELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1370 VAQWRTKYET------DAIQRTEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANALAAN 1443
Cdd:PRK02224 267 IAETEREREElaeevrDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAES 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1444 LDKKQRNFDKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEE-------TLDQLETLKRENKNLQQEISDLTE 1516
Cdd:PRK02224 347 LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEElrerfgdAPVDLGNAEDFLEELREERDELRE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1517 QLGETGKSIHELEKSKKAVET--------------EKAEIQTALEEAEGTLEHEESKILRVQLELNQVKSEIDR--KLAE 1580
Cdd:PRK02224 427 REAELEATLRTARERVEEAEAlleagkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERaeDLVE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1581 KDEEIEQIKRNSQRITDSMqSTLDSEVRSRNDALRIKKKMEGDLN-EMEIQLSHANRQAAEAQKQLRNVqAQLKDAQLHL 1659
Cdd:PRK02224 507 AEDRIERLEERREDLEELI-AERRETIEEKRERAEELRERAAELEaEAEEKREAAAEAEEEAEEAREEV-AELNSKLAEL 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1660 DDAVRGQEDMKEQVAMVERrntlMQSEIEELRAALEQ-TERGRKVAEQeLVDASERvgllhsqntsllntKKKLEADLvq 1738
Cdd:PRK02224 585 KERIESLERIRTLLAAIAD----AEDEIERLREKREAlAELNDERRER-LAEKRER--------------KRELEAEF-- 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1739 iqseVEDTVQEARNAEDKAKKAITDAAMMAEELKKEQDtsahlermkkNLEVTVKDLQHRLDEAENLamkggKKQLQKLE 1818
Cdd:PRK02224 644 ----DEARIEEAREDKERAEEYLEQVEEKLDELREERD----------DLQAEIGAVENELEELEEL-----RERREALE 704
|
....*...
gi 288856329 1819 SRVRELES 1826
Cdd:PRK02224 705 NRVEALEA 712
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1035-1654 |
6.18e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 81.11 E-value: 6.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1035 DLEGSLEQEKKLRMDLERAKRKLEgdlkLAQESIMDLE--NDKQQSEEKLKKKDFETSQLLSKIEDEQSlgaqlQKKIKE 1112
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALE----DAREQIELLEpiRELAERYAAARERLAELEYLRAALRLWFA-----QRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1113 LQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQIEmnkKREAEFQKLRRDLEESTLQHEATAA 1192
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLE---REIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1193 ALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEYKMEIDDLssnmeAVAKAKANLEKmcRTLEDQLSEIKSKN---DENL 1269
Cdd:COG4913 370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEA-----EAALRDLRREL--RELEAEIASLERRKsniPARL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1270 RQINDLSAQRARLQTEN----GE---------------------FGRQL---EEKEALVSQL---TRGKQAF-TQQIEEL 1317
Cdd:COG4913 443 LALRDALAEALGLDEAElpfvGElievrpeeerwrgaiervlggFALTLlvpPEHYAAALRWvnrLHLRGRLvYERVRTG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1318 KRQIEEEVKAKNALAHAVQSARHDC-----DLLREQF-------EEE--QEAKAELQRGMSKANsevaqwRTKYETDAiq 1383
Cdd:COG4913 523 LPDPERPRLDPDSLAGKLDFKPHPFrawleAELGRRFdyvcvdsPEElrRHPRAITRAGQVKGN------GTRHEKDD-- 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1384 rteeleesKKKLAQRL---QEAEEQIEAvnskcasLEKTKQRLQGEVEDLMIDVERANALAANLDKKQRNFDKVlaewkQ 1460
Cdd:COG4913 595 --------RRRIRSRYvlgFDNRAKLAA-------LEAELAELEEELAEAEERLEALEAELDALQERREALQRL-----A 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1461 KYEEGQAELEGAQKEARSLSTELFKMknsyEETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAVETEKA 1540
Cdd:COG4913 655 EYSWDEIDVASAEREIAELEAELERL----DASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1541 EIQTALEEAEGTLEHEESKIL---RVQLELNQVKSEIDRKLAEK-DEEIEQIKRNSQRITDSMQ----------STLDSE 1606
Cdd:COG4913 731 ELQDRLEAAEDLARLELRALLeerFAAALGDAVERELRENLEERiDALRARLNRAEEELERAMRafnrewpaetADLDAD 810
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 288856329 1607 VRSRNDALRIKKKMEGD------------LNEMEIQ-----LSHANRQAAEAQKQLRNVQAQLKD 1654
Cdd:COG4913 811 LESLPEYLALLDRLEEDglpeyeerfkelLNENSIEfvadlLSKLRRAIREIKERIDPLNDSLKR 875
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
906-1655 |
6.42e-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: 80.78 E-value: 6.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 906 RCEGLIKSKIQLEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHAT----ENKVKNLT 981
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERkqvlEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 982 EEMAAQDESIGKLTKEKKALQEAH--QQTLDDLQAEEDKVNTLTKSKTKLEQQVDdlegslEQEKKLRMDLErakrkleg 1059
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEELRAQEAVLEETQERIN------RARKAAPLAAH-------- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1060 dlklaQESIMDLENDKQQSEEKLKKKDFETSQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKvekqRA 1139
Cdd:TIGR00618 299 -----IKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSI----RE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1140 DLSRELEeiserLEEAGGATAAQIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKL 1219
Cdd:TIGR00618 370 ISCQQHT-----LTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1220 EKEKSEYKMEIddlssnmeavaKAKANLEKMCRTLEDQlseiksknDENLRQINDLSAQRARLQTENGEFGRQLEEKEAL 1299
Cdd:TIGR00618 445 AAITCTAQCEK-----------LEKIHLQESAQSLKER--------EQQLQTKEQIHLQETRKKAVVLARLLELQEEPCP 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1300 VSQLTRGKQAFTQQIEE---LKRQIEEEVKAKNALAHAVQSARHDCDLLREQF----EEEQEAKAELQRGMSKAN--SEV 1370
Cdd:TIGR00618 506 LCGSCIHPNPARQDIDNpgpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRaslkEQMQEIQQSFSILTQCDNrsKED 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1371 AQWRTKYETDAIQRTEELEESKKKLA--QRLQEAEEQIEAVNSKCA--------SLEKTKQRLQGEVEDLMIDVERANAL 1440
Cdd:TIGR00618 586 IPNLQNITVRLQDLTEKLSEAEDMLAceQHALLRKLQPEQDLQDVRlhlqqcsqELALKLTALHALQLTLTQERVREHAL 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1441 AANLDKKQrnfdkvlaewkqKYEEGQAELEGAQKEARSLSTELfKMKNSYEETLDQLETLKRENKNLQQEI--------S 1512
Cdd:TIGR00618 666 SIRVLPKE------------LLASRQLALQKMQSEKEQLTYWK-EMLAQCQTLLRELETHIEEYDREFNEIenassslgS 732
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1513 DLTEQLGETGKSIHELEKSKKAVETEKAEIQTALEEAEGTLEH---EESKILRVQLELNQVKSEIDRKLAEKDEEIEQIK 1589
Cdd:TIGR00618 733 DLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQtgaELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEI 812
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 288856329 1590 RNSQRITDSMQSTLDSEVRSRNDALRIKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDA 1655
Cdd:TIGR00618 813 PSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1374-1924 |
8.31e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.49 E-value: 8.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1374 RTKYETDAIQRTEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANAL----------AAN 1443
Cdd:PRK03918 177 RIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELekeleslegsKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1444 LDKKQRNFDKVLAEWKQKYEEGQaELEGAQKEARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGETGK 1523
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELE-EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1524 SIHELEKSKKavetEKAEIQTALEEAEGTLEHEEsKILRVQLELNQVKSEIDRKLAEK-DEEIEQIKRNSQRITD----- 1597
Cdd:PRK03918 336 KEERLEELKK----KLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPEKlEKELEELEKAKEEIEEeiski 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1598 -SMQSTLDSEVRSRNDALRIKKKMEGD--LNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAqlhlddavrgqEDMKEQVA 1674
Cdd:PRK03918 411 tARIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEI-----------EEKERKLR 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1675 MVERrntlmqsEIEELRAALEQTERGRKVAEQelvdaservgllhsqntsLLNTKKKLEADLVQiqsEVEDTVQEARNAE 1754
Cdd:PRK03918 480 KELR-------ELEKVLKKESELIKLKELAEQ------------------LKELEEKLKKYNLE---ELEKKAEEYEKLK 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1755 DKAKKAITDAAMMAEELKKEQDtsahLERMKKNLEVTVKDLQHRLDEAENLAMKGGKKQLQKLESRVRELESEVEaEQRR 1834
Cdd:PRK03918 532 EKLIKLKGEIKSLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYN-EYLE 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1835 GADAVKGVRKYERRVKELTYQTEEDKKNVNRLQDLVDKLQLKVKAYKRQ--SEEAEEQANSHLSK---LRKVQHELEEAE 1909
Cdd:PRK03918 607 LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKysEEEYEELREEYLELsreLAGLRAELEELE 686
|
570
....*....|....*
gi 288856329 1910 ERADIAESQVNKLRA 1924
Cdd:PRK03918 687 KRREEIKKTLEKLKE 701
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1200-1911 |
1.06e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 80.34 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1200 DSVAELGEQIDNLQRVKQKLEKEKSEYKM--EIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSknDENLRQINDLSA 1277
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRLWFAQRRL--ELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1278 QRARLQTENGEFGRQLEEKEALVSQLTRGKQAF-TQQIEELKRQIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAK 1356
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1357 AELQRgmskansEVAQWRTKYEtdaiQRTEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLmidveR 1436
Cdd:COG4913 383 AALRA-------EAAALLEALE----EELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL-----R 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1437 AnALAANLDKKQRNFdKVLAEW---KQKYEEGQAELEGAqkeARSLSTELFKMKNSYEETLDQLETLKRenknlqqeisd 1513
Cdd:COG4913 447 D-ALAEALGLDEAEL-PFVGELievRPEEERWRGAIERV---LGGFALTLLVPPEHYAAALRWVNRLHL----------- 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1514 lteqlgetgksiheleksKKAVETEKAEiqTALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKD-----EEIEQI 1588
Cdd:COG4913 511 ------------------RGRLVYERVR--TGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAELGRRFdyvcvDSPEEL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1589 KRNSQRITDSMQSTLDSEVRSRNDALRIKKK-------------MEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLkDA 1655
Cdd:COG4913 571 RRHPRAITRAGQVKGNGTRHEKDDRRRIRSRyvlgfdnraklaaLEAELAELEEELAEAEERLEALEAELDALQERR-EA 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1656 QLHLDDAVRGQEDMKEQVAMVERRntlmQSEIEELRAA---LEQTERGRKVAEQELVDASERVGLLHSQntsllntKKKL 1732
Cdd:COG4913 650 LQRLAEYSWDEIDVASAEREIAEL----EAELERLDASsddLAALEEQLEELEAELEELEEELDELKGE-------IGRL 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1733 EADLVQIQSEVEdtvQEARNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAEnlamkggkk 1812
Cdd:COG4913 719 EKELEQAEEELD---ELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAE--------- 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1813 qlQKLESRVRELESEVEAEQRRGADAVKGVRKYERRVKELtyqtEEDkknvnrlqDLVDKLQlkvkAYKRQSEEAEEQAN 1892
Cdd:COG4913 787 --EELERAMRAFNREWPAETADLDADLESLPEYLALLDRL----EED--------GLPEYEE----RFKELLNENSIEFV 848
|
730
....*....|....*....
gi 288856329 1893 SHLskLRKVQHELEEAEER 1911
Cdd:COG4913 849 ADL--LSKLRRAIREIKER 865
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
920-1490 |
1.27e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.96 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 920 KLKETTERLEDEEEINAELTAKKRKLEdecselKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAQDESIGKLTKEKK 999
Cdd:COG4913 246 DAREQIELLEPIRELAERYAAARERLA------ELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1000 ALQEahqqTLDDLQAEEDKVNTltKSKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKL-------EGDLKLAQESIMDLE 1072
Cdd:COG4913 320 ALRE----ELDELEAQIRGNGG--DRLEQLEREIERLERELEERERRRARLEALLAALglplpasAEEFAALRAEAAALL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1073 NDKQQSEEKLKKKDFETSQLLSKIEDEQslgAQLQKKIKELqarieeleeeieaeraarakvEKQRADLSRELEEISERL 1152
Cdd:COG4913 394 EALEEELEALEEALAEAEAALRDLRREL---RELEAEIASL---------------------ERRKSNIPARLLALRDAL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1153 EEAGGATAAQ-------IEMnKKREAEFQK--------LRRDL--EEstlQHEATAAA------LRKK-QADSVAELGEQ 1208
Cdd:COG4913 450 AEALGLDEAElpfvgelIEV-RPEEERWRGaiervlggFALTLlvPP---EHYAAALRwvnrlhLRGRlVYERVRTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1209 IDNLQRVKQ----KLEKEKSEYKMEIDDLSSNMEAVAKAkANLEKMCR-----TLEDQLseiksKNDENLRQINDLSAQR 1279
Cdd:COG4913 526 PERPRLDPDslagKLDFKPHPFRAWLEAELGRRFDYVCV-DSPEELRRhpraiTRAGQV-----KGNGTRHEKDDRRRIR 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1280 ARLQtengeFG----RQLEEKEALVSQLTRGKQAFTQQIEELKRQIEEEVKAKNALAHAVQSARHDCDLLREQfEEEQEA 1355
Cdd:COG4913 600 SRYV-----LGfdnrAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE-REIAEL 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1356 KAELQRgMSKANSEVaqwrtkyetdaiqrtEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVE 1435
Cdd:COG4913 674 EAELER-LDASSDDL---------------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 288856329 1436 RANALA-----ANLDKK--QRNFDKVLAEWKQKYEEgqaELEGAQKEARSLSTELFKMKNSY 1490
Cdd:COG4913 738 AAEDLArlelrALLEERfaAALGDAVERELRENLEE---RIDALRARLNRAEEELERAMRAF 796
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1187-1918 |
2.50e-14 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 79.11 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1187 HEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEiksKND 1266
Cdd:pfam12128 228 RDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKE---KRD 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1267 EnLRQinDLSAQRARLQTENgefgrqlEEKEALVSQLTRGKQAftqQIEELKRQIEEEVKAKNALAHavQSARHDCdLLR 1346
Cdd:pfam12128 305 E-LNG--ELSAADAAVAKDR-------SELEALEDQHGAFLDA---DIETAAADQEQLPSWQSELEN--LEERLKA-LTG 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1347 EQFEEEQEAKAELQRGMSKANSEVAqwRTKYETDAIQRTEE--LEESKKKLAQRLQEAEEQIEAVNskcASLEKTKQRLQ 1424
Cdd:pfam12128 369 KHQDVTAKYNRRRSKIKEQNNRDIA--GIKDKLAKIREARDrqLAVAEDDLQALESELREQLEAGK---LEFNEEEYRLK 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1425 GEVEDLMIDVERANAlAANLDKKQRNFDKVLaewkqkyEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLETLKREN 1504
Cdd:pfam12128 444 SRLGELKLRLNQATA-TPELLLQLENFDERI-------ERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1505 KNLQQEISDLTEQLGETGKSIHELEKSkkavetekaeiqtaleEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEE 1584
Cdd:pfam12128 516 EERQSALDELELQLFPQAGTLLHFLRK----------------EAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELN 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1585 IEQIKRNSQRITDSMQSTLDSEVRSRNDALrikkkmegdlnEMEIQLSHANRQAAEaqKQLRNVQAQLKDAQLHLDDAVR 1664
Cdd:pfam12128 580 LYGVKLDLKRIDVPEWAASEEELRERLDKA-----------EEALQSAREKQAAAE--EQLVQANGELEKASREETFART 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1665 GQEDMKEQvamVERRNTLMQSeieELRAALEQTERGRKVAEQELvdaservgllhsqnTSLLNTKKKLEADLVQIQSEVE 1744
Cdd:pfam12128 647 ALKNARLD---LRRLFDEKQS---EKDKKNKALAERKDSANERL--------------NSLEAQLKQLDKKHQAWLEEQK 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1745 DTVQEARNAEDKAKKAItdaammaeelkkEQDTSAHLERMKKNLEVTVKDLQHRLDEAE-----NLAMKGGKKQ-LQKLE 1818
Cdd:pfam12128 707 EQKREARTEKQAYWQVV------------EGALDAQLALLKAAIAARRSGAKAELKALEtwykrDLASLGVDPDvIAKLK 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1819 SRVRELESEVEAEQRRGADavkgVRKYERRVKE--------LTYQTEEDKKNVNRLQDLVDKLQLKVKAYKRQ------- 1883
Cdd:pfam12128 775 REIRTLERKIERIAVRRQE----VLRYFDWYQEtwlqrrprLATQLSNIERAISELQQQLARLIADTKLRRAKlemerka 850
|
730 740 750
....*....|....*....|....*....|....*
gi 288856329 1884 SEEAEEQANSHLSKLRKVQHELEEAEERADIAESQ 1918
Cdd:pfam12128 851 SEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQ 885
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1145-1595 |
1.54e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 75.96 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1145 LEEISERLEEAGGATAAQIEMNKKreaEFQKLRRDLEESTLQHEATAAALRKKQadsvaELGEQIDNLQRVKQKLEKEKS 1224
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLK---ELKELEEELKEAEEKEEEYAELQEELE-----ELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1225 EYKMEIdDLSSNMEAVAKAKANLEkmcrTLEDQLSEIKSKndenLRQINDLSAQRARLQTENGEFGRQLEEKEALVSQLT 1304
Cdd:COG4717 120 KLEKLL-QLLPLYQELEALEAELA----ELPERLEELEER----LEELRELEEELEELEAELAELQEELEELLEQLSLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1305 RGK-QAFTQQIEELKRQIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKaELQRGMSKANSEVAQWRTKYETDAIQ 1383
Cdd:COG4717 191 EEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE-RLKEARLLLLIAAALLALLGLGGSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1384 RTEE------------LEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANALAANLDKKQRNF 1451
Cdd:COG4717 270 SLILtiagvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1452 DKVLAEWKQkyEEGQAELEGAQKEARSLsteLFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEK- 1530
Cdd:COG4717 350 QELLREAEE--LEEELQLEELEQEIAAL---LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEa 424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 288856329 1531 -SKKAVETEKAEIQTALEEAEGTLEHEESKILRVQLELNQVKS--EIDRKLAEKDEEIEQIKRNSQRI 1595
Cdd:COG4717 425 lDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEdgELAELLQELEELKAELRELAEEW 492
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
908-1628 |
1.66e-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: 75.91 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 908 EGLIKSKIQLEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAQ 987
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 988 DESIGKLTKEKkalqEAHQQTLDDLQaeedkvNTLTKSKTKLEQqvddlegsleqekkLRMDLERAKRKLEGDLKLAQES 1067
Cdd:pfam05483 168 AEKTKKYEYER----EETRQVYMDLN------NNIEKMILAFEE--------------LRVQAENARLEMHFKLKEDHEK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1068 IMDLEndkQQSEEKLKKKDFETSQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEE 1147
Cdd:pfam05483 224 IQHLE---EEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELED 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1148 ISERLEEAggataaqIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQADS---VAELGEQIDNLQRV----KQKLE 1220
Cdd:pfam05483 301 IKMSLQRS-------MSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHsfvVTEFEATTCSLEELlrteQQRLE 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1221 KEKSEYK---MEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDENlRQINDLsAQRARLQTENGEFGRQLEEK- 1296
Cdd:pfam05483 374 KNEDQLKiitMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEK-KQFEKI-AEELKGKEQELIFLLQAREKe 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1297 ----EALVSQLTRGKQAFTQQIEELKRQIEEEvKAKNALAHAvqsarhDCDLLREQFEEEQEAKAELQRGMSKANSEVAQ 1372
Cdd:pfam05483 452 ihdlEIQLTAIKTSEEHYLKEVEDLKTELEKE-KLKNIELTA------HCDKLLLENKELTQEASDMTLELKKHQEDIIN 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1373 WRtKYETDAIQRTEELEESKKKLAQRLQ----EAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANALAANLDKKQ 1448
Cdd:pfam05483 525 CK-KQEERMLKQIENLEEKEMNLRDELEsvreEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI 603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1449 RNfdkvlaewKQKYEEgqaELEGAQKEARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGETgKSIHEl 1528
Cdd:pfam05483 604 EN--------KNKNIE---ELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIED-KKISE- 670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1529 EKSKKAVETEKAEIQTALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEEIEQIKRNSQRiTDSMQSTLDSEVR 1608
Cdd:pfam05483 671 EKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQE-QSSAKAALEIELS 749
|
730 740
....*....|....*....|.
gi 288856329 1609 S-RNDALRIKKKMEGDLNEME 1628
Cdd:pfam05483 750 NiKAELLSLKKQLEIEKEEKE 770
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
895-1536 |
3.85e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.10 E-value: 3.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 895 SESENLSDAEERCEGLIKSKIQ-LEAKLKETTERLEDEEEINAELtAKKRKLEDECSELKKDIDDLELTLAKVEKEKHAT 973
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKeLEEVLREINEISSELPELREEL-EKLEKEVKELEELKEEIEELEKELESLEGSKRKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 974 ENKVKNLTEEMAAQDESIGKLTKEKKALQEahqqtlddLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEqekklrmdlera 1053
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKELKE--------LKEKAEEYIKLSEFYEEYLDELREIEKRLS------------ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1054 krKLEGDLKLAQESIMDLENDKQQSEEkLKKKDFETSQLLSKIEDEQSLGAQLQKKIKELQarieeleeeieaeraaraK 1133
Cdd:PRK03918 318 --RLEEEINGIEERIKELEEKEERLEE-LKKKLKELEKRLEELEERHELYEEAKAKKEELE------------------R 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1134 VEKQRADLsrELEEISERLEEAggataaqiemnKKREAEFQKLRRDLEESTLQHEATAAALRKkqadSVAELGEQIDNLQ 1213
Cdd:PRK03918 377 LKKRLTGL--TPEKLEKELEEL-----------EKAKEEIEEEISKITARIGELKKEIKELKK----AIEELKKAKGKCP 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1214 RVKQKLEKE-----KSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLEDQLseiksKNDENLRQINDLSAQRARLQTENGE 1288
Cdd:PRK03918 440 VCGRELTEEhrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVL-----KKESELIKLKELAEQLKELEEKLKK 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1289 FG-RQLEEKEALVSQLTRGKQAFTQQIEELKRQIEEEVKAKNALAhavqsarhdcdLLREQFEEEQEAKAELQRGMSkan 1367
Cdd:PRK03918 515 YNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLA-----------ELEKKLDELEEELAELLKELE--- 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1368 sevaqwrtkyetdaiqrtEELEESKKKLAQRLQEAE----EQIEAVNSkcaslEKTKQRLQGEVEDLMIDVERANALAAN 1443
Cdd:PRK03918 581 ------------------ELGFESVEELEERLKELEpfynEYLELKDA-----EKELEREEKELKKLEEELDKAFEELAE 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1444 LDKKQRNFDKVLAEWKQKYEEgqAELEGAQKEARSLSTELFKMKNSYEETLDQLETLKRenknlqqEISDLTEQLGETGK 1523
Cdd:PRK03918 638 TEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRREEIKK-------TLEKLKEELEEREK 708
|
650
....*....|...
gi 288856329 1524 SIHELEKSKKAVE 1536
Cdd:PRK03918 709 AKKELEKLEKALE 721
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1203-1708 |
4.99e-13 |
|
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: 74.39 E-value: 4.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1203 AELGEQIDNLQRVKQKLEKEKSEYKMEIDDLSS-------NMEAVAKAKANLEKMCRTLEDQLSEIKSKNDENlrqindl 1275
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEKkasalkrQLDRESDRNQELQKRIRLLEKREAEAEEALREQ------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1276 sAQRARLQTENGE-FGRQLEEKEALVSQLTRGKQAFTQQIEELKRQIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQE 1354
Cdd:pfam05557 75 -AELNRLKKKYLEaLNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1355 AKAELQRgmskansevaqwRTKYETDAIQRTEELEeskKKLAQRLQEAEEqIEAVNSKCAS---LEKTKQRLQGEVEDLM 1431
Cdd:pfam05557 154 LRQNLEK------------QQSSLAEAEQRIKELE---FEIQSQEQDSEI-VKNSKSELARipeLEKELERLREHNKHLN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1432 IDVERANALAANLDKKQRNFDKvlaewkqkYEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQL---ETLKRENKNLQ 1508
Cdd:pfam05557 218 ENIENKLLLKEEVEDLKRKLER--------EEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLrspEDLSRRIEQLQ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1509 QEISDLTEQLGETGKSIHELEKSKKAVETEKAEIQTALEEAEGTLEHEESKILRVQLELNQVKSEID--RKLAEKDEEIE 1586
Cdd:pfam05557 290 QREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDgyRAILESYDKEL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1587 QIKRNSQRITDSMQSTLDsevrsrndalrIKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKdaqlhlddAVRGQ 1666
Cdd:pfam05557 370 TMSNYSPQLLERIEEAED-----------MTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQ--------ALRQQ 430
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 288856329 1667 EDMKEQVAMVERRNTLMQsEIEELRAALEQTERGRKVAEQEL 1708
Cdd:pfam05557 431 ESLADPSYSKEEVDSLRR-KLETLELERQRLREQKNELEMEL 471
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1423-1929 |
5.00e-13 |
|
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: 74.83 E-value: 5.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1423 LQGEVEDLMIDVERANALAANLDKKQRNFDKVLAEWKQKYEEGQAELEgAQKEARSLSTELFKMKNSYEETLDQLET--- 1499
Cdd:pfam01576 7 MQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETE-LCAEAEEMRARLAARKQELEEILHELESrle 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1500 --------LKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAVETEKAEiqtaLEEAEGTLEHEESKILRVQLELNQVK 1571
Cdd:pfam01576 86 eeeersqqLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKK----LEEDILLLEDQNSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1572 SEIDRKLAEKDEE---IEQIKRNSQRITDSMQSTLDSEVRSRNDALRIKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNV 1648
Cdd:pfam01576 162 SEFTSNLAEEEEKaksLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1649 QAQLKDAQLHLDDAvrgqedmKEQVAMVERRNTLMQSEIEELRAALEQTERGRKVAEQElvdaservgllhsqntsllnt 1728
Cdd:pfam01576 242 EEELQAALARLEEE-------TAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQ--------------------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1729 KKKLEADLVQIQSEVEDTVQEARNAEDKAKKAITDAAMMAEELKKEQDT-SAHLERMKKNLEVTVKDLQHRLDEAENLAM 1807
Cdd:pfam01576 294 RRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRShEAQLQEMRQKHTQALEELTEQLEQAKRNKA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1808 kGGKKQLQKLESRVRELESEVEAEQRRGADAVKGVRKYERRVKELtyqteedkknvnrlqdlvdklQLKVKAYKRQSEEA 1887
Cdd:pfam01576 374 -NLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQEL---------------------QARLSESERQRAEL 431
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 288856329 1888 EEQANSHLSKLRKVQHELEEAEERADIAESQVNKLRAKSRDS 1929
Cdd:pfam01576 432 AEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT 473
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
845-1588 |
5.65e-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: 74.62 E-value: 5.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 845 AETEKELATMKEDFVKCKEDLAKAEAKKKELEEKMVALLQEKNDLQLAVA-------SESENLSDAEERCEGLIKSKIQL 917
Cdd:pfam02463 275 KEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKkaekelkKEKEEIEELEKELKELEIKREAE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 918 EAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDdlELTLAKVEKEKHATENKVKNLTEEMAAQDESIGKLTKE 997
Cdd:pfam02463 355 EEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE--EELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEIL 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 998 KKALqeaHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQ 1077
Cdd:pfam02463 433 EEEE---ESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGL 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1078 SEEKLKKKDFETSQLLSKIEDEQSLGAQLQKkiKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGG 1157
Cdd:pfam02463 510 KVLLALIKDGVGGRIISAHGRLGDLGVAVEN--YKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKL 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1158 ATAAQIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQ---IDNLQRVKQKLEKEKSEYKMEIDDLS 1234
Cdd:pfam02463 588 KLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKesaKAKESGLRKGVSLEEGLAEKSEVKAS 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1235 SNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDENLRQINDLSA--QRARLQTENGEFGRQLEEKEALVSQLTRGKQAFTQ 1312
Cdd:pfam02463 668 LSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEelKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDE 747
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1313 QIEELKRQIEEEVKAKNALAHAVQSARHDCDLLREQFEE--EQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEELEE 1390
Cdd:pfam02463 748 EEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLkvEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQE 827
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1391 SKKKLAQRLQEAEEQIEAVNSKCASLEKTKqrlqgevEDLMIDVERANALAANLDKKQRNFDKVLAEWKQKYEEGQAELE 1470
Cdd:pfam02463 828 EKIKEEELEELALELKEEQKLEKLAEEELE-------RLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKK 900
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1471 GAQKEARSLSTELFKMKNSYEETldqletlKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAVETEKAEIQTALEEAE 1550
Cdd:pfam02463 901 ELEEESQKLNLLEEKENEIEERI-------KEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELG 973
|
730 740 750
....*....|....*....|....*....|....*...
gi 288856329 1551 GTLEHEESKILRVQLELNQVKSEIDRKLAEKDEEIEQI 1588
Cdd:pfam02463 974 KVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAI 1011
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1397-1925 |
5.66e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.57 E-value: 5.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1397 QRLQEAEEQIEA---VNSKCASLEKTKQRLQG-EVEDLMIDVERANALAANLDKKQRNFDKVLAEWKQKYEEGQAELEGA 1472
Cdd:COG4913 242 EALEDAREQIELlepIRELAERYAAARERLAElEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1473 QKEARSLSTELfkmknsYEETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAVETEKAEIQTALEEAEGT 1552
Cdd:COG4913 322 REELDELEAQI------RGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1553 LEHEESKILRVQLELNQVKSEIDRKLAEKDEEIEQIKRNSQRITDSMQstldsEVRSR-NDALRIKkkmEGDL----NEM 1627
Cdd:COG4913 396 LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL-----ALRDAlAEALGLD---EAELpfvgELI 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1628 EIQLSHAN-RQAAEaqKQLRNV-------QAQLKDA-----QLHLDDAVRGQ---EDMKEQVAMVERRNTL---MQSEIE 1688
Cdd:COG4913 468 EVRPEEERwRGAIE--RVLGGFaltllvpPEHYAAAlrwvnRLHLRGRLVYErvrTGLPDPERPRLDPDSLagkLDFKPH 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1689 ELRAALEQTERGR----KVA-EQELVDASERV---GLLHSQNTSL-LNTKKKLEADLV-------QIQsEVEDTVQEARN 1752
Cdd:COG4913 546 PFRAWLEAELGRRfdyvCVDsPEELRRHPRAItraGQVKGNGTRHeKDDRRRIRSRYVlgfdnraKLA-ALEAELAELEE 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1753 AEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNlEVTVKDLQHRLDEAENlamkggkkQLQKLE---SRVRELESEVE 1829
Cdd:COG4913 625 ELAEAEERLEALEAELDALQERREALQRLAEYSWD-EIDVASAEREIAELEA--------ELERLDassDDLAALEEQLE 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1830 AEQRRGADAVKGVRKYERRVKELTYQTEEDKKNVNRLQDLVDKLQLKVKAYKRQSEEA----EEQANSHLSKLRKVQHEL 1905
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEErfaaALGDAVERELRENLEERI 775
|
570 580
....*....|....*....|
gi 288856329 1906 EEAEERADIAESQVNKLRAK 1925
Cdd:COG4913 776 DALRARLNRAEEELERAMRA 795
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1072-1924 |
7.99e-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: 74.24 E-value: 7.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1072 ENDKQQSEEKLKKKDFETSQLLSKIEDEQSLGAQLQKKIKELQARIEELEEeieaeRAARAKVEKQRADLSRELEEISER 1151
Cdd:pfam02463 145 EIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEEL-----KLQELKLKEQAKKALEYYQLKEKL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1152 LEEAGGATAAQIEmnkKREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEYKMEID 1231
Cdd:pfam02463 220 ELEEEYLLYLDYL---KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1232 DLSSNMEavakakaNLEKMCRTLEDQLSEIKSKNDENLRQINDLSAQRARLQTENGEFGRQLEEKEALVSQLTRGKQAFT 1311
Cdd:pfam02463 297 ELKSELL-------KLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1312 QQIEEL--------KRQIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQ 1383
Cdd:pfam02463 370 QLEEELlakkklesERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEE 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1384 RTEELEESKKKLAQRLQEAEEQIEAvnskcASLEKTKQRLQGEVEDLMIDVERANAL---AANLDKKQRNFDKVLAEWKQ 1460
Cdd:pfam02463 450 KEELEKQELKLLKDELELKKSEDLL-----KETQLVKLQEQLELLLSRQKLEERSQKeskARSGLKVLLALIKDGVGGRI 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1461 KYEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAVETEKA 1540
Cdd:pfam02463 525 ISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILN 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1541 EIQTALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEEIEQIKRNSQRITDSMQSTLDSEVRSRNDALRIKKKM 1620
Cdd:pfam02463 605 LAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1621 EGDLNEMEIQLSHANRQAAEAQKQLRNVQaQLKDAQLHLDDAVRGQEDMKEQVAMVERRNTLMQSEIEELRAALEQTERG 1700
Cdd:pfam02463 685 AESELAKEEILRRQLEIKKKEQREKEELK-KLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKE 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1701 RKVAEQELVDASERVGLLHsqntsllNTKKKLEADLVQIQSEVEDTVQEARnaEDKAKKAITDAAMMAEELKKEQDTSAH 1780
Cdd:pfam02463 764 EEKSELSLKEKELAEEREK-------TEKLKVEEEKEEKLKAQEEELRALE--EELKEEAELLEEEQLLIEQEEKIKEEE 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1781 LERMKKNLEVTVKDLQHRLDEAENLAMKGGKKQLQKLESRVRELESEVEAEQRRGADAVKGVRKYERRVKELTY---QTE 1857
Cdd:pfam02463 835 LEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKlnlLEE 914
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 288856329 1858 EDKKNVNRLQDLVDKLQLKVKAYKRQSEEAEEQANSHLSKLRKVQHELEEAEERADIAESQVNKLRA 1924
Cdd:pfam02463 915 KENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIE 981
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1262-1921 |
1.41e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.64 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1262 KSKNDENLRQINDLSAQRARLQTENGEFGRQLEEKEALVSQLTRGKQAftQQIEELkRQIEEEVKAKNALAHAVQSARHD 1341
Cdd:PTZ00121 1086 DNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEA--RKAEDA-RKAEEARKAEDAKRVEIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1342 CDLLREQFEEEQEAKAELQRGMSKANsEVAQWRTKYETDAIQRTEELEESKKKLAQRLQEAEEQIEAVnsKCASLEKTKQ 1421
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKAEAARKAEEVR-KAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAV--KKAEEAKKDA 1239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1422 RLQGEVEDLMIDVERANALAANLDKKQRNFDKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMknsyeETLDQLETLK 1501
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKA-----DEAKKKAEEA 1314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1502 RENKNLQQEISDLTEQLGETGKsihELEKSKKAVETEKAEIQTALEEAEGTLEHEESKILRVQLElnQVKSEIDRKLAEK 1581
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKK---KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA--KKKADAAKKKAEE 1389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1582 DEEIEQIKRNSQRitdsmqstldsevrSRNDALRIKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDD 1661
Cdd:PTZ00121 1390 KKKADEAKKKAEE--------------DKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1662 AVRGQEDMKEqvAMVERRNTLMQSEIEELRAALE---QTERGRKVAEQELVDASERvgllhsqntsllntKKKLEADlvq 1738
Cdd:PTZ00121 1456 AKKAEEAKKK--AEEAKKADEAKKKAEEAKKADEakkKAEEAKKKADEAKKAAEAK--------------KKADEAK--- 1516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1739 iQSEVEDTVQEARNAEDKAKkaiTDAAMMAEELKKEQDTSaHLERMKKNLEVTVKDLQHRLDEAENLAMKGGKKQLQKLE 1818
Cdd:PTZ00121 1517 -KAEEAKKADEAKKAEEAKK---ADEAKKAEEKKKADELK-KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE 1591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1819 SRVREL-------------ESEVEAEQRRGADAVKGVRKYERRVKELTYQTEEDKKNVNRL-----QDLVDKLQLKVKAY 1880
Cdd:PTZ00121 1592 ARIEEVmklyeeekkmkaeEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELkkaeeENKIKAAEEAKKAE 1671
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 288856329 1881 --KRQSEE---AEEQANSHLSKLRKVQHELEEAEERADIAESQVNK 1921
Cdd:PTZ00121 1672 edKKKAEEakkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK 1717
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1247-1711 |
1.61e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.49 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1247 LEKMCRTLEDQLSEIKSKNDE-NLRQINDLSAQRARLQTENGEFGRQLEEKEALVSQLTRGKQaftqQIEELKRQIEEEV 1325
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPElNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA----ELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1326 KAKNALAHAVQSARHDCDLLR-----EQFEEEQEAKAELQRGMSKANSEVAQWRTkyetdaiQRTEELEESKKKLAQRLQ 1400
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAElperlEELEERLEELRELEEELEELEAELAELQE-------ELEELLEQLSLATEEELQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1401 EAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANALAANLDKKQRNFDkvlAEWKQKYEEGQAELEGAQKEARSLS 1480
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE---ARLLLLIAAALLALLGLGGSLLSLI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1481 ------------------TELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLG-ETGKSIHELEKSKKAVEtEKAE 1541
Cdd:COG4717 273 ltiagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIE-ELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1542 IQTALEEAEGTLEHEESKILRVQLeLNQVKSEIDRKLAEKDEEIEQIKRNSQRItDSMQSTLDSEVRSRNDALRikkkmE 1621
Cdd:COG4717 352 LLREAEELEEELQLEELEQEIAAL-LAEAGVEDEEELRAALEQAEEYQELKEEL-EELEEQLEELLGELEELLE-----A 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1622 GDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQE--DMKEQVAMVERRNTLMQSEIEELRAALEQTER 1699
Cdd:COG4717 425 LDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALELLEE 504
|
490
....*....|..
gi 288856329 1700 GRKVAEQELVDA 1711
Cdd:COG4717 505 AREEYREERLPP 516
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1198-1415 |
1.70e-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: 71.33 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1198 QADSVAELGEQIDNLQRVKQKLEKEKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDENLRQINDLSA 1277
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1278 QRARLQTENGEF-------GRQLEEKEAL----VSQLTRGKQAFTQQIEELKRQIEEEVKAKNALAHAVQSARHDCDLLR 1346
Cdd:COG4942 98 ELEAQKEELAELlralyrlGRQPPLALLLspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 288856329 1347 EQFEEEQEAKAELQRGMSKANSEVAQWRTKYETDAiQRTEELEESKKKLAQRLQEAEEQIEAVNSKCAS 1415
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
897-1424 |
2.39e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.40 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 897 SENLSDAEERCEGLIKSKIQLEA---KLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHAT 973
Cdd:PRK03918 213 SSELPELREELEKLEKEVKELEElkeEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 974 ENKVKnLTEEMAAQDESIGKLTKEKKALQE---AHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEKKLRMDL 1050
Cdd:PRK03918 293 EEYIK-LSEFYEEYLDELREIEKRLSRLEEeinGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKK 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1051 ERAKRKLEgdlKLAQESIMDLENDKQQSEEKLKKKDFETSQLLSKIEDEQSLGAQLQKKIKELQARIEE-----LEEEIE 1125
Cdd:PRK03918 372 EELERLKK---RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1126 AERAARAKVEKQRADLSRELEEISERLEEAgGATAAQIEMNKKREAEFQKLRRDLEestlQHEATAAALRKKQADSVAEL 1205
Cdd:PRK03918 449 HRKELLEEYTAELKRIEKELKEIEEKERKL-RKELRELEKVLKKESELIKLKELAE----QLKELEEKLKKYNLEELEKK 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1206 GEQIDNLQRVKQKLEKEKSEYKMEIDDLssnmEAVAKAKANLEKMCRTLEDQLSEIKSKNDE-NLRQINDLSAQRARLQT 1284
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKELEKL----EELKKKLAELEKKLDELEEELAELLKELEElGFESVEELEERLKELEP 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1285 ENGEFGRQLEEKEALVSQLTRgkqaftqqIEELKRQIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAElqRGMS 1364
Cdd:PRK03918 600 FYNEYLELKDAEKELEREEKE--------LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR--EEYL 669
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1365 KANSEVAQWRTKYEtdaiqRTEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQ 1424
Cdd:PRK03918 670 ELSRELAGLRAELE-----ELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
837-1517 |
6.66e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 71.33 E-value: 6.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 837 KIKPLLKSAETEKELATMKEDFVKCKEDLAKAEakkkeleekmvallqekndlqlavasesenlsdaeercegliKSKIQ 916
Cdd:PTZ00121 1330 KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA------------------------------------------EEKAE 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 917 LEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLEltlAKVEKEKHATENKVKnlTEEMAAQDEsIGKLTK 996
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELK---KAAAAKKKADEAKKK--AEEKKKADE-AKKKAE 1441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 997 EKKALQEAHQqtlddlQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEKKlrmdLERAKRKLEGDLKLAQEsIMDLENDKQ 1076
Cdd:PTZ00121 1442 EAKKADEAKK------KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK----ADEAKKKAEEAKKKADE-AKKAAEAKK 1510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1077 QSEEKLKKKDFETSQLLSKIED----EQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERL 1152
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEakkaDEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE 1590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1153 EEAGGATAAQIEMNKKREAEfqKLRRDLEESTLQHEATAAALRKKQadsVAELGEQIDNLQRVKQKLEKEKSEYKMEIDD 1232
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAE--EAKKAEEAKIKAEELKKAEEEKKK---VEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1233 LSSNMEAvAKAKANLEKMCRTLEDQLSEIKSKNDENLRQINDLSAQRARLQTENGEFGRQLEEKEALVSQLTRGKQAFTQ 1312
Cdd:PTZ00121 1666 EAKKAEE-DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK 1744
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1313 QIEELKRQIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGM-------SKANSEVAQWRTKYETDAIQRT 1385
Cdd:PTZ00121 1745 KAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEvdkkikdIFDNFANIIEGGKEGNLVINDS 1824
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1386 EELEESKKKlaqrlqeaeeqiEAVNSKCASLEKTKQRLQGEVEDLMIDVERANAlAANLDKKQRNFDKVLAEWKQKYEEG 1465
Cdd:PTZ00121 1825 KEMEDSAIK------------EVADSKNMQLEEADAFEKHKFNKNNENGEDGNK-EADFNKEKDLKEDDEEEIEEADEIE 1891
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 288856329 1466 QAELEGAQKEarsLSTELFKMKN--SYEETLDQLETLKRENKNLQQEISDLTEQ 1517
Cdd:PTZ00121 1892 KIDKDDIERE---IPNNNMAGKNndIIDDKLDKDEYIKRDAEETREEIIKISKK 1942
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
33-78 |
1.39e-11 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 60.91 E-value: 1.39e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 288856329 33 DAKTACYVVDDKELYVKGTIKSKDGGKVTVITlDTKEEKVVKEDDV 78
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
894-1268 |
1.43e-11 |
|
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: 70.10 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 894 ASESENLSDAEERCEGLIKSKIQLEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHAT 973
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 974 ENKVKNLTEEMAAQDESIGKLTKEKKALQEAhqqtLDDLQAEED--KVNTLTKSKTKLEQQVDDLEGSLEqekklrmDLE 1051
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEELEEDLHKLEEA----LNDLEARLShsRIPEIQAELSKLEEEVSRIEARLR-------EIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1052 RAKRKLEGDLKLAQESIMDLENDKQQSEEKLKKKDFETSQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAAR 1131
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1132 AKVEKQRADLSRELEEISERLEEAGGATAA------QIEMNKKREAEFQKLRRDLEESTLQHEATAAALRK------KQA 1199
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRLSELKAKLEAleeelsEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAlepvnmLAI 978
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 288856329 1200 DSVAELGEQIDNLQRVKQKLEKEKSEYKMEIDDL-----SSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDEN 1268
Cdd:TIGR02169 979 QEYEEVLKRLDELKEKRAKLEEERKAILERIEEYekkkrEVFMEAFEAINENFNEIFAELSGGTGELILENPDD 1052
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
933-1438 |
1.73e-11 |
|
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: 69.76 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 933 EINAELTAKKRKLEDECSELKKD--IDDLELTLAKVEKEKHATENkvKNLTEEMAAQDESIGKLTKEKKALQEAHQQTLD 1010
Cdd:pfam15921 328 QLRSELREAKRMYEDKIEELEKQlvLANSELTEARTERDQFSQES--GNLDDQLQKLLADLHKREKELSLEKEQNKRLWD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1011 dlqaeEDKVNTLTKSktKLEQQVDDLEGSLEQEKKLrmdLERAKRKLEGDLKLAQESImdlendkQQSEEKLKKKDFETS 1090
Cdd:pfam15921 406 -----RDTGNSITID--HLRRELDDRNMEVQRLEAL---LKAMKSECQGQMERQMAAI-------QGKNESLEKVSSLTA 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1091 QLLSKIEdeqslgaQLQKKIKELQARIEELEEEieaeraarakvEKQRADLSRELEEISERLEeaggATAAQIEMNKKRE 1170
Cdd:pfam15921 469 QLESTKE-------MLRKVVEELTAKKMTLESS-----------ERTVSDLTASLQEKERAIE----ATNAEITKLRSRV 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1171 ----AEFQKLRRDLEE-STLQHEATAAALRKKQADSVAE-LGEQIDNLQ-------RVKQKLEKEKSEYKMEIDDLSSNM 1237
Cdd:pfam15921 527 dlklQELQHLKNEGDHlRNVQTECEALKLQMAEKDKVIEiLRQQIENMTqlvgqhgRTAGAMQVEKAQLEKEINDRRLEL 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1238 EAVAKAKANLEKMCRTLEDQLSEIK-------SKNDENLRQINDLSAQRARL----QTENGEFGRQLEEKEALVSQLTRG 1306
Cdd:pfam15921 607 QEFKILKDKKDAKIRELEARVSDLElekvklvNAGSERLRAVKDIKQERDQLlnevKTSRNELNSLSEDYEVLKRNFRNK 686
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1307 KQAFTQQIEELKRQIE----EEVKAKNALAHAVQSARHdcdLLREQFEEEQEAKAelQRGMSKANSEVAQWRTKYETDAI 1382
Cdd:pfam15921 687 SEEMETTTNKLKMQLKsaqsELEQTRNTLKSMEGSDGH---AMKVAMGMQKQITA--KRGQIDALQSKIQFLEEAMTNAN 761
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 288856329 1383 QRTEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERAN 1438
Cdd:pfam15921 762 KEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKAS 817
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
884-1285 |
2.71e-11 |
|
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: 68.89 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 884 QEKNDLQLAVASESENLSDAEERcegLIKSKIQLEAKLKEtterLEDEEEINAELTAKKRKLEDECSELKKD-----IDD 958
Cdd:TIGR04523 239 QEINEKTTEISNTQTQLNQLKDE---QNKIKKQLSEKQKE----LEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwNKE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 959 LELTLAKVEKEKHATENKVKNLTEEMAAQDESIGKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTK-------SKTKLEQ 1031
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKenqsykqEIKNLES 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1032 QVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSEEKLKKKDFETSQLLSKIEDEQSLGAQLQKKIK 1111
Cdd:TIGR04523 392 QINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLK 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1112 ELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQIEMNKKREAEfqKLRRDLEESTLQHEATA 1191
Cdd:TIGR04523 472 VLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE--KKEKESKISDLEDELNK 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1192 AALRKKQA---DSVAELGEQIDNLQRVKQKLEKEKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDEN 1268
Cdd:TIGR04523 550 DDFELKKEnleKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKL 629
|
410
....*....|....*..
gi 288856329 1269 LRQINDLSAQRARLQTE 1285
Cdd:TIGR04523 630 SSIIKNIKSKKNKLKQE 646
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1147-1907 |
2.85e-11 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 68.92 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1147 EISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEEstLQHEATaaalrkkqadSVAELGEQIDNLQRVKQKLEKEKSEY 1226
Cdd:TIGR00606 221 EIRDQITSKEAQLESSREIVKSYENELDPLKNRLKE--IEHNLS----------KIMKLDNEIKALKSRKKQMEKDNSEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1227 KMEIDD-LSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDENLRQINDLSAQRARLQTENGEFGRQLE--EKEALVSQL 1303
Cdd:TIGR00606 289 ELKMEKvFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADrhQEHIRARDS 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1304 TRGKQAFTQQIEELKRQIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQ 1383
Cdd:TIGR00606 369 LIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEI 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1384 RTEELEESKKKLAQrLQEAEEQIEAVNSKCASLEKTKQRL-----QGEVEDLMIDVERANALAANLDKKQRNFDKVLAEw 1458
Cdd:TIGR00606 449 LEKKQEELKFVIKE-LQQLEGSSDRILELDQELRKAERELskaekNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQ- 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1459 KQKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAVETE 1538
Cdd:TIGR00606 527 LNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQN 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1539 KAEIQTALEEAEGTLEHEESKILRV-QLELNQVKSEIDRKLAEKDEEIEQIKRNSQRITDSMQSTLDSEVRSRNDALRIK 1617
Cdd:TIGR00606 607 KNHINNELESKEEQLSSYEDKLFDVcGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRV 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1618 KKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQE---DMKE-QVAMVERRNTLMQSEIEELRAA 1693
Cdd:TIGR00606 687 FQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQsiiDLKEkEIPELRNKLQKVNRDIQRLKND 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1694 LEQTER--GRKVAEQELV-DASERVGLLHSQNTSLLNTKKKLEADLVQIQS-EVEDTVQEARNAEDKAKKAITDAAMMAE 1769
Cdd:TIGR00606 767 IEEQETllGTIMPEEESAkVCLTDVTIMERFQMELKDVERKIAQQAAKLQGsDLDRTVQQVNQEKQEKQHELDTVVSKIE 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1770 ELKKeqdTSAHLERMKKNLEVTVKDLQ-HRLDEAENLAMKGG-KKQLQKLESRVRELESEVEAEQRRGADAVKGVRKYER 1847
Cdd:TIGR00606 847 LNRK---LIQDQQEQIQHLKSKTNELKsEKLQIGTNLQRRQQfEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQ 923
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 288856329 1848 RVKELTYQTEEDKKNVN---------------RLQDLVDKLQLKVKAYKRQSEEAEEQANSHLSKLRKVQHELEE 1907
Cdd:TIGR00606 924 EKEELISSKETSNKKAQdkvndikekvknihgYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINE 998
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
916-1353 |
2.94e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.64 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 916 QLEAKLKEtterLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEK--HATENKVKNLTEEMAAQDESIGK 993
Cdd:COG4717 75 ELEEELKE----AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqlLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 994 LTKEKKALQEAHQQtLDDLQAEedkvntLTKSKTKLEQQVDDLegSLEQEKKLRmDLERAKRKLEGDLKLAQESIMDLEN 1073
Cdd:COG4717 151 LEERLEELRELEEE-LEELEAE------LAELQEELEELLEQL--SLATEEELQ-DLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1074 DKQQSEEKLK--KKDFETSQLLSKIEDEQSLGA--------------------------------------QLQKKIKEL 1113
Cdd:COG4717 221 ELEELEEELEqlENELEAAALEERLKEARLLLLiaaallallglggsllsliltiagvlflvlgllallflLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1114 QARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEESTLQheataAA 1193
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA-----AL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1194 LRKKQADSVAELGEQIDNLQRvKQKLEKEKSEYKMEIDDLSSNMEAVAkAKANLEkmcrTLEDQLSEIKSKNDENLRQIN 1273
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELL-EALDEE----ELEEELEELEEELEELEEELE 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1274 DLSAQRARLQTENgefgRQLEEKEALVSQLtrgkqaftQQIEELKRQIEEEVKAKNALAHAVQSARHdcdlLREQFEEEQ 1353
Cdd:COG4717 450 ELREELAELEAEL----EQLEEDGELAELL--------QELEELKAELRELAEEWAALKLALELLEE----AREEYREER 513
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1390-1601 |
3.08e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 67.48 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1390 ESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANALAANLDKKQRNFDKVLAEWKQKYEEGQAEL 1469
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1470 EGAQKEARSLSTELFKMKN-----------SYEETLDQLETLKRENKNLQQEISDLTEQLgetgksiHELEKSKKAVETE 1538
Cdd:COG4942 100 EAQKEELAELLRALYRLGRqpplalllspeDFLDAVRRLQYLKYLAPARREQAEELRADL-------AELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 288856329 1539 KAEIQTALEEaegtLEHEESKILRVQLELNQVKSEIDRKLAEKDEEIEQIKRNSQRITDSMQS 1601
Cdd:COG4942 173 RAELEALLAE----LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1490-1920 |
3.94e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.40 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1490 YEETLDQLETLKRENKNLQQeISDLTEQLGETGKSIHELEKSKKAVETEKAeiQTALEEAEGTLEHEESKILRVQLELNQ 1569
Cdd:COG4913 237 LERAHEALEDAREQIELLEP-IRELAERYAAARERLAELEYLRAALRLWFA--QRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1570 VKSEIDRKLAEKDEEIEQIKRNSQRITDSMQSTLDSEVRSRNDALRIKKKMEGDLNEMEIQLSHA----NRQAAEAQKQL 1645
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASaeefAALRAEAAALL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1646 RNVQAQLKDAQLHLDDAVRGQEDMKEQ-------VAMVERRNTLMQSEIEELRAALEQtERGRKVAE----QELVD---- 1710
Cdd:COG4913 394 EALEEELEALEEALAEAEAALRDLRRElreleaeIASLERRKSNIPARLLALRDALAE-ALGLDEAElpfvGELIEvrpe 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1711 ------ASERVglLHSQNTSLLNTkkklEADLVQIQSEVEDT-------VQEARNAEDKAKKAITDAAMMAEELKKEQ-- 1775
Cdd:COG4913 473 eerwrgAIERV--LGGFALTLLVP----PEHYAAALRWVNRLhlrgrlvYERVRTGLPDPERPRLDPDSLAGKLDFKPhp 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1776 ------------------DTSAHLER----------MKKNLEVTVKDLQHRLDE--------AENLAMKggKKQLQKLES 1819
Cdd:COG4913 547 frawleaelgrrfdyvcvDSPEELRRhpraitragqVKGNGTRHEKDDRRRIRSryvlgfdnRAKLAAL--EAELAELEE 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1820 RVRELESEVEA---------EQRRGADAVKGVRKYERRVKELTY---QTEEDKKNVNRLQDLVDKLQLKVKAYKRQSEEA 1887
Cdd:COG4913 625 ELAEAEERLEAleaeldalqERREALQRLAEYSWDEIDVASAEReiaELEAELERLDASSDDLAALEEQLEELEAELEEL 704
|
490 500 510
....*....|....*....|....*....|...
gi 288856329 1888 EEQANSHLSKLRKVQHELEEAEERADIAESQVN 1920
Cdd:COG4913 705 EEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1527-1935 |
6.46e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 68.24 E-value: 6.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1527 ELEKSKKAVETEkaeiqtALEEAEGTLEhEESKILRVQLElNQVKSEIDRKLAEKDEEIEQIKR--NSQRITDSMQSTLD 1604
Cdd:PTZ00121 1080 DFDAKEDNRADE------ATEEAFGKAE-EAKKTETGKAE-EARKAEEAKKKAEDARKAEEARKaeDARKAEEARKAEDA 1151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1605 SEV---RSRNDALRIK--------KKMEGDLNEMEIQLSHANRQAAEAqkqlRNVQAQLKDAQLHLDDAVRGQEDMKEQV 1673
Cdd:PTZ00121 1152 KRVeiaRKAEDARKAEearkaedaKKAEAARKAEEVRKAEELRKAEDA----RKAEAARKAEEERKAEEARKAEDAKKAE 1227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1674 AMverrntlmqSEIEELRAALEQTERGRKVAEQELVDASERVGLLH-SQNTSLLNTKKKLEADLVQIQSEVEDTvQEARN 1752
Cdd:PTZ00121 1228 AV---------KKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHfARRQAAIKAEEARKADELKKAEEKKKA-DEAKK 1297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1753 AEDKAKkaITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQH--RLDEAENLAMKGGKKQLQKLESRVRELESEVEa 1830
Cdd:PTZ00121 1298 AEEKKK--ADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEakKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE- 1374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1831 EQRRGADAVKGVRKYERRVKELTYQTEEDKKNVNRLQdlvdklqlKVKAYKRQSEEAEEQANS--HLSKLRKVQHELEEA 1908
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELK--------KAAAAKKKADEAKKKAEEkkKADEAKKKAEEAKKA 1446
|
410 420
....*....|....*....|....*....
gi 288856329 1909 EERADIAES--QVNKLRAKSRDSGKGKDA 1935
Cdd:PTZ00121 1447 DEAKKKAEEakKAEEAKKKAEEAKKADEA 1475
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1213-1892 |
7.40e-11 |
|
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: 67.35 E-value: 7.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1213 QRVKQKLEKEKSEYK---MEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDENLRQINDLSAQRARLqteNGEF 1289
Cdd:TIGR04523 36 KQLEKKLKTIKNELKnkeKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKI---NSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1290 GRQLEEKEALVSQLTRGKQaftqQIEELKRQIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSE 1369
Cdd:TIGR04523 113 KNDKEQKNKLEVELNKLEK----QKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1370 VAQWRTKYetdaiQRTEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANALAANLDKKQR 1449
Cdd:TIGR04523 189 IDKIKNKL-----LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1450 NFDKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEEtlDQLETLKRENKNLQQEISDLTEQLGETGKSIHELE 1529
Cdd:TIGR04523 264 KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ--DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1530 KSKKAVETEKAEiqtaleeaegtleheeskilrvqleLNQVKSEIDRKLAEKDEEIEQIKRNSQRITDSMQStLDSEVRS 1609
Cdd:TIGR04523 342 EQISQLKKELTN-------------------------SESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN-LESQIND 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1610 RNDALRIKKKMEgdlNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAMVERRNTLMQSEIEE 1689
Cdd:TIGR04523 396 LESKIQNQEKLN---QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1690 LRAALEQTERGRKVAEQELVDASERVGLLHSQNTSLLNTKKKLEADLVQIQSEVEDTVQEARNAEDKAKKAITDAAMMAE 1769
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1770 ELKKEqdtsahlermkkNLEVTVKDLQHRLDEaenlaMKGGKKQLQKLESRVRELESEVEAEQRrgaDAVKGVRKYERRV 1849
Cdd:TIGR04523 553 ELKKE------------NLEKEIDEKNKEIEE-----LKQTQKSLKKKQEEKQELIDQKEKEKK---DLIKEIEEKEKKI 612
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 288856329 1850 KELTYQTEEDKKNVNRLQDLVDKLQLKVKAYKRQSEEAEEQAN 1892
Cdd:TIGR04523 613 SSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIK 655
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
843-1426 |
1.14e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.99 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 843 KSAETEKELATMKEDFVKCKEDLAKAEAKKKELEEKMVALLQEKNDLqlavaseSENLSDAEERCEGLikskiqleakLK 922
Cdd:PRK02224 231 QARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREEL-------AEEVRDLRERLEEL----------EE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 923 ETTERLEDEEEINAELTAkkrkLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAQDESIGKLTKEKKALQ 1002
Cdd:PRK02224 294 ERDDLLAEAGLDDADAEA----VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1003 EAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSEEKL 1082
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1083 KK-------KDFETSQLLSKIEDEqslgaqlQKKIKELqarieeleeeieaeraarakvEKQRADLSRELEEISERLEEA 1155
Cdd:PRK02224 450 EAgkcpecgQPVEGSPHVETIEED-------RERVEEL---------------------EAELEDLEEEVEEVEERLERA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1156 GGATAAQIEMNKKREAefqklRRDLEESTLQHEATAAALRKKQA---DSVAELGEQIDNLQRVKQKLEKEKSEYKMEIDD 1232
Cdd:PRK02224 502 EDLVEAEDRIERLEER-----REDLEELIAERRETIEEKRERAEelrERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1233 LSSNMEAVAKAKANLEKmcrtLEDQLSEIksknDENLRQINDLSAQRARLQTENGEFGRQLEEKealvsqltrgkqaftq 1312
Cdd:PRK02224 577 LNSKLAELKERIESLER----IRTLLAAI----ADAEDEIERLREKREALAELNDERRERLAEK---------------- 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1313 qiEELKRQIEEEVKAKnalahAVQSARHDcdllREQFEEEQEAKAELQRGMSKANSEVaQWRTKYETDAIQRTEELEESK 1392
Cdd:PRK02224 633 --RERKRELEAEFDEA-----RIEEARED----KERAEEYLEQVEEKLDELREERDDL-QAEIGAVENELEELEELRERR 700
|
570 580 590
....*....|....*....|....*....|....
gi 288856329 1393 KKLAQRLqeaeEQIEAVNSKCASLEKTKQRLQGE 1426
Cdd:PRK02224 701 EALENRV----EALEALYDEAEELESMYGDLRAE 730
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
892-1649 |
2.05e-10 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 66.40 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 892 AVASESENLSDAEERCEGLIKSKIQLEAKLKETTERLEDEEEINAELTAKKRkledecSELKKDIDDLELTLAKVEKEKH 971
Cdd:pfam12128 238 KIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELN------QLLRTLDDQWKEKRDELNGELS 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 972 ATENKVKNLTEEMAAQDESIGKLTKEKKALQEAHQQTLDDLQAE-----------EDKVNTLTKSKTKL-----EQQVDD 1035
Cdd:pfam12128 312 AADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSElenleerlkalTGKHQDVTAKYNRRrskikEQNNRD 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1036 LEGSLEQEKKLRMDLERAKRKLEGDLKlAQESIMDLENDKQQSEEKLKKKDFETSQLLSKI--------EDEQSLGAQLQ 1107
Cdd:pfam12128 392 IAGIKDKLAKIREARDRQLAVAEDDLQ-ALESELREQLEAGKLEFNEEEYRLKSRLGELKLrlnqatatPELLLQLENFD 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1108 KKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQIEMNKKREAEFQKLRR----DLEES 1183
Cdd:pfam12128 471 ERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRkeapDWEQS 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1184 TLQHEATAAALR-----------KKQADSVAELG---EQID------NLQRVKQKLEKEKSEYKMEIDDLSSNMEAVAKA 1243
Cdd:pfam12128 551 IGKVISPELLHRtdldpevwdgsVGGELNLYGVKldlKRIDvpewaaSEEELRERLDKAEEALQSAREKQAAAEEQLVQA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1244 KANLEKMCRTLEDQLSEIKSkNDENLRQINDLSAQRAR-----LQTENGEFGRQLEEKEALVSQLTRGKQAFTQQIeelK 1318
Cdd:pfam12128 631 NGELEKASREETFARTALKN-ARLDLRRLFDEKQSEKDkknkaLAERKDSANERLNSLEAQLKQLDKKHQAWLEEQ---K 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1319 RQIEEEVKAKNALAHAVQSARHD-CDLLREQFEEEQE-AKAELQRGMSKANSEVAQWRTKYETDAIQRTE--ELEESKKK 1394
Cdd:pfam12128 707 EQKREARTEKQAYWQVVEGALDAqLALLKAAIAARRSgAKAELKALETWYKRDLASLGVDPDVIAKLKREirTLERKIER 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1395 LAQRLQEAEE-----------QIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANA--------------LAANLDKKQR 1449
Cdd:pfam12128 787 IAVRRQEVLRyfdwyqetwlqRRPRLATQLSNIERAISELQQQLARLIADTKLRRAklemerkasekqqvRLSENLRGLR 866
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1450 NFDKVLAEWKQKYEEGQAELEGAQKEArslSTELFKMKNSYEEtldqlETLKRENKNLQQEISDLT-EQLGETGKSIHEL 1528
Cdd:pfam12128 867 CEMSKLATLKEDANSEQAQGSIGERLA---QLEDLKLKRDYLS-----ESVKKYVEHFKNVIADHSgSGLAETWESLREE 938
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1529 EKS---KKAVETEKAEIQTALEEAEGTLEHEESKILRVQLELN-QVKSEIDRKLAEKDEEIEQIkrnSQRITDSMQSTLD 1604
Cdd:pfam12128 939 DHYqndKGIRLLDYRKLVPYLEQWFDVRVPQSIMVLREQVSILgVDLTEFYDVLADFDRRIASF---SRELQREVGEEAF 1015
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 288856329 1605 SEvRSRNDALRIKKKMEgdlnemEIQLSHANRQAAEAQKQLRNVQ 1649
Cdd:pfam12128 1016 FE-GVSESAVRIRSKVS------ELEYWPELRVFVKAFRLWKSDG 1053
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1076-1565 |
3.38e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1076 QQSEEKLKKKDFETSQLLSKIEDEQSLGAQ---LQKKIKELQARIEELEEEIEAERaarakVEKQRADLSRELEEISERL 1152
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEEleeLEAELEELREELEKLEKLLQLLP-----LYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1153 EEAggataaqiemnKKREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEYKMEIDD 1232
Cdd:COG4717 149 EEL-----------EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1233 LSSNMEAVAKAKANLEKmcrtlEDQLSEIKSKNDENLRQINDLSAQRARLQTENGEFGRQLEEKEALVSQLtrgkQAFTQ 1312
Cdd:COG4717 218 AQEELEELEEELEQLEN-----ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVL----GLLAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1313 QIEELKRQieeevkaknalahavqsarhdcdllREQFEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEELEESK 1392
Cdd:COG4717 289 LFLLLARE-------------------------KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1393 KKLAQrLQEAEEQIEAVNS--KCASLEKTKQRLQGEVedlmiDVERANALAANLDKKQRnfdkvLAEWKQKYEEGQAELE 1470
Cdd:COG4717 344 DRIEE-LQELLREAEELEEelQLEELEQEIAALLAEA-----GVEDEEELRAALEQAEE-----YQELKEELEELEEQLE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1471 GAQKEARSLSTELfkmknSYEETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEKSkkaveTEKAEIQTALEEAE 1550
Cdd:COG4717 413 ELLGELEELLEAL-----DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED-----GELAELLQELEELK 482
|
490
....*....|....*
gi 288856329 1551 GTLEHEESKILRVQL 1565
Cdd:COG4717 483 AELRELAEEWAALKL 497
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
843-1416 |
6.02e-10 |
|
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: 64.81 E-value: 6.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 843 KSAETEKELATMKEDFVKCKEDLAKAEAKKKELEEKMVALLQEKNDLQLAVASESENLSDAEERCEGLIKSKIQLEAKLK 922
Cdd:pfam01576 455 KNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 923 ETTERLEDEEEIN--------------AELTAKKRKLEDECSELKKDIDDLELTLA------------------------ 964
Cdd:pfam01576 535 EDAGTLEALEEGKkrlqrelealtqqlEEKAAAYDKLEKTKNRLQQELDDLLVDLDhqrqlvsnlekkqkkfdqmlaeek 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 965 -----------KVEKEKHATENKVKNLTEEMAAQDESIGKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQV 1033
Cdd:pfam01576 615 aisaryaeerdRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQV 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1034 DDLEGSLEQEKKLRMDLERAKRKLEGDLK-LAQESIMDLENDKQQSEEKLKKKDFETSQLLSKIEDEQSLGAQ------- 1105
Cdd:pfam01576 695 EEMKTQLEELEDELQATEDAKLRLEVNMQaLKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQavaakkk 774
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1106 LQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEESTl 1185
Cdd:pfam01576 775 LELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASE- 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1186 QHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKN 1265
Cdd:pfam01576 854 RARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTS 933
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1266 DENlrqindlSAQRARLQTENGEFGRQLEEKEALV-SQLTRGKQAFTQQIEELKRQIEEEVKAKNALAHAVQSARHDCDL 1344
Cdd:pfam01576 934 QKS-------ESARQQLERQNKELKAKLQEMEGTVkSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKE 1006
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 288856329 1345 LREQFEEEQEAKAELQRGMSKANSEVAQWRTKYEtDAIQRTEELEESKKKLAQRLQEAEEQIEAVNSKCASL 1416
Cdd:pfam01576 1007 VLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE-EAEEEASRANAARRKLQRELDDATESNESMNREVSTL 1077
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1342-1830 |
7.18e-10 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 63.94 E-value: 7.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1342 CDLLREQFEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEELEesKKKLAQRLQEAEEQIEAVNS----KCASLE 1417
Cdd:pfam05622 16 CHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLL--LQKQLEQLQEENFRLETARDdyriKCEELE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1418 KTKQRLQGEVEDLMIDVERANALAANLDKKQRNFDKVlaewkQKYEegqAELEgaqkearslstelfkmknSYEETLDQL 1497
Cdd:pfam05622 94 KEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKV-----KKLE---ATVE------------------TYKKKLEDL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1498 ETLKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAVETEKAEIQtaleEAEGTLEHEESKILRVQLELNQ-------V 1570
Cdd:pfam05622 148 GDLRRQVKLLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKKleekleaL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1571 KSEIDRKLAEKD---EEIEQIK-RNSQRITDSMQSTLDSEVRSRNDALrIKKKMEGDLNEMEIQLSHANRQAAEAQKQlr 1646
Cdd:pfam05622 224 QKEKERLIIERDtlrETNEELRcAQLQQAELSQADALLSPSSDPGDNL-AAEIMPAEIREKLIRLQHENKMLRLGQEG-- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1647 NVQAQLKDAQLHLDDAVRGQEDMKEQVAMVERRNTLMQSEIEELRAALEQTErgrkvaeqelvdaservgllhSQNTSLL 1726
Cdd:pfam05622 301 SYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQG---------------------SKAEDSS 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1727 NTKKKLEADLVQIqSEVEDTVQEARNA-EDKAKKAITDAAMMAEEL-----KKEQDTSAHLERMKKNLE---VTVKDLQH 1797
Cdd:pfam05622 360 LLKQKLEEHLEKL-HEAQSELQKKKEQiEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEkakSVIKTLDP 438
|
490 500 510
....*....|....*....|....*....|...
gi 288856329 1798 RLDEAENLAMKGGKKQLQKLESRVRELESEVEA 1830
Cdd:pfam05622 439 KQNPASPPEIQALKNQLLEKDKKIEHLERDFEK 471
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
920-1502 |
7.22e-10 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 64.15 E-value: 7.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 920 KLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAQDESIGKLT---K 996
Cdd:PRK01156 170 KLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSsleD 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 997 EKKALQEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDD--------------LEGSLEQEKKLRMDLERAKRKLEGDLK 1062
Cdd:PRK01156 250 MKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDpvyknrnyindyfkYKNDIENKKQILSNIDAEINKYHAIIK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1063 LAQesimDLENDKQQSEEKLKKKDFETSQLLSKIEDE---QSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRA 1139
Cdd:PRK01156 330 KLS----VLQKDYNDYIKKKSRYDDLNNQILELEGYEmdyNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPD 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1140 DLSRELEEISERLEEAGGATAAqieMNKKREAefqkLRRDLEEstLQHEATAAALRKKQADSVAELGEqiDNLQRVKQKL 1219
Cdd:PRK01156 406 AIKKELNEINVKLQDISSKVSS---LNQRIRA----LRENLDE--LSRNMEMLNGQSVCPVCGTTLGE--EKSNHIINHY 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1220 EKEKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLEdqlseiKSKNDENLRQINDLSAQRArlqtengefgrQLEEKEAL 1299
Cdd:PRK01156 475 NEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLE------SEEINKSINEYNKIESARA-----------DLEDIKIK 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1300 VSQLTRGKQAFTQQIEELKRQIEEEVKAKNALAHAVQSARH--DCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRTkY 1377
Cdd:PRK01156 538 INELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISliDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKS-Y 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1378 ETDAIQRTEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANALAANLDKKQRNFDKVLAE 1457
Cdd:PRK01156 617 IDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKAN 696
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 288856329 1458 wkqkyeegQAELEGAQKEARSLSTELFKMKNSYEETLDQLETLKR 1502
Cdd:PRK01156 697 --------RARLESTIEILRTRINELSDRINDINETLESMKKIKK 733
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1502-1916 |
8.22e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 8.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1502 RENKNLQQEISDLTEQLGEtgksIHELEKSKKAVETEKAEIQTALEEAEGtlEHEESKILRVQLELNQVKSEIDRKLAEK 1581
Cdd:COG4717 71 KELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELRE--ELEKLEKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1582 DEEIEQIKRNSQRITDSMQSTLDSEVRSRNDALRIKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDD 1661
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1662 AvrgqedmkeqvamverrntlmQSEIEELRAALEQTERGRKVAEQE--LVDASERVGLLHSQNTSLLNTKKKLEADLVQI 1739
Cdd:COG4717 225 L---------------------EEELEQLENELEAAALEERLKEARllLLIAAALLALLGLGGSLLSLILTIAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1740 QSEVEDTVQEARNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENLamKGGKKQLQKLES 1819
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL--QELLREAEELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1820 RVRELESEVEAEQ-------------RRGADAVKGVRKYERRVKELTYQTEEDKKNVNRLQDLVDKLQLKVKA--YKRQS 1884
Cdd:COG4717 362 ELQLEELEQEIAAllaeagvedeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELeeLEEEL 441
|
410 420 430
....*....|....*....|....*....|..
gi 288856329 1885 EEAEEQANSHLSKLRKVQHELEEAEERADIAE 1916
Cdd:COG4717 442 EELEEELEELREELAELEAELEQLEEDGELAE 473
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1079-1776 |
1.18e-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: 63.59 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1079 EEKLKKKDFETSQLLSKIEDEQSLGAQlqkKIKELQARIEELEEEIEAERAARAKV-EKQRA---DLSRELEEISERLEE 1154
Cdd:pfam05483 62 QEGLKDSDFENSEGLSRLYSKLYKEAE---KIKKWKVSIEAELKQKENKLQENRKIiEAQRKaiqELQFENEKVSLKLEE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1155 AGGATAAQIEMNKKREAEFQKLRRDLE---ESTLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEYKMEid 1231
Cdd:pfam05483 139 EIQENKDLIKENNATRHLCNLLKETCArsaEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFK-- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1232 dLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDENLRQINDLSAqrarLQTENGEFGRQLEEKEALVS----QLTRGK 1307
Cdd:pfam05483 217 -LKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTF----LLEESRDKANQLEEKTKLQDenlkELIEKK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1308 QAFTQQIEELKRQIEEEVKAKNALAHAVQSA-RHDCDLLRE---QFEEEQEAKAELQRGMSKANSEVAQWRTKYETDAiQ 1383
Cdd:pfam05483 292 DHLTKELEDIKMSLQRSMSTQKALEEDLQIAtKTICQLTEEkeaQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQ-Q 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1384 RTEELEESKKKLAQRLQ----EAEEQIEAVNSKCASLEKTKQRLqGEVEDLMidveranalaanldKKQRNFDKVLAEWK 1459
Cdd:pfam05483 371 RLEKNEDQLKIITMELQkkssELEEMTKFKNNKEVELEELKKIL-AEDEKLL--------------DEKKQFEKIAEELK 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1460 QKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQlgetgksihelekskkavetek 1539
Cdd:pfam05483 436 GKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAH---------------------- 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1540 aeiqtaleeaegtleheESKILRVQLELNQVKSEIDRKLAEKDEEIEQIKRNSQRITDSMQSTLDSEVRSRNDALRIKKK 1619
Cdd:pfam05483 494 -----------------CDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1620 MEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAMVERRNTLMQSEIEELRAALEQTER 1699
Cdd:pfam05483 557 FIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEI 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1700 GRKVAEQELVDASERVGLLHSQNTSLLNTKKKLEADLVQIQSEVEDTVQEA----RNAEDKAKKAITDAAMMAEELKKEQ 1775
Cdd:pfam05483 637 KVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAvklqKEIDKRCQHKIAEMVALMEKHKHQY 716
|
.
gi 288856329 1776 D 1776
Cdd:pfam05483 717 D 717
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
845-1267 |
1.19e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 845 AETEKELATMKEDfVKCKEDLAKAEAKKKELEEKMVALLQEKNDLQLAVASESENLSDAEERCEGLIKSKIQLE---AKL 921
Cdd:PRK03918 269 EELKKEIEELEEK-VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEelkKKL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 922 KETTERLEDEEEiNAELTAKKRKLEDECSELKK-----DIDDLELTLAKVEKEKHATENKVKNLTEEMAAQDESIGKLTK 996
Cdd:PRK03918 348 KELEKRLEELEE-RHELYEEAKAKKEELERLKKrltglTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 997 EKKALQEAHQQ--TLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQE-------- 1066
Cdd:PRK03918 427 AIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLkelaeqlk 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1067 ------SIMDLENDKQQSE--EKLKKKDFETSQLLSKIEDEQSLGAQLQKKIKELQarieeleeeieaerAARAKVEKQR 1138
Cdd:PRK03918 507 eleeklKKYNLEELEKKAEeyEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELE--------------KKLDELEEEL 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1139 ADLSREL--------EEISERLEEAGGATAAQIEM-NKKREAEFQKLRRDLEESTLqhEATAAALRKKQADsVAELGEQI 1209
Cdd:PRK03918 573 AELLKELeelgfesvEELEERLKELEPFYNEYLELkDAEKELEREEKELKKLEEEL--DKAFEELAETEKR-LEELRKEL 649
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 288856329 1210 DNLQRV-----KQKLEKEKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDE 1267
Cdd:PRK03918 650 EELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
916-1244 |
1.69e-09 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 62.61 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 916 QLEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAQDESIGKLT 995
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 996 KEKKALQEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDK 1075
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1076 QQSEEKLKKKDFETSQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSR------------ 1143
Cdd:pfam07888 195 QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSmaaqrdrtqael 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1144 -----ELEEISERLEEA------GGATAAQ--------IEMNKKR----EAEFQKLRRDLEESTLQHEATAAAL------ 1194
Cdd:pfam07888 275 hqarlQAAQLTLQLADAslalreGRARWAQeretlqqsAEADKDRieklSAELQRLEERLQEERMEREKLEVELgrekdc 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 288856329 1195 -RKKQADSVAELGEQIDNL---QRVKQKLEKEKSEYKMEIDDLSSNMEAVAKAK 1244
Cdd:pfam07888 355 nRVQLSESRRELQELKASLrvaQKEKEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1460-1679 |
1.72e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1460 QKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAVETEK 1539
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1540 AEIQTALEEAEGTLeHEESKILRVQLELNQVKSEidrKLAEKDEEIEQIKRNSQRITDSMQSTLDSEVRSRNDALRIKKK 1619
Cdd:COG4942 100 EAQKEELAELLRAL-YRLGRQPPLALLLSPEDFL---DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1620 MEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAMVERR 1679
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1399-1610 |
2.13e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.77 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1399 LQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANALAANLDKKQRNFDKVLAEWKQKYEEGQAELEG----AQK 1474
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraraLYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1475 EARSLST-ELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGEtgksiheLEKSKKAVETEKAEIQTALEEAEGTL 1553
Cdd:COG3883 98 SGGSVSYlDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAE-------LEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 288856329 1554 EHEESKILRVQLELNQVKSEIDRKLAEKDEEIEQIKRNSQRITDSMQSTLDSEVRSR 1610
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
916-1116 |
2.22e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 916 QLEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAQDESIGKLT 995
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 996 KEKK----ALQEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDL 1071
Cdd:COG4942 104 EELAellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 288856329 1072 ENDKQQSEEKLKKKDFETSQLLSKIEDEQSLGAQLQKKIKELQAR 1116
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
918-1692 |
2.87e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 62.66 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 918 EAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEkekhatenkvknltEEMAAQDESIGKLTKE 997
Cdd:COG3096 353 QEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQ--------------QALDVQQTRAIQYQQA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 998 KKALQEAHQQT-LDDLqAEEDKVNTLTKSKTKLEQQVDDLegsLEQEKKLRMDlERAKRKLEGDLKL------------- 1063
Cdd:COG3096 419 VQALEKARALCgLPDL-TPENAEDYLAAFRAKEQQATEEV---LELEQKLSVA-DAARRQFEKAYELvckiageversqa 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1064 ---AQESIMDLENDKQQSE--EKLKKKDFETSQLLSKIEDEQSLGAQLQKKIKElqarieeleeeieaERAARAKVEKQR 1138
Cdd:COG3096 494 wqtARELLRRYRSQQALAQrlQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQ--------------QLDAAEELEELL 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1139 ADLSRELEEISERLEEAGgatAAQIEMNKKREaEFQKLRRDLEESTLQHEATAAALRKKQAdsvaELGEQIDNLQRV--- 1215
Cdd:COG3096 560 AELEAQLEELEEQAAEAV---EQRSELRQQLE-QLRARIKELAARAPAWLAAQDALERLRE----QSGEALADSQEVtaa 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1216 -KQKLEKEKsEYKMEIDDLssnmeavAKAKANLEKMCRTL------EDQ-------------LSEIK---SKNDE----- 1267
Cdd:COG3096 632 mQQLLERER-EATVERDEL-------AARKQALESQIERLsqpggaEDPrllalaerlggvlLSEIYddvTLEDApyfsa 703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1268 ---NLRQ---INDLSAQRARLQT-----------------------ENGEFGR----QLEEKEALVSQLTR----GKQAF 1310
Cdd:COG3096 704 lygPARHaivVPDLSAVKEQLAGledcpedlyliegdpdsfddsvfDAEELEDavvvKLSDRQWRYSRFPEvplfGRAAR 783
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1311 TQQIEELKRQIEEEVKAKNALAHAVQS------------ARHDCDLLREQFEEE----QEAKAELQRGMSKANSEVAQWR 1374
Cdd:COG3096 784 EKRLEELRAERDELAEQYAKASFDVQKlqrlhqafsqfvGGHLAVAFAPDPEAElaalRQRRSELERELAQHRAQEQQLR 863
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1375 TKYEtdaiQRTEELEESKK-----------KLAQRLQEAEEQIEAVNSKCASLEKTKQRLqGEVEDlmidveranaLAAN 1443
Cdd:COG3096 864 QQLD----QLKEQLQLLNKllpqanlladeTLADRLEELREELDAAQEAQAFIQQHGKAL-AQLEP----------LVAV 928
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1444 LDKKQRNFDKVlaewKQKYEEGQAELEGAQKEARSLsTELFKMKN--SYEETLDQLEtlkrenknlqqEISDLTEQLGEt 1521
Cdd:COG3096 929 LQSDPEQFEQL----QADYLQAKEQQRRLKQQIFAL-SEVVQRRPhfSYEDAVGLLG-----------ENSDLNEKLRA- 991
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1522 gksihELEKskkaVETEKAEIQTALEEAEGtlEHEESkiLRVQLELN---QVKSEIdrkLAEKDEEIEQIkrnSQRITDS 1598
Cdd:COG3096 992 -----RLEQ----AEEARREAREQLRQAQA--QYSQY--NQVLASLKssrDAKQQT---LQELEQELEEL---GVQADAE 1052
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1599 MQSTLDSEVRSRNDALRIKKkmeGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAM--V 1676
Cdd:COG3096 1053 AEERARIRRDELHEELSQNR---SRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAGWCAVLRLARDndV 1129
|
890 900
....*....|....*....|.
gi 288856329 1677 ERRntLMQSEI-----EELRA 1692
Cdd:COG3096 1130 ERR--LHRRELaylsaDELRS 1148
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
997-1855 |
2.91e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 62.67 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 997 EKKALQEAHQQTLDDLQAEEDkvnTLTKSKTKLEQQVDDLEGSL----------EQEKKLRMDLERAKRKLEGDL---KL 1063
Cdd:PRK04863 297 TSRRQLAAEQYRLVEMARELA---ELNEAESDLEQDYQAASDHLnlvqtalrqqEKIERYQADLEELEERLEEQNevvEE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1064 AQESIMDLENDKQQSEEklkkkdfETSQLLSKIED-EQSLGAQLQKKIKELQARIEELeeeieaeraaraKVEKQRADLS 1142
Cdd:PRK04863 374 ADEQQEENEARAEAAEE-------EVDELKSQLADyQQALDVQQTRAIQYQQAVQALE------------RAKQLCGLPD 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1143 RELEEISERLEEAggATAAQIEMNKKREAEfQKLRrDLEESTLQHEATAAALRKkqadsvaeLGEQID--NLQRVKQKLE 1220
Cdd:PRK04863 435 LTADNAEDWLEEF--QAKEQEATEELLSLE-QKLS-VAQAAHSQFEQAYQLVRK--------IAGEVSrsEAWDVARELL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1221 KEKSEYKMEIDDLSSnmeavakAKANLEKMCRTLEDQLSEIKSKNDENLRQINDLSAQrARLQTENGEFGRQLEEKEALV 1300
Cdd:PRK04863 503 RRLREQRHLAEQLQQ-------LRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDE-DELEQLQEELEARLESLSESV 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1301 SQLTRGKQAFTQQIEELKRQIEEeVKAKNALAHAVQSArhdCDLLREQFEEEQEAKAELQRGMSkansevaqwrtkyetD 1380
Cdd:PRK04863 575 SEARERRMALRQQLEQLQARIQR-LAARAPAWLAAQDA---LARLREQSGEEFEDSQDVTEYMQ---------------Q 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1381 AIQRTEELEESKKKLAQRLQEAEEQIEAVNSKCAS----LEKTKQRLQGE-VEDLMIDVERANA--------------LA 1441
Cdd:PRK04863 636 LLERERELTVERDELAARKQALDEEIERLSQPGGSedprLNALAERFGGVlLSEIYDDVSLEDApyfsalygparhaiVV 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1442 ANLDKKQRNFDKvlaewkqkyEEGQAE----LEG---AQKEARSLSTELFK----------MKNSYEETLDQLETLKREN 1504
Cdd:PRK04863 716 PDLSDAAEQLAG---------LEDCPEdlylIEGdpdSFDDSVFSVEELEKavvvkiadrqWRYSRFPEVPLFGRAAREK 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1505 --KNLQQEISDLTEQLGETGKSIHELEKSKKAV----------------ETEKAEIQTALEEAEGTLEHEESKILRVQLE 1566
Cdd:PRK04863 787 riEQLRAEREELAERYATLSFDVQKLQRLHQAFsrfigshlavafeadpEAELRQLNRRRVELERALADHESQEQQQRSQ 866
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1567 LNQVKSEID--RKLAEK---------DEEIEQIKRNSQRITDSMQStldseVRSRNDALRIKKKMEGDLNEMEIQLSHAN 1635
Cdd:PRK04863 867 LEQAKEGLSalNRLLPRlnlladetlADRVEEIREQLDEAEEAKRF-----VQQHGNALAQLEPIVSVLQSDPEQFEQLK 941
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1636 RQAAEAQKQLRNVQAQLKDaqlhLDDAVRGQEDMK--EQVAMVERRNTLmqseIEELRAALEQTERGRKVAEQELVDASE 1713
Cdd:PRK04863 942 QDYQQAQQTQRDAKQQAFA----LTEVVQRRAHFSyeDAAEMLAKNSDL----NEKLRQRLEQAEQERTRAREQLRQAQA 1013
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1714 RvgllHSQNTSLLntkkkleADLVQIQSEVEDTVQEA-RNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKN-LEvt 1791
Cdd:PRK04863 1014 Q----LAQYNQVL-------ASLKSSYDAKRQMLQELkQELQDLGVPADSGAEERARARRDELHARLSANRSRRNqLE-- 1080
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 288856329 1792 vkdLQHRLDEAEnlaMKGGKKQLQKLESRVRELESEVEAEQRRGADAVKGVRKY--ERRV--KELTYQ 1855
Cdd:PRK04863 1081 ---KQLTFCEAE---MDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNgvERRLhrRELAYL 1142
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
944-1531 |
4.78e-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: 61.99 E-value: 4.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 944 KLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAQDESI------GKLTKEKKALQEAHQQTLDDLQAEED 1017
Cdd:TIGR00606 581 SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEIEKSSKQRAMLAG 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1018 KVNTLTKSKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQesimdlenDKQQSEEK-LKKKDFETSQLLSKI 1096
Cdd:TIGR00606 661 ATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAP--------DKLKSTESeLKKKEKRRDEMLGLA 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1097 EDEQSLGAQLQKKIKELQarieeleeeieaeraarAKVEKQRADLSRELEEISERlEEAGGATAAQIEMNKKREAEFQKL 1176
Cdd:TIGR00606 733 PGRQSIIDLKEKEIPELR-----------------NKLQKVNRDIQRLKNDIEEQ-ETLLGTIMPEEESAKVCLTDVTIM 794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1177 RRdLEESTLQHEataaalrKKQADSVAELgeQIDNLQRVKQKLEKEKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLED 1256
Cdd:TIGR00606 795 ER-FQMELKDVE-------RKIAQQAAKL--QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKS 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1257 QLSEIKSKN---DENLRQINDLSAQRARLQTENGEFGRQLEEKEALVSQLTRGKQAFTQQIEEL-KRQIEEEVKAKNALA 1332
Cdd:TIGR00606 865 KTNELKSEKlqiGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELiSSKETSNKKAQDKVN 944
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1333 HAVQSARHDCDLLREQFEEEQEAKAELQR-------GMSKANSEVAQWRTKYETDAIQRTEELEESKKKlaQRLQEAEEQ 1405
Cdd:TIGR00606 945 DIKEKVKNIHGYMKDIENKIQDGKDDYLKqketelnTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQ--ERWLQDNLT 1022
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1406 IEAVNSKCASLEKTKQRLQGEVEDLMIDVERA--NALAANLDKKQRNFDKVLAEwKQKYEEgqaELEGAQKEARslSTEL 1483
Cdd:TIGR00606 1023 LRKRENELKEVEEELKQHLKEMGQMQVLQMKQehQKLEENIDLIKRNHVLALGR-QKGYEK---EIKHFKKELR--EPQF 1096
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 288856329 1484 FKMKNSYEETLDQLETLKRENKNL--------QQEISDLTEQLGETGKSIHELEKS 1531
Cdd:TIGR00606 1097 RDAEEKYREMMIVMRTTELVNKDLdiyyktldQAIMKFHSMKMEEINKIIRDLWRS 1152
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1293-1911 |
5.68e-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: 5.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1293 LEEKE------ALVSQLTRGKQAFtQQIEELKRQIEeevkaknALAHAVQSArhdcdllrEQFEEEQEAKAELQRGMSKA 1366
Cdd:COG4913 218 LEEPDtfeaadALVEHFDDLERAH-EALEDAREQIE-------LLEPIRELA--------ERYAAARERLAELEYLRAAL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1367 NSEVAQwrTKYETdAIQRTEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGE-VEDLMIDVERANALAANLD 1445
Cdd:COG4913 282 RLWFAQ--RRLEL-LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1446 KKQRNFDKVLAEWKQKYEEGQAELEGAQKEARSLSTELfkmknsyeetldqletlkrenknlQQEISDLTEQLGETGKSI 1525
Cdd:COG4913 359 RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL------------------------EEELEALEEALAEAEAAL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1526 HELEKSKKAVETEKAEIQtaleeaegtleheeskilrvqlelnQVKSEIDRKL--------------------------- 1578
Cdd:COG4913 415 RDLRRELRELEAEIASLE-------------------------RRKSNIPARLlalrdalaealgldeaelpfvgeliev 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1579 AEKDEE-----------------------------IEQIKrNSQRI-TDSMQSTLDSEVRSRNDALRIKKKMEGDLN--- 1625
Cdd:COG4913 470 RPEEERwrgaiervlggfaltllvppehyaaalrwVNRLH-LRGRLvYERVRTGLPDPERPRLDPDSLAGKLDFKPHpfr 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1626 ---EMEIQlSHANRQAAEAQKQLRNVQAQL-KDAQLHlDDAVRGQEDMKEQVAmveRRNTLMQS---EIEELRAALEQTE 1698
Cdd:COG4913 549 awlEAELG-RRFDYVCVDSPEELRRHPRAItRAGQVK-GNGTRHEKDDRRRIR---SRYVLGFDnraKLAALEAELAELE 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1699 RGRKVAEQELVDASERVGLLHSQNTSLLNTKKKLEA--DLVQIQSEVEDtVQEARNAEDKAKKAITDAAMMAEELKKEQD 1776
Cdd:COG4913 624 EELAEAEERLEALEAELDALQERREALQRLAEYSWDeiDVASAEREIAE-LEAELERLDASSDDLAALEEQLEELEAELE 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1777 TsahLERMKKNLEVTVKDLQHRLDEAEnlamkggkKQLQKLESRVRELESEVEAEQRRGADAVKGVRKYERRVKELTYQT 1856
Cdd:COG4913 703 E---LEEELDELKGEIGRLEKELEQAE--------EELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENL 771
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 288856329 1857 EED-KKNVNRLQDLVDKLQLKVKAYKRQ----------SEEAEEQANSHLSKLRkvQHELEEAEER 1911
Cdd:COG4913 772 EERiDALRARLNRAEEELERAMRAFNREwpaetadldaDLESLPEYLALLDRLE--EDGLPEYEER 835
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
991-1426 |
1.01e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 991 IGKLTKEKKAL--------------QEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEKKLRMDLERAKRK 1056
Cdd:COG4717 48 LERLEKEADELfkpqgrkpelnlkeLKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1057 LE--GDLKLAQESIMDLENDKQQSEEKLKkkdfETSQLLSKIEDEQSLGAQLQKKIKEL-QARIEELEEEIEAERAARAK 1133
Cdd:COG4717 128 LPlyQELEALEAELAELPERLEELEERLE----ELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1134 VEKQRADLSRELEEISERLEEAGGATaAQIEMNKKREAEFQKLRR------------------DLEESTLQHEATAAALR 1195
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEEL-EQLENELEAAALEERLKEarlllliaaallallglgGSLLSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1196 --------KKQADSVAELGEQIDNLQRVKQKLEKEKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDE 1267
Cdd:COG4717 283 lgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1268 nlRQINDLSAQRARLQTENGefgrqLEEKEALVSQLTRGKQAftQQIEELKRQIEEEVKAKNALAHAvQSARHDCDLLRE 1347
Cdd:COG4717 363 --LQLEELEQEIAALLAEAG-----VEDEEELRAALEQAEEY--QELKEELEELEEQLEELLGELEE-LLEALDEEELEE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1348 QFEEEQEAKAELQRGMSKANSEVAqwRTKYETDAIQRTEELEESKKKLAQ---RLQEAEEQIEAVNSKCASLEKTKQRLQ 1424
Cdd:COG4717 433 ELEELEEELEELEEELEELREELA--ELEAELEQLEEDGELAELLQELEElkaELRELAEEWAALKLALELLEEAREEYR 510
|
..
gi 288856329 1425 GE 1426
Cdd:COG4717 511 EE 512
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
916-1697 |
1.07e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.74 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 916 QLEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEkekhatenkvknltEEMAAQDESIGKLT 995
Cdd:PRK04863 352 RYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQ--------------QALDVQQTRAIQYQ 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 996 KEKKALQEAHQQT-LDDLQAE--EDKVNTLTKSKTKLEQQVDDLEGSLEQEKKLRMDLERAK---RKLEGDL------KL 1063
Cdd:PRK04863 418 QAVQALERAKQLCgLPDLTADnaEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYqlvRKIAGEVsrseawDV 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1064 AQESIMDLENDKQQSE--EKLKKKDFETSQLLSKIEDEQSLGAQLQKKikelqarieeleeeIEAERAARAKVEKQRADL 1141
Cdd:PRK04863 498 ARELLRRLREQRHLAEqlQQLRMRLSELEQRLRQQQRAERLLAEFCKR--------------LGKNLDDEDELEQLQEEL 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1142 SRELEEISERLEEAGgatAAQIEMNKKREaefqklrrDLEESTLQHEATAAALRKKQaDSVAELGEQ----IDNLQRV-- 1215
Cdd:PRK04863 564 EARLESLSESVSEAR---ERRMALRQQLE--------QLQARIQRLAARAPAWLAAQ-DALARLREQsgeeFEDSQDVte 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1216 --KQKLEKEKsEYKMEIDDLSSNMEAV--------AKAKANLEKMcRTLEDQ-----LSEIKSknDENL----------- 1269
Cdd:PRK04863 632 ymQQLLERER-ELTVERDELAARKQALdeeierlsQPGGSEDPRL-NALAERfggvlLSEIYD--DVSLedapyfsalyg 707
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1270 --RQ---INDLSAQRARLQTE------------------NGEFGRQLEEKEALVSQLTR-------------GKQAFTQQ 1313
Cdd:PRK04863 708 paRHaivVPDLSDAAEQLAGLedcpedlyliegdpdsfdDSVFSVEELEKAVVVKIADRqwrysrfpevplfGRAAREKR 787
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1314 IEELKRQIEEEVKAKNALAHAVQsarhDCDLLREQFEE--------------EQEAKA------ELQRGMSKANSEVAQW 1373
Cdd:PRK04863 788 IEQLRAEREELAERYATLSFDVQ----KLQRLHQAFSRfigshlavafeadpEAELRQlnrrrvELERALADHESQEQQQ 863
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1374 RTKYET--DAIQRTEELEESKK-----KLAQRLQEAEEQIEAVNSKCASLEKTKQRLqgevedlmidvERANALAANLDK 1446
Cdd:PRK04863 864 RSQLEQakEGLSALNRLLPRLNlladeTLADRVEEIREQLDEAEEAKRFVQQHGNAL-----------AQLEPIVSVLQS 932
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1447 KQRNFDKVlaewKQKYEEGQAELEGAQKEARSLsTELFKMKN--SYEETLDQLEtlkrenknlqqEISDLTEQLGetgks 1524
Cdd:PRK04863 933 DPEQFEQL----KQDYQQAQQTQRDAKQQAFAL-TEVVQRRAhfSYEDAAEMLA-----------KNSDLNEKLR----- 991
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1525 ihelEKSKKAvETEKAEIQTALEEAEGTLeheeSKILRVQLELnqvKSEIDRKLAEKDEEIEQIKRNSQRITDSMQSTLD 1604
Cdd:PRK04863 992 ----QRLEQA-EQERTRAREQLRQAQAQL----AQYNQVLASL---KSSYDAKRQMLQELKQELQDLGVPADSGAEERAR 1059
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1605 SEVRSRNDALRIKKkmeGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAM--VERRntL 1682
Cdd:PRK04863 1060 ARRDELHARLSANR---SRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDngVERR--L 1134
|
890 900
....*....|....*....|
gi 288856329 1683 MQSEI-----EELRAALEQT 1697
Cdd:PRK04863 1135 HRRELaylsaDELRSMSDKA 1154
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1064-1281 |
1.16e-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: 59.39 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1064 AQESIMDLENDKQQSEEKLKKKDFETSQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSR 1143
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1144 ELEEISERLEE-------AGGATAAQIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQadsvAELGEQIDNLQRVK 1216
Cdd:COG4942 98 ELEAQKEELAEllralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL----AELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 288856329 1217 QKLEKEKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDENLRQINDLSAQRAR 1281
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
913-1642 |
1.21e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 60.45 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 913 SKIQLEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAQDESIG 992
Cdd:TIGR00606 350 GRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQAD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 993 KLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQEsiMDLE 1072
Cdd:TIGR00606 430 EIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEV--KSLQ 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1073 NDKQQSEEKLKKKDFETSQLLSKIEDEQSLGAQLQKK------IKELQARIEELEEEIEAERAARAKVEKQRADLSRELE 1146
Cdd:TIGR00606 508 NEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKmdkdeqIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEIN 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1147 EISERLEEAGGATAAQIEMNKKREAEFQKLRRdlEESTLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEY 1226
Cdd:TIGR00606 588 QTRDRLAKLNKELASLEQNKNHINNELESKEE--QLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVY 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1227 KMEIDDLSSNMEA-------VAKAKANLEKMCRTLEDQLSEIKSKNDENLRQINDLSAQRARLQTENGEFGRQLEEKEAL 1299
Cdd:TIGR00606 666 SQFITQLTDENQSccpvcqrVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKE 745
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1300 VSQLTRGKQAFTQQIEELKRQIEEEVKAKNALAHAVQSAR---HDCDLLREQFEEEQEAKAELQRGMSKANSeVAQWRTK 1376
Cdd:TIGR00606 746 IPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvclTDVTIMERFQMELKDVERKIAQQAAKLQG-SDLDRTV 824
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1377 YETDaiQRTEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANALAANLDKKQRNFDKVLA 1456
Cdd:TIGR00606 825 QQVN--QEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIR 902
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1457 EWKQKYEEgQAELEGAQKEARSLSTELFKMKN-SYEETLDQLETLKRENKNLQQEISDLTEQLGEtGKsihelEKSKKAV 1535
Cdd:TIGR00606 903 EIKDAKEQ-DSPLETFLEKDQQEKEELISSKEtSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQD-GK-----DDYLKQK 975
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1536 ETEKAEIQTALEEAEGTLE----------------HEESKILRVQLELNQVKSEI---DRKLAEKDEEIEQIKRNSQRIT 1596
Cdd:TIGR00606 976 ETELNTVNAQLEECEKHQEkinedmrlmrqdidtqKIQERWLQDNLTLRKRENELkevEEELKQHLKEMGQMQVLQMKQE 1055
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 288856329 1597 -DSMQSTLDSEVRSRNDALRIKKKMEGDLNEMEIQLSHANRQAAEAQ 1642
Cdd:TIGR00606 1056 hQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEK 1102
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1452-1935 |
1.22e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1452 DKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMKNSYE-ETLDQLETLKRENKNLQQEISDLTEQlgetGKSIHELEK 1530
Cdd:PTZ00121 1096 AFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKaEDARKAEEARKAEDAKRVEIARKAED----ARKAEEARK 1171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1531 SKKAVETEKAEIQTALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEEIEQIKRNSQRITDSMQSTLDSEVRSR 1610
Cdd:PTZ00121 1172 AEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNN 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1611 NDalrIKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVamverrntlmqseiEEL 1690
Cdd:PTZ00121 1252 EE---IRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA--------------EEA 1314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1691 RAALE---QTERGRKVAEQELVDASERvgllhsqntsllntKKKLEADlvqiQSEVEDTVQEARNAEDKAK---KAITDA 1764
Cdd:PTZ00121 1315 KKADEakkKAEEAKKKADAAKKKAEEA--------------KKAAEAA----KAEAEAAADEAEAAEEKAEaaeKKKEEA 1376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1765 AMMAEELKKEQDTSAHLERMKKNLEVTVKdlqhrldEAENLAMKGGKKQlqklesrvRELESEVEAEQRRGADAVKGVRK 1844
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEAKKKAEEDKK-------KADELKKAAAAKK--------KADEAKKKAEEKKKADEAKKKAE 1441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1845 YERRVKELTYQTEEDKKNVNRLQDLVDKL---QLKVKA-YKRQSEEAE---EQANSHLSKLRKVQHELEEAEERADIAES 1917
Cdd:PTZ00121 1442 EAKKADEAKKKAEEAKKAEEAKKKAEEAKkadEAKKKAeEAKKADEAKkkaEEAKKKADEAKKAAEAKKKADEAKKAEEA 1521
|
490
....*....|....*...
gi 288856329 1918 QVNKLRAKSRDSGKGKDA 1935
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEA 1539
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1191-1548 |
1.29e-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: 59.52 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1191 AAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDENLR 1270
Cdd:pfam07888 29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1271 QINDLSAQRARLQTENGEFG---RQLEEKEALVSQLTRGKQA----FTQQIEELKRQIEEEVKAKNALAHAVQSARHDCD 1343
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEariRELEEDIKTLTQRVLERETelerMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1344 LLREQFEEEQEAKAELQRGMSKANSEVAQWRTKYETdAIQRTEELEESKKKLA---QRLQEAEEQIEAVNSKCASLEKTK 1420
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTT-AHRKEAENEALLEELRslqERLNASERKVEGLGEELSSMAAQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1421 QRLQGEVEDLMIDVERANALAANLDKKQRnfdKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLETL 1500
Cdd:pfam07888 268 DRTQAELHQARLQAAQLTLQLADASLALR---EGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKL 344
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 288856329 1501 KREnknLQQEISDLTEQLGETGKSIHELEKSKKAVETEKAEIQTALEE 1548
Cdd:pfam07888 345 EVE---LGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQE 389
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1530-1790 |
1.58e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 59.93 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1530 KSKKAVETEKAEIQTALEEAEGTLEheesKILRVQLELNQVKseidRKLAEKDEEIEQIKRNSQRitdsMQSTLDSEVRS 1609
Cdd:PRK11281 49 NKQKLLEAEDKLVQQDLEQTLALLD----KIDRQKEETEQLK----QQLAQAPAKLRQAQAELEA----LKDDNDEETRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1610 RNDALRIKKkMEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAvrgqedmkeQVAMVERRNTLMQSEIEE 1689
Cdd:PRK11281 117 TLSTLSLRQ-LESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYAN---------SQRLQQIRNLLKGGKVGG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1690 lrAALEQTERGRKVAEQELVDA--SERVGLL--HSQNTSLLNTK--------KKLEADLVQIQSEV--------EDTVQE 1749
Cdd:PRK11281 187 --KALRPSQRVLLQAEQALLNAqnDLQRKSLegNTQLQDLLQKQrdyltariQRLEHQLQLLQEAInskrltlsEKTVQE 264
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 288856329 1750 ARNAEDKAKkaITDAAMMAEELKKEQDTSAHL--------ERMKKNLEV 1790
Cdd:PRK11281 265 AQSQDEAAR--IQANPLVAQELEINLQLSQRLlkateklnTLTQQNLRV 311
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1617-1838 |
1.77e-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: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1617 KKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAMVERRNTLMQSEIEELRAALEQ 1696
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1697 tergRKVAEQELVDASERVG-------LLHSQNTSLLNTKKKLEADLVQIQSEVEDTVQEARNAEDKAKKAITDAAMMAE 1769
Cdd:COG4942 102 ----QKEELAELLRALYRLGrqpplalLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1770 ELKKEQDTS-AHLERMKKNLEVTVKDLQHRLDEAENlAMKGGKKQLQKLESRVRELESEVEAEQRRGADA 1838
Cdd:COG4942 178 ALLAELEEErAALEALKAERQKLLARLEKELAELAA-ELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1532-1928 |
1.97e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.67 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1532 KKAVETEKAEIQTALEEAEGTLEHEESKilrvqlELNQVKSEIDRKLAEKDEEIEQI---KRNSQRITDSMQSTLDsEVR 1608
Cdd:PRK02224 175 RLGVERVLSDQRGSLDQLKAQIEEKEEK------DLHERLNGLESELAELDEEIERYeeqREQARETRDEADEVLE-EHE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1609 SRNDALrikKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQE-DMKEQVAMVERRNTLmQSEI 1687
Cdd:PRK02224 248 ERREEL---ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlDDADAEAVEARREEL-EDRD 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1688 EELRAALEQTERGRKVAEQELVDASERVGLLHSQNTSLLNTKKKLEADLVQIQSEVED---TVQEARNAEDKAKKAITDA 1764
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDrreEIEELEEEIEELRERFGDA 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1765 AM----MAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENLaMKGGK----KQLQKLESRVRELEsevEAEQRRGa 1836
Cdd:PRK02224 404 PVdlgnAEDFLEELREERDELREREAELEATLRTARERVEEAEAL-LEAGKcpecGQPVEGSPHVETIE---EDRERVE- 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1837 davkgvrKYERRVKELTYQTEEDKKNVNRLQDLVdklqlkvkaykrqseEAEEQANSHLSKLRKVQHELEEAEERADIAE 1916
Cdd:PRK02224 479 -------ELEAELEDLEEEVEEVEERLERAEDLV---------------EAEDRIERLEERREDLEELIAERRETIEEKR 536
|
410
....*....|..
gi 288856329 1917 SQVNKLRAKSRD 1928
Cdd:PRK02224 537 ERAEELRERAAE 548
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1239-1477 |
2.20e-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: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1239 AVAKAKANLEKMCRTLEDQLSEIKSKNDENLRQINDLSAQRARLQTENGEFGRQLEEKEALVSQLTRGKQAFTQQIEELK 1318
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1319 RQIEEEVKA-KNALAHAVQSARHDcdllREQFEEEQEAKAELQRgMSKANSEVAQWRtkyetdaIQRTEELEESKKKLAQ 1397
Cdd:COG4942 97 AELEAQKEElAELLRALYRLGRQP----PLALLLSPEDFLDAVR-RLQYLKYLAPAR-------REQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1398 RLQEAEEQIEAVNSKCASLEKTKQRLQGEvedlmidVERANALAANLDKKQRNFDKVLAEWKQKYEEGQAELEGAQKEAR 1477
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEAL-------KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1039-1902 |
2.60e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 59.29 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1039 SLEQEKKLRMDLERAKRKLEGDLKL----------AQESIMDLENDKQQSEEKLKKKDFETSQLLSKiedeqslgaqlQK 1108
Cdd:TIGR00606 187 ALETLRQVRQTQGQKVQEHQMELKYlkqykekaceIRDQITSKEAQLESSREIVKSYENELDPLKNR-----------LK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1109 KIKELQARIEELEeeieAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQIEMNKKREA-EFQKLRRDLEESTLQH 1187
Cdd:TIGR00606 256 EIEHNLSKIMKLD----NEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVrEKERELVDCQRELEKL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1188 EATAAALRKKQADSVAELGE-----QIDNLQRVKQKLEKEKSEYKMEIDDLSSNME-------AVAKAKANLEKMCRTLE 1255
Cdd:TIGR00606 332 NKERRLLNQEKTELLVEQGRlqlqaDRHQEHIRARDSLIQSLATRLELDGFERGPFserqiknFHTLVIERQEDEAKTAA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1256 DQLSEIKSKNDENLRQINDLSAQRARLQTENGEFGRQLEEKEALVSQLTRGKQAFTQQIEELKRQIEEEVKAKNALAHAV 1335
Cdd:TIGR00606 412 QLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAE 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1336 QSARHDCDLLREQFeeEQEAKAELQRGMSKANSEVAQwrTKYETDAIQRTEELEESKKKLAQRLQEAEEQIEAVNSKCAS 1415
Cdd:TIGR00606 492 KNSLTETLKKEVKS--LQNEKADLDRKLRKLDQEMEQ--LNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLG 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1416 LEKTKQRLQGEVEDLMIDVERanalaanLDKKQRNFDKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLD 1495
Cdd:TIGR00606 568 YFPNKKQLEDWLHSKSKEINQ-------TRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESD 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1496 qLETLKRENKNLQQEISDLTEQLGETGKSIHEL-EKSKKAVETEKAEIQTALEEAEgTLEHEESKILRVQLELNQVKSEI 1574
Cdd:TIGR00606 641 -LERLKEEIEKSSKQRAMLAGATAVYSQFITQLtDENQSCCPVCQRVFQTEAELQE-FISDLQSKLRLAPDKLKSTESEL 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1575 DRKLAEKDEEIEQIKrNSQRITDSMQSTLdSEVRSRNDAL-RIKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNV----- 1648
Cdd:TIGR00606 719 KKKEKRRDEMLGLAP-GRQSIIDLKEKEI-PELRNKLQKVnRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVtimer 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1649 -QAQLKDAQLHLDDAVrGQEDMKEQVAMVERRNTLMQSEIEELRAALEQTERGRKVAEqelvDASERVGLLHSQNTSLLN 1727
Cdd:TIGR00606 797 fQMELKDVERKIAQQA-AKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQ----DQQEQIQHLKSKTNELKS 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1728 TKKKLEADLVQIQSEVEDTVQEA-------RNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLD 1800
Cdd:TIGR00606 872 EKLQIGTNLQRRQQFEEQLVELStevqsliREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVK 951
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1801 EA-------ENLAMKGGKKQLQKLESRVRELESEVEAEQRRGadavkgvRKYERRVKELTYQTEEDKKNVNRLQDlvdkl 1873
Cdd:TIGR00606 952 NIhgymkdiENKIQDGKDDYLKQKETELNTVNAQLEECEKHQ-------EKINEDMRLMRQDIDTQKIQERWLQD----- 1019
|
890 900
....*....|....*....|....*....
gi 288856329 1874 QLKVKAYKRQSEEAEEQANSHLSKLRKVQ 1902
Cdd:TIGR00606 1020 NLTLRKRENELKEVEEELKQHLKEMGQMQ 1048
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1495-1712 |
3.02e-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: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1495 DQLETLKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAVETEKAEIQTALEEAEGTLEHEESKILRVQLELNQVKSEI 1574
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1575 DRKLAEKDEEIEQIKRNSQRITDSM----QSTLDSEVRSR--NDALRIKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNV 1648
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 288856329 1649 QAQLKDAQLHLDDAVRGQEDM----KEQVAMVERRNTLMQSEIEELRAALEQTERGRKVAEQELVDAS 1712
Cdd:COG4942 180 LAELEEERAALEALKAERQKLlarlEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1355-1649 |
3.62e-08 |
|
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: 59.08 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1355 AKAELQRGMSKANSEVAQwrTKYETDAIQRTEELEESKKKLAQrlqEAEEQIEAVNSKCASLEKTKQrlqgevedlmidv 1434
Cdd:NF012221 1536 ATSESSQQADAVSKHAKQ--DDAAQNALADKERAEADRQRLEQ---EKQQQLAAISGSQSQLESTDQ------------- 1597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1435 eraNALAANldkkqrnfdkvlaewkqkyeeGQAELEGAQKEARSLSTELFKMKnsyeETLDQLETLKRENKNLQQE---- 1510
Cdd:NF012221 1598 ---NALETN---------------------GQAQRDAILEESRAVTKELTTLA----QGLDALDSQATYAGESGDQwrnp 1649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1511 -----ISDLTEQLGETGKSIHE-LEKSKKAVETEKAEIQTALEEAEGTLEHEESKILRVQLELNQVKSEIDRKlaeKDEE 1584
Cdd:NF012221 1650 fagglLDRVQEQLDDAKKISGKqLADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKR---KDDA 1726
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 288856329 1585 IEQIKRNSQRITDSMQSTLDSEVRSRNDAlrikkkmegdlnemeiqlSHANRQAAEAQKQLRNVQ 1649
Cdd:NF012221 1727 LAKQNEAQQAESDANAAANDAQSRGEQDA------------------SAAENKANQAQADAKGAK 1773
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1019-1597 |
3.64e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.76 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1019 VNTLTKSKTKLEQQVDDLEGSLEQEKKLRMDLERakrklegdlklaqeSIMDLENDKQQSEEKLKKKdfetSQLLSKIED 1098
Cdd:PRK01156 161 INSLERNYDKLKDVIDMLRAEISNIDYLEEKLKS--------------SNLELENIKKQIADDEKSH----SITLKEIER 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1099 EQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEE---ISERLEEAGGATAAQIEMNKKREAEFQK 1175
Cdd:PRK01156 223 LSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKnnyYKELEERHMKIINDPVYKNRNYINDYFK 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1176 LRRDLEESTLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKleKEKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLE 1255
Cdd:PRK01156 303 YKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKK--SRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1256 DQLSEIKSKNDENLRQINDLSAQRARLQTENGEFGRQLEEKEALVSQLTRGKQAFTQQIEELKRQIEEEVKAKNALAHAV 1335
Cdd:PRK01156 381 EYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGT 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1336 QSARHDCDLLREQFEEE----QEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEELEESKKKLAQ-------------R 1398
Cdd:PRK01156 461 TLGEEKSNHIINHYNEKksrlEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESaradledikikinE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1399 LQEAEEQIEAVNSKCASLEktkqrlQGEVEDLMIDVERANALAANLD-----KKQRNFDKVLAEWKQKYEEGQAELEGAQ 1473
Cdd:PRK01156 541 LKDKHDKYEEIKNRYKSLK------LEDLDSKRTSWLNALAVISLIDietnrSRSNEIKKQLNDLESRLQEIEIGFPDDK 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1474 KEARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGEtgksIHELEKSKKAVETEKAEIQTALEEAEGTL 1553
Cdd:PRK01156 615 SYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAE----IDSIIPDLKEITSRINDIEDNLKKSRKAL 690
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 288856329 1554 EHEESKI--LRVQLELNQVK-SEIDRKLAEKDEEIEQIKRNSQRITD 1597
Cdd:PRK01156 691 DDAKANRarLESTIEILRTRiNELSDRINDINETLESMKKIKKAIGD 737
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
882-1147 |
3.81e-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: 58.58 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 882 LLQEKNDLQLAVASESENLSDAEERCEGLIKskiQLEaKLKETTERLEDE-EEINAELTAKKRKLEDECSELKKDIDDLE 960
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDIINCKKQEERMLK---QIE-NLEEKEMNLRDElESVREEFIQKGDEVKCKLDKSEENARSIE 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 961 LTLAKVEKEKHATENKVKNLTEEMAAQDESIGKLTKEKKALQEAHQQTLDDLQAEEDKVNT----LTKSKTKLEQQVDDL 1036
Cdd:pfam05483 580 YEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKleleLASAKQKFEEIIDNY 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1037 EGSLE----QEKKLRMDLERAKRKLEGDLKLAQ-----------ESIMDLENDKQQSEEKLKKKDFETSQLLSKIEDEQS 1101
Cdd:pfam05483 660 QKEIEdkkiSEEKLLEEVEKAKAIADEAVKLQKeidkrcqhkiaEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSS 739
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 288856329 1102 LGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEE 1147
Cdd:pfam05483 740 AKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1452-1603 |
5.35e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 55.70 E-value: 5.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1452 DKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGETGKS------- 1524
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeyealq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1525 --IHELEKSKKAVETEKAEIQTALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEEIEQIKRNSQRITDSMQST 1602
Cdd:COG1579 96 keIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
|
.
gi 288856329 1603 L 1603
Cdd:COG1579 176 L 176
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1012-1333 |
8.19e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 8.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1012 LQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKL--AQESIMDLENDKQQseeklkkkdfet 1089
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVasAEREIAELEAELER------------ 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1090 sqllskIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQiemnkkR 1169
Cdd:COG4913 680 ------LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE------L 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1170 EAEFQKLRRDLEEstlqhEATAAALRKKQADSVAELGEQIDNL-QRVKQKLEKEKSEYKMEIDDLSSNMEAVAKakanLE 1248
Cdd:COG4913 748 RALLEERFAAALG-----DAVERELRENLEERIDALRARLNRAeEELERAMRAFNREWPAETADLDADLESLPE----YL 818
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1249 KMCRTLEDqlseikskndenlrqiNDLSAQRARLqtengefgrqleeKEALVSQLTRGKQAFTQQIEELKRQIEEEVKAK 1328
Cdd:COG4913 819 ALLDRLEE----------------DGLPEYEERF-------------KELLNENSIEFVADLLSKLRRAIREIKERIDPL 869
|
....*.
gi 288856329 1329 N-ALAH 1333
Cdd:COG4913 870 NdSLKR 875
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1479-1906 |
1.10e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.95 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1479 LSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAVETEKAEIQTALEEAEGTLEHEE- 1557
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLEl 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1558 ----------------SKILRVQLELNQVKSEIDRKLAEKDEEIEQIKRNSQRITDSMQS------TLDSEVRSRNDALR 1615
Cdd:TIGR04523 202 llsnlkkkiqknksleSQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEqnkikkQLSEKQKELEQNNK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1616 IKKKMEGDLNEMEIQLSHANRQAA-----EAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAMVERRNTLMQSEIEEL 1690
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1691 RAALEQTERgrkvaeqelvdaseRVGLLHSQNTSLLNTKKKLEADLVQIQSEVEDTVQEARNAEDKAKKAITDAAMMAEE 1770
Cdd:TIGR04523 362 QRELEEKQN--------------EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1771 LKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENLaMKGGKKQLQKLESRVRELESEVEAEQRRGADAVKGVRKYERRVK 1850
Cdd:TIGR04523 428 IERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNT-RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 288856329 1851 ELTYQTEEDKKNVNRLQDLVDKLQLKVKAYKRQSEEAEEQANSHLSKLRKVQHELE 1906
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKE 562
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1172-1697 |
1.29e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 56.75 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1172 EFQKLRRDLEESTLQHEATAAALRKKQaDSVAELGEQIDNlQRVKQKLEKEKSEYKMEIDDLSSnmeAVAKAKANLEKMC 1251
Cdd:pfam10174 131 ELFLLRKTLEEMELRIETQKQTLGARD-ESIKKLLEMLQS-KGLPKKSGEEDWERTRRIAEAEM---QLGHLEVLLDQKE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1252 RTLEDQLSEIKSKNdenlrQINDLSAQRARLQTengefgrQLEEKEALVSQLTRGKQAFTQQIEELKRQIEEEVKAKNAL 1331
Cdd:pfam10174 206 KENIHLREELHRRN-----QLQPDPAKTKALQT-------VIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEE 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1332 AHAVQSARHDCDLLREQFEEeqeakaeLQRGMSKANSEVAQWRTKYET------DAIQRTEELEESKKKLAQR------- 1398
Cdd:pfam10174 274 IKQMEVYKSHSKFMKNKIDQ-------LKQELSKKESELLALQTKLETltnqnsDCKQHIEVLKESLTAKEQRaailqte 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1399 -------LQEAEEQIEAVNSKCASLEKTKQRLQGEVEDL--MIDVE--RANALAA---NLDKKQRNFDKVLAEWKQKYEE 1464
Cdd:pfam10174 347 vdalrlrLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLkdMLDVKerKINVLQKkieNLQEQLRDKDKQLAGLKERVKS 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1465 GQ----------AELEGAQKEARSLSTELFKMKNSYE-ETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEKSKK 1533
Cdd:pfam10174 427 LQtdssntdtalTTLEEALSEKERIIERLKEQREREDrERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHAS 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1534 AVETEKAEIQTALEEAEGTLEH--EESKILRVQLELNQVKSEIDRKLAEKDEEIEQIKRNSQRITDSmQSTLDSEVRSRN 1611
Cdd:pfam10174 507 SLASSGLKKDSKLKSLEIAVEQkkEECSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEE-SGKAQAEVERLL 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1612 DALRI----KKKMEGDLNEMEiqlSHANRQAAEAQKQLRNVQA-----QLKDAQLhLDDAVRGQEDMKEQVAmverrntl 1682
Cdd:pfam10174 586 GILREveneKNDKDKKIAELE---SLTLRQMKEQNKKVANIKHgqqemKKKGAQL-LEEARRREDNLADNSQ-------- 653
|
570
....*....|....*
gi 288856329 1683 mQSEIEELRAALEQT 1697
Cdd:pfam10174 654 -QLQLEELMGALEKT 667
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1243-1869 |
1.46e-07 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 56.73 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1243 AKANLEKmcrtLEDQLSEIKSKNDENLRQIND----LSAQRARLQTENGEFGRQLE---EKEALVSQLTRGKQAFTQQIE 1315
Cdd:PRK10246 196 ARTELEK----LQAQASGVALLTPEQVQSLTAslqvLTDEEKQLLTAQQQQQQSLNwltRLDELQQEASRRQQALQQALA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1316 ELKrqieeevKAKNALA--HAVQSARHdcdlLREQFEEEQEAKAELQRGMSKANS------EVAQWRTKYETDAIQRTEE 1387
Cdd:PRK10246 272 AEE-------KAQPQLAalSLAQPARQ----LRPHWERIQEQSAALAHTRQQIEEvntrlqSTMALRARIRHHAAKQSAE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1388 LEESKKKLAQRLQEAE------EQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANALAAN-LDKKQRNFDKVLAEwkq 1460
Cdd:PRK10246 341 LQAQQQSLNTWLAEHDrfrqwnNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLNALPAItLTLTADEVAAALAQ--- 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1461 kyeegqaelegaQKEARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGET-------------GKSIHE 1527
Cdd:PRK10246 418 ------------HAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMrqrykektqqladVKTICE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1528 LEKSKKAVETEKAEIQTALE------------EAEGTLEHEESKILRVQLE--LNQVKSEIDRKLAEKDEEIEQIKRN-- 1591
Cdd:PRK10246 486 QEARIKDLEAQRAQLQAGQPcplcgstshpavEAYQALEPGVNQSRLDALEkeVKKLGEEGAALRGQLDALTKQLQRDes 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1592 -SQRITDSMQsTLDSEVRSRNDALRIKKKMEGDLN-------EMEIQLSHANR------QAAEAQKQLRNVQAQLKDAQL 1657
Cdd:PRK10246 566 eAQSLRQEEQ-ALTQQWQAVCASLNITLQPQDDIQpwldaqeEHERQLRLLSQrhelqgQIAAHNQQIIQYQQQIEQRQQ 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1658 HLDDAVRG-----QEDMKEQVAMVER------------RNTLMQSEIEELRAALEQTERGRKVAEQELVDASERVGLLHS 1720
Cdd:PRK10246 645 QLLTALAGyaltlPQEDEEASWLATRqqeaqswqqrqnELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHE 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1721 QNTSLLNTKKKLEADLVQIQSEVEDtVQEARNAEDKAKKAITDAAMMAEELKKEqdTSAHLERMKKNLEvtvkdlqHRLD 1800
Cdd:PRK10246 725 QCLSLHSQLQTLQQQDVLEAQRLQK-AQAQFDTALQASVFDDQQAFLAALLDEE--TLTQLEQLKQNLE-------NQRQ 794
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 288856329 1801 EAENLAMKGGKKQLQKLESRVRELESEVEAEQRRGADAV--KGVRKYERRVKELTYQTEEDKKNVNRLQDL 1869
Cdd:PRK10246 795 QAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQlaQQLRENTTRQGEIRQQLKQDADNRQQQQAL 865
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1305-1900 |
1.48e-07 |
|
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: 56.68 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1305 RGKQAFTQQIEELKRQIEEEVKAKNALAHAVQSARHDCDLLREQFEE-------EQEAKAELQrGMSKANSEVAQWRTKY 1377
Cdd:pfam07111 56 EGSQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMEldalavaEKAGQAEAE-GLRAALAGAEMVRKNL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1378 ETDAIQRTEELEE-SKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQ----GEVEDLMIDVERANALAANLDKKQRNFD 1452
Cdd:pfam07111 135 EEGSQRELEEIQRlHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkraGEAKQLAEAQKEAELLRKQLSKTQEELE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1453 K--VLAEWKQKYEEGQaelegAQKEARSLSTELFKmknsyEETLDQLETLKRENKNLQQEISDLTEQLGETGK--SIHEL 1528
Cdd:pfam07111 215 AqvTLVESLRKYVGEQ-----VPPEVHSQTWELER-----QELLDTMQHLQEDRADLQATVELLQVRVQSLTHmlALQEE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1529 EKSKKAVETEKAEIQTAlEEAEGTLEHEESKI--LRVQLELNQVK-SEIDRKLAEKDEEI-EQIKRNSQRITDSMQSTLD 1604
Cdd:pfam07111 285 ELTRKIQPSDSLEPEFP-KKCRSLLNRWREKVfaLMVQLKAQDLEhRDSVKQLRGQVAELqEQVTSQSQEQAILQRALQD 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1605 SEVRSRNDALRIkKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAMVERRNTLMQ 1684
Cdd:pfam07111 364 KAAEVEVERMSA-KGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAV 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1685 SEIEELRAALeqterGRKVAEQEL-------------VDASERVGLLHsqntsLLNTKKKLEADLVQIQSEVEDTVQEAR 1751
Cdd:pfam07111 443 RKVHTIKGLM-----ARKVALAQLrqescpppppappVDADLSLELEQ-----LREERNRLDAELQLSAHLIQQEVGRAR 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1752 NAEDKAKKAITDAAMMAE-ELKKEQDTsahLERMKKNLEVTVKDLQHRLDEAENLAMKGGKKQ----------LQKLESR 1820
Cdd:pfam07111 513 EQGEAERQQLSEVAQQLEqELQRAQES---LASVGQQLEVARQGQQESTEEAASLRQELTQQQeiygqalqekVAEVETR 589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1821 VRELESEVEAE----QRRGADAVKGVRKYERRVKeltyQTEEDKKNVNRLQDLVDKLQLKVKAykRQSEEAEEQANSHLS 1896
Cdd:pfam07111 590 LREQLSDTKRRlneaRREQAKAVVSLRQIQHRAT----QEKERNQELRRLQDEARKEEGQRLA--RRVQELERDKNLMLA 663
|
....
gi 288856329 1897 KLRK 1900
Cdd:pfam07111 664 TLQQ 667
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
971-1201 |
1.51e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 971 HATENKVKNLTEEMAAQDESIGKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSL----EQEKKL 1046
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaeleKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1047 RMDLERAKRKLEGDLKLAQESimdlendKQQSEEK--LKKKDFETS----QLLSKIEDE-QSLGAQLQKKIKELQARIEE 1119
Cdd:COG4942 96 RAELEAQKEELAELLRALYRL-------GRQPPLAllLSPEDFLDAvrrlQYLKYLAPArREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1120 LEEEIEAERAARAKVEKQRADLSRELEEISERLEEAggatAAQIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQA 1199
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARL----EKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
..
gi 288856329 1200 DS 1201
Cdd:COG4942 245 AA 246
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1453-1657 |
1.67e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.56 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1453 KVLAEWKQKYEEGQAEL--EGAQKEARSLSTELFKMKNSYEETLDQLETLKRENK--NLQQEISDLTEQLGETGKSIHEL 1528
Cdd:COG3206 152 AVANALAEAYLEQNLELrrEEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1529 EKSKKAVETEKAEIQTALEEAEGTLE--HEESKILRVQLELNQVKSEIDRKLA----------EKDEEIEQIKRNSQRIT 1596
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPelLQSPVIQQLRAQLAELEAELAELSArytpnhpdviALRAQIAALRAQLQQEA 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 288856329 1597 DSMQSTLDSEV---RSRNDALR-----IKKKMEgDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQL 1657
Cdd:COG3206 312 QRILASLEAELealQAREASLQaqlaqLEARLA-ELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
977-1447 |
1.73e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 977 VKNLTEEMAAQDESIGKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEKKLRMDLERAKRK 1056
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1057 LEgdlklaqesimdLENDKQQSEEKLKKKDFETSQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAArakVEK 1136
Cdd:COG4717 128 LP------------LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA---TEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1137 QRADLSRELEEISERLEEAGGATaaqiemnKKREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQIDNLQRVK 1216
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEEL-------EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1217 QKLEKEKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDENLRQINDLSAQRARLQTENGEFGRQLEEK 1296
Cdd:COG4717 266 GSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1297 EALVSQLTRGKQAFTQQIEELKRQIEEEVKAKNALAHAVQSARHDCDLLREqFEEEQEAKAELQRGMSKANSEVAQWRTK 1376
Cdd:COG4717 346 IEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEA 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 288856329 1377 YETDAI-QRTEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKtkqrlQGEVEDLMIDVERANALAANLDKK 1447
Cdd:COG4717 425 LDEEELeEELEELEEELEELEEELEELREELAELEAELEQLEE-----DGELAELLQELEELKAELRELAEE 491
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
912-1270 |
1.85e-07 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 56.30 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 912 KSKIQLEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDD-LELTLAKVE-----------KEKHATENKVKN 979
Cdd:pfam09731 86 KKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEvLKEAISKAEsatavakeakdDAIQAVKAHTDS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 980 LTEEMAAQDESIGKLTKEKKALQEAHQQTLDDLQAEEDKVNTlTKSKTKLEQQVDDLEGSLEQEKKLRMDLERAkRKLEG 1059
Cdd:pfam09731 166 LKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEE-EAAPPLLDAAPETPPKLPEHLDNVEEKVEKA-QSLAK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1060 DLKLAQESIMDLENDKQQSEEKL---------KKKDFETSQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEieaeraa 1130
Cdd:pfam09731 244 LVDQYKELVASERIVFQQELVSIfpdiipvlkEDNLLSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHIER------- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1131 raKVEKQRADLSRELEEISERLEEAGGATAAQIEmnKKREAEFQKLRRDLEES---TLQHEATAAALRKKQADSVAELGE 1207
Cdd:pfam09731 317 --ALEKQKEELDKLAEELSARLEEVRAADEAQLR--LEFEREREEIRESYEEKlrtELERQAEAHEEHLKDVLVEQEIEL 392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 288856329 1208 QIDNLQRVKQKLEKEKSEYKmeiddlssnmEAVAKAKANLekmcRTLEDQLSEIKSKNDENLR 1270
Cdd:pfam09731 393 QREFLQDIKEKVEEERAGRL----------LKLNELLANL----KGLEKATSSHSEVEDENRK 441
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1486-1922 |
1.91e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 56.00 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1486 MKNSYEETLDQLETLKRE--NKNLQQEISDLtEQLGETGKSIHELEKSKKA----VETEKAEIQTALEEAEGTLE----- 1554
Cdd:PRK04778 23 LRKRNYKRIDELEERKQEleNLPVNDELEKV-KKLNLTGQSEEKFEEWRQKwdeiVTNSLPDIEEQLFEAEELNDkfrfr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1555 HEESKILRVQLELNQVKSEIDRKLAEKDEEIEQIKRNSQRIT------DSMQSTLDSEVRSRNDALrikKKMEGDLNEME 1628
Cdd:PRK04778 102 KAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEqlkdlyRELRKSLLANRFSFGPAL---DELEKQLENLE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1629 IQLSHANRQAA-----EAQKQLRNVQAQLkdAQLhlddavrgQEDMKEQVAMVERRNTLMQSEIEELRAALEQ-TERGRK 1702
Cdd:PRK04778 179 EEFSQFVELTEsgdyvEAREILDQLEEEL--AAL--------EQIMEEIPELLKELQTELPDQLQELKAGYRElVEEGYH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1703 VAEQELVdasERVGLLHSQNTSLLNTKKKLEAD-----LVQIQSEVE---DTVQ---EARNAEDKAKKAITDAAMMAEEL 1771
Cdd:PRK04778 249 LDHLDIE---KEIQDLKEQIDENLALLEELDLDeaeekNEEIQERIDqlyDILErevKARKYVEKNSDTLPDFLEHAKEQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1772 KKEqdTSAHLERMKKNLEVT------VKDLQHRLDEAENL------AMKGGKKQLQKLESRVRELE---SEVEAEQRRGA 1836
Cdd:PRK04778 326 NKE--LKEEIDRVKQSYTLNeselesVRQLEKQLESLEKQydeiteRIAEQEIAYSELQEELEEILkqlEEIEKEQEKLS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1837 DAVKGVRKYERRVKELTYQTEEDKKNVNRlqdLVDKLQL-----KVKAYKRQSEEAEEQANSHLSKLR----KVQHELEE 1907
Cdd:PRK04778 404 EMLQGLRKDELEAREKLERYRNKLHEIKR---YLEKSNLpglpeDYLEMFFEVSDEIEALAEELEEKPinmeAVNRLLEE 480
|
490
....*....|....*
gi 288856329 1908 AEERADIAESQVNKL 1922
Cdd:PRK04778 481 ATEDVETLEEETEEL 495
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1427-1925 |
2.39e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.06 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1427 VEDLMIDVERANALAANLDKKQRNFDKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKM------KNSYEETLDQLETL 1500
Cdd:PRK01156 185 IDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELssledmKNRYESEIKTAESD 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1501 KRENKNLQQEISDLTEQLGETGKS---------------IHELEKSKKAVETEKAEIQT--ALEEAEGTLEHEESKILRV 1563
Cdd:PRK01156 265 LSMELEKNNYYKELEERHMKIINDpvyknrnyindyfkyKNDIENKKQILSNIDAEINKyhAIIKKLSVLQKDYNDYIKK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1564 QLELNQVKSEIDrklaekdeEIEQIKRNSQRITDSMQSTLDSEVRSRNDALRIKKKMEGDLNEMEIQLSHANRQAAEAQK 1643
Cdd:PRK01156 345 KSRYDDLNNQIL--------ELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINV 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1644 QLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAMVERRN-------TLMQSEIEELR-----------AALEQTERGRKVAE 1705
Cdd:PRK01156 417 KLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgtTLGEEKSNHIInhynekksrleEKIREIEIEVKDID 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1706 QELVDASERVGLLHSQNTSLLNTKKKLEADLVQIQSEVEDTVQEARNAEDKAKKAITDAAMMAEELKKEQDTSaHLERMK 1785
Cdd:PRK01156 497 EKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTS-WLNALA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1786 KNLEVTVKDLQHRLDEAenlamkggKKQLQKLESRVRELESEVEaeqrrgaDAVKGVRKYERRVKELTYQTEEDKKNVNR 1865
Cdd:PRK01156 576 VISLIDIETNRSRSNEI--------KKQLNDLESRLQEIEIGFP-------DDKSYIDKSIREIENEANNLNNKYNEIQE 640
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 288856329 1866 LQDLVDKLQLKVKAYKRQS---EEAEEQANSHLSKLRKVQHELEEAEERADIAESQVNKLRAK 1925
Cdd:PRK01156 641 NKILIEKLRGKIDNYKKQIaeiDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLEST 703
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
836-1264 |
2.79e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 836 YKIKPLLKSAETEKELATMKEDFVKCKEDLAKAEAKKKELE---------EKMVALLQEKNDLQLAVASESENLSDAEER 906
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEelkkklkelEKRLEELEERHELYEEAKAKKEELERLKKR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 907 CEGLIKSKIqlEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLE-----LTLAKVEKEKHATEN------ 975
Cdd:PRK03918 381 LTGLTPEKL--EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkCPVCGRELTEEHRKElleeyt 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 976 -KVKNLTEEMAAQDESIGKLTKEKKALQEA---------HQQTLDDLQAEEDKVNTLTKSktKLEQQVDDLEGSLEQEKK 1045
Cdd:PRK03918 459 aELKRIEKELKEIEEKERKLRKELRELEKVlkkeselikLKELAEQLKELEEKLKKYNLE--ELEKKAEEYEKLKEKLIK 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1046 LRMDLERAKRKLegdlklaqESIMDLENDKQQSEEKLKKKDFETSQLLSKIEDEQ-SLGAQLQKKIKELQARIEELEEEI 1124
Cdd:PRK03918 537 LKGEIKSLKKEL--------EKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELK 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1125 EAERAARAKvEKQRADLSRELEEISERLEEAggataaqiemnkkrEAEFQKLRRDLEEstLQHEATAAALRKKQaDSVAE 1204
Cdd:PRK03918 609 DAEKELERE-EKELKKLEEELDKAFEELAET--------------EKRLEELRKELEE--LEKKYSEEEYEELR-EEYLE 670
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1205 LGEQIDNLQRVKQKLEKEKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLEDqLSEIKSK 1264
Cdd:PRK03918 671 LSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALER-VEELREK 729
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
841-1098 |
2.80e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 841 LLKSAETEKELATMKEDFVKCKEDLAKAEAKK--------KELEEKMVALLQEKNDLQLAVASE-----SENLSDAEERC 907
Cdd:TIGR02169 728 LEQEEEKLKERLEELEEDLSSLEQEIENVKSElkeleariEELEEDLHKLEEALNDLEARLSHSripeiQAELSKLEEEV 807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 908 EGLIKSKIQLEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAQ 987
Cdd:TIGR02169 808 SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 988 DESIGKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEG-------------SLEQEKKLRMDLERAK 1054
Cdd:TIGR02169 888 KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDpkgedeeipeeelSLEDVQAELQRVEEEI 967
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 288856329 1055 RKLEGDLKLAQESIMDLENDKQQSEEKLKKKDFETSQLLSKIED 1098
Cdd:TIGR02169 968 RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1641-1910 |
2.84e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1641 AQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAMVERRNTLMQSEIEELRAALEQTERGRKVAEQELVDASERVGLLHS 1720
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1721 ---QNTSLLNTKKKLEADLVQIQSEVEDTVQEARNAEDKAKKAitdaammaEELKKEQDTSAHLERMKKNLEVtvkdlqh 1797
Cdd:PRK03918 243 lekELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL--------KELKEKAEEYIKLSEFYEEYLD------- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1798 rldeaenlamkgGKKQLQKLESRVRELESEVEAEQRRGADAVKGVRKYERRVKELTYQTEEDKKNVNRLQDLVDKLQLKV 1877
Cdd:PRK03918 308 ------------ELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELE 375
|
250 260 270
....*....|....*....|....*....|...
gi 288856329 1878 KAYKRQSEEAEEQANSHLSKLRKVQHELEEAEE 1910
Cdd:PRK03918 376 RLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS 408
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1621-1937 |
4.38e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 4.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1621 EGDLNEMEIQLSHANRQAAEAQ-KQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAMVERRNTLMQSEIEELRAALEQTER 1699
Cdd:PTZ00121 1044 EKDIIDEDIDGNHEGKAEAKAHvGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKK 1123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1700 GRKVAEQELVDASERVgllhsqnTSLLNTKKKLEADLVQIQSEVEDT--VQEARNAED-----KAKKAITdaAMMAEELK 1772
Cdd:PTZ00121 1124 AEDARKAEEARKAEDA-------RKAEEARKAEDAKRVEIARKAEDArkAEEARKAEDakkaeAARKAEE--VRKAEELR 1194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1773 KEQDTSA-----------HLERMKKNLEVTVKDLQHRLDEAENLAMKGGKKQLQKLESRVRELESEVEAEQRRGADAVKG 1841
Cdd:PTZ00121 1195 KAEDARKaeaarkaeeerKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA 1274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1842 VRKyeRRVKELTYQTEEDKKNVNRLQDLVDKL-QLKVKAY-KRQSEEAEEQANSHLSKLRKVQHELEEAEERADIAESQV 1919
Cdd:PTZ00121 1275 EEA--RKADELKKAEEKKKADEAKKAEEKKKAdEAKKKAEeAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEA 1352
|
330
....*....|....*...
gi 288856329 1920 NKLRAKSRDSGKGKDAAE 1937
Cdd:PTZ00121 1353 EAAADEAEAAEEKAEAAE 1370
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1248-1494 |
5.92e-07 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 54.47 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1248 EKMCRtLEDQLSEIKS------KNDENLR-QINDLSAQRARLQTENGEFGRQLEEKEALVSQLTRGKQAFTQQIEELKRQ 1320
Cdd:pfam09726 395 DALVR-LEQDIKKLKAelqasrQTEQELRsQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKR 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1321 IEEEVKAKNALAHAVQSARHdcdllREQFEEEQEAKAELQRGMSKANSevaqwrtkyeTDAI-QRTEELEESKKKLAQRL 1399
Cdd:pfam09726 474 LKAEQEARASAEKQLAEEKK-----RKKEEEATAARAVALAAASRGEC----------TESLkQRKRELESEIKKLTHDI 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1400 QEAEEQIEAVNSKCASLEKTKQRlQGEVEDLMidveraNALAANLDKKQRNFDKVLAEWKQKYE------EGQAELEGAQ 1473
Cdd:pfam09726 539 KLKEEQIRELEIKVQELRKYKES-EKDTEVLM------SALSAMQDKNQHLENSLSAETRIKLDlfsalgDAKRQLEIAQ 611
|
250 260
....*....|....*....|.
gi 288856329 1474 KEARSLSTELFKMKNSYEETL 1494
Cdd:pfam09726 612 GQIYQKDQEIKDLKQKIAEVM 632
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1191-1923 |
6.75e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.57 E-value: 6.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1191 AAALRKKQADSVAELGEQIDNLQRVKQKLEKEK-------SEYKMEIDDLSSNMEAVAKAkanlEKMCRTLEDqLSEIKS 1263
Cdd:COG3096 287 ALELRRELFGARRQLAEEQYRLVEMARELEELSaresdleQDYQAASDHLNLVQTALRQQ----EKIERYQED-LEELTE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1264 KNDENLRQINDLSAQRARLQTEngeFGRQLEEKEALVSQLTRGKQAF-TQQIEELKRQieeevKAKNALahavQSARHDC 1342
Cdd:COG3096 362 RLEEQEEVVEEAAEQLAEAEAR---LEAAEEEVDSLKSQLADYQQALdVQQTRAIQYQ-----QAVQAL----EKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1343 ---DLLREQFEEEQEA-KAELQRG----------MSKANSEVAQWRTKYE-----TDAIQRTEELEESKKKLAQ--RLQE 1401
Cdd:COG3096 430 glpDLTPENAEDYLAAfRAKEQQAteevleleqkLSVADAARRQFEKAYElvckiAGEVERSQAWQTARELLRRyrSQQA 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1402 AEEQIEAVNSKCASLEKTKQRLQgevedlmidveRANALAANLDKKQR-------NFDKVLAEWKQKYEEGQAELEGAQK 1474
Cdd:COG3096 510 LAQRLQQLRAQLAELEQRLRQQQ-----------NAERLLEEFCQRIGqqldaaeELEELLAELEAQLEELEEQAAEAVE 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1475 EARSLstelfkmknsyEETLDQLETLKRENKN-------LQQEISDLTEQLGETGKSIHEL-EKSKKAVETEKaEIQTAL 1546
Cdd:COG3096 579 QRSEL-----------RQQLEQLRARIKELAArapawlaAQDALERLREQSGEALADSQEVtAAMQQLLERER-EATVER 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1547 EEAEGTLEHEESKILRVQL-------ELNQVK--------SEI-------------------------------DRKLAE 1580
Cdd:COG3096 647 DELAARKQALESQIERLSQpggaedpRLLALAerlggvllSEIyddvtledapyfsalygparhaivvpdlsavKEQLAG 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1581 KD---EEIEQIKRNSQRITDSMQSTLDSE----VRSRNDALRI----------KKKMEGDLNEMEIQLSHANRQAAEA-- 1641
Cdd:COG3096 727 LEdcpEDLYLIEGDPDSFDDSVFDAEELEdavvVKLSDRQWRYsrfpevplfgRAAREKRLEELRAERDELAEQYAKAsf 806
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1642 --QKQLRNVQAQLKDAQLHLDDAVrgQEDMKEQVAMVERRNTLMQSEIEELRAALEQtergrkvAEQELVDASERVGLLH 1719
Cdd:COG3096 807 dvQKLQRLHQAFSQFVGGHLAVAF--APDPEAELAALRQRRSELERELAQHRAQEQQ-------LRQQLDQLKEQLQLLN 877
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1720 SqntsLLNTKKKLEADlvqiqsEVEDTVQEARNAEDKAKKAitdaammAEELKKEQDTSAHLERMkknlevtVKDLQHRL 1799
Cdd:COG3096 878 K----LLPQANLLADE------TLADRLEELREELDAAQEA-------QAFIQQHGKALAQLEPL-------VAVLQSDP 933
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1800 DEAENLamkggKKQLQKLESRVRELeseveaeqRRGADAVKGVRKyerRVKELTYQTEEDKKNVNrlQDLVDKLQLKVKA 1879
Cdd:COG3096 934 EQFEQL-----QADYLQAKEQQRRL--------KQQIFALSEVVQ---RRPHFSYEDAVGLLGEN--SDLNEKLRARLEQ 995
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 288856329 1880 YKRQSEEAEEQANSHLSKLRKVQHELEEAEERADIAESQVNKLR 1923
Cdd:COG3096 996 AEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELE 1039
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1666-1899 |
7.26e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 7.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1666 QEDMKEQVAMVERRNTLMQSEIEELRAALEQTERgrKVA----EQELVDASERVGLLHSQNTSLLNTKKKLEADLVQIQS 1741
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEA--ALEefrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1742 EVeDTVQEARNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEV---TVKDLQHRLDEAEnlamkggkKQLQKLE 1818
Cdd:COG3206 241 RL-AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQIAALR--------AQLQQEA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1819 SRVR-ELESEVEAEQRRGADAVKGVRKYERRVKELTyqteEDKKNVNRLQDLVDKLQLKVKAYKRQSEEAEEQANSHLSK 1897
Cdd:COG3206 312 QRILaSLEAELEALQAREASLQAQLAQLEARLAELP----ELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGN 387
|
..
gi 288856329 1898 LR 1899
Cdd:COG3206 388 VR 389
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
875-1211 |
9.57e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 9.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 875 LEEKMVALLQEKNDLQLAVAsESENLSDAEERCEGLIKSKI---QLEAKLKETTERLEDEEEINAELtakkRKLEDECSE 951
Cdd:COG4913 622 LEEELAEAEERLEALEAELD-ALQERREALQRLAEYSWDEIdvaSAEREIAELEAELERLDASSDDL----AALEEQLEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 952 LKKDIDDLELTLAKVEKEKHATENKVKNLTEEmaaQDESIGKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKSKTKLEQ 1031
Cdd:COG4913 697 LEAELEELEEELDELKGEIGRLEKELEQAEEE---LDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1032 QVDDLEGSLEQ-EKKLRMDLERAKRKLEGDLKLAQESIMDLEndkqqseeklkkkDFEtsQLLSKIEDEQsLgAQLQKKI 1110
Cdd:COG4913 774 RIDALRARLNRaEEELERAMRAFNREWPAETADLDADLESLP-------------EYL--ALLDRLEEDG-L-PEYEERF 836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1111 KELQarieeleeeieaERAARAKVEKQRADLSRELEEISERLEEA---------GGATAAQIEMNKKREAEFQKLRRDLE 1181
Cdd:COG4913 837 KELL------------NENSIEFVADLLSKLRRAIREIKERIDPLndslkripfGPGRYLRLEARPRPDPEVREFRQELR 904
|
330 340 350
....*....|....*....|....*....|
gi 288856329 1182 ESTLQHEATAAALRKKQADSVAELGEQIDN 1211
Cdd:COG4913 905 AVTSGASLFDEELSEARFAALKRLIERLRS 934
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1086-1330 |
9.60e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 9.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1086 DFETSQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEaggataaqiem 1165
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE----------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1166 nkkREAEFQKLRRDLEESTLQHEATAAALrkkQADSVAELGEQIDNLQRVKQKLEKEKSEYKMEIDDLSSNMEAVAKAKA 1245
Cdd:COG3883 84 ---RREELGERARALYRSGGSVSYLDVLL---GSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1246 NLEKMCRTLEDQLSEIKSKNDENLRQINDLSAQRARLQTENGEFGRQLEEKEALVSQLTRGKQAFTQQIEELKRQIEEEV 1325
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
....*
gi 288856329 1326 KAKNA 1330
Cdd:COG3883 238 AAAAA 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
917-1405 |
1.21e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 917 LEAKLKETTERLEDEEEINAELTAKKRKLEDECSELK--------KDIDDLELTLAKVEKEKHATENKVKNLTEEMAAQD 988
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEaqirgnggDRLEQLEREIERLERELEERERRRARLEALLAALG 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 989 ESIGKLTKEKKALQEAHQQTLDDLQAEEDKVNT----LTKSKTKLEQQVDDLEG---SLEQEK--------KLRMDLERA 1053
Cdd:COG4913 373 LPLPASAEEFAALRAEAAALLEALEEELEALEEalaeAEAALRDLRRELRELEAeiaSLERRKsniparllALRDALAEA 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1054 KRKLEGDLKLAQE--SIMDLENDKQQSEEKL----------KKKDFetSQLLSKIEDEQsLGAQLQkkIKELQARIEELE 1121
Cdd:COG4913 453 LGLDEAELPFVGEliEVRPEEERWRGAIERVlggfaltllvPPEHY--AAALRWVNRLH-LRGRLV--YERVRTGLPDPE 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1122 EEIEAERAARAKVE----KQRADLSRELEEIS-----ERLEEAGGATAA-----QIEMNKKReaeFQKLRRDLEEST--L 1185
Cdd:COG4913 528 RPRLDPDSLAGKLDfkphPFRAWLEAELGRRFdyvcvDSPEELRRHPRAitragQVKGNGTR---HEKDDRRRIRSRyvL 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1186 QHEATA--AALRKKQA---DSVAELGEQIDNLQRVKQKLEKEKSEYKM--EIDDLSSNMEAVAKAKANLEKMCRTLE--- 1255
Cdd:COG4913 605 GFDNRAklAALEAELAeleEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERLDass 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1256 DQLSEIKSKNDENLRQINDLSAQRARLQTENGEFGRQLEEKEALVSQLTRGKQAFTQQIEELKRQIEEEVKAKNALAHAV 1335
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVE 764
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1336 QSARHDCDLLREQFEEEQE-AKAELQRGMSKANSE----VAQWRTKYET----DAI---QRTEELEESKKKLAQRLQEAE 1403
Cdd:COG4913 765 RELRENLEERIDALRARLNrAEEELERAMRAFNREwpaeTADLDADLESlpeyLALldrLEEDGLPEYEERFKELLNENS 844
|
..
gi 288856329 1404 EQ 1405
Cdd:COG4913 845 IE 846
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1267-1580 |
1.23e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 52.62 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1267 ENLRQINDLSA---QRAR-LQTENGEFGRQLEEKEALVS-QLTRGKQAFTQQIEELKRQIEEEVKAKnalahavqsarhd 1341
Cdd:pfam00038 4 EQLQELNDRLAsyiDKVRfLEQQNKLLETKISELRQKKGaEPSRLYSLYEKEIEDLRRQLDTLTVER------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1342 cdllreqfeeeqeAKAELQRGmsKANSEVAQWRTKYETDAIQRTeELEESKKKLAQRLQEA-------EEQIEAVNSKCA 1414
Cdd:pfam00038 71 -------------ARLQLELD--NLRLAAEDFRQKYEDELNLRT-SAENDLVGLRKDLDEAtlarvdlEAKIESLKEELA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1415 SLEKTKQ----RLQGEVEDLMIDVERANALAANLdkkqrnfDKVLAEWKQKYEEgQAELEGAQKEarslstelfkmknsy 1490
Cdd:pfam00038 135 FLKKNHEeevrELQAQVSDTQVNVEMDAARKLDL-------TSALAEIRAQYEE-IAAKNREEAE--------------- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1491 eetldqlETLKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAVETE-------KAEIQTALEEAEGTLEHE----ESK 1559
Cdd:pfam00038 192 -------EWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIElqslkkqKASLERQLAETEERYELQladyQEL 264
|
330 340
....*....|....*....|.
gi 288856329 1560 ILRVQLELNQVKSEIDRKLAE 1580
Cdd:pfam00038 265 ISELEAELQETRQEMARQLRE 285
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
884-1548 |
1.25e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 53.69 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 884 QEKNDLQLAVASE-SENLSDAEERCEGLIKSKIQLEAKLKETTERLEdeEEINAELTAKKRKLEDECSELKKDIDDLELT 962
Cdd:pfam12128 375 AKYNRRRSKIKEQnNRDIAGIKDKLAKIREARDRQLAVAEDDLQALE--SELREQLEAGKLEFNEEEYRLKSRLGELKLR 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 963 LAKVEKEKHATENKvKNLTEEMAAQDESIGKLTKEKKALQE-------AHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDD 1035
Cdd:pfam12128 453 LNQATATPELLLQL-ENFDERIERAREEQEAANAEVERLQSelrqarkRRDQASEALRQASRRLEERQSALDELELQLFP 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1036 LEGSLEQekklrmdlerakrKLEGDLKLAQESImdlenDKQQSEEKLKKKDFETSQLLSKIEDEQSL-GAQLQ-KKI--- 1110
Cdd:pfam12128 532 QAGTLLH-------------FLRKEAPDWEQSI-----GKVISPELLHRTDLDPEVWDGSVGGELNLyGVKLDlKRIdvp 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1111 ------KELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGAtaaqiemnkkreaeFQKLRRDLEEST 1184
Cdd:pfam12128 594 ewaaseEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTA--------------LKNARLDLRRLF 659
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1185 LQHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEYKMEIDDLSSnmEAVAKAKANLEKMCRTLEDQLSEIKSK 1264
Cdd:pfam12128 660 DEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKR--EARTEKQAYWQVVEGALDAQLALLKAA 737
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1265 NDEnlRQINdLSAQRARLQTENGEFGRQLEEKEALVSQLTRGKQAFTQQIEELKRQieeevkaknalAHAVQSARhdcDL 1344
Cdd:pfam12128 738 IAA--RRSG-AKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVR-----------RQEVLRYF---DW 800
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1345 LREQFEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEELEESKK---KLAQRLQEAEEQIEAVNSKCASL--EKT 1419
Cdd:pfam12128 801 YQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKaseKQQVRLSENLRGLRCEMSKLATLkeDAN 880
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1420 KQRLQGE-------VEDLMIDVERanaLAANLDKKQRNFDKVLAEwkqKYEEGQAEL-EGAQKEARSLSTELFKMKNsYE 1491
Cdd:pfam12128 881 SEQAQGSigerlaqLEDLKLKRDY---LSESVKKYVEHFKNVIAD---HSGSGLAETwESLREEDHYQNDKGIRLLD-YR 953
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 288856329 1492 ETLDQLETLKreNKNLQQEISDLTEQLGETGKSIHE----LEKSKKAVETEKAEIQTALEE 1548
Cdd:pfam12128 954 KLVPYLEQWF--DVRVPQSIMVLREQVSILGVDLTEfydvLADFDRRIASFSRELQREVGE 1012
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
964-1661 |
1.26e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 53.65 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 964 AKVEKEK-HATENKVKNLTEEMAAQ-DESIGKLTKEKKAL---QEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEG 1038
Cdd:PRK10246 196 ARTELEKlQAQASGVALLTPEQVQSlTASLQVLTDEEKQLltaQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEK 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1039 SLEQEKKLrmDLERAKRKLEGDLKLAQESIMDLENDKQQSEEKlkkkdfeTSQLLSKIEDEQSLGAQLQKKIKELQArie 1118
Cdd:PRK10246 276 AQPQLAAL--SLAQPARQLRPHWERIQEQSAALAHTRQQIEEV-------NTRLQSTMALRARIRHHAAKQSAELQA--- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1119 eleeeieaeraarakvekQRADLSRELEEiSERLEEAGGATA---AQIEMNKKREAEFQKLRRDLEESTLQHEATAAALR 1195
Cdd:PRK10246 344 ------------------QQQSLNTWLAE-HDRFRQWNNELAgwrAQFSQQTSDREQLRQWQQQLTHAEQKLNALPAITL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1196 KKQADSVAELGEQIDNLQRVKQKLEKEKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDENLR----- 1270
Cdd:PRK10246 405 TLTADEVAAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADvktic 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1271 ----QINDLSAQRARLQTengefGRQLEEKEALVSQLTRGKQAFTQQIEELKR-QIEEEVKaknALAHAVQSARHDCDLL 1345
Cdd:PRK10246 485 eqeaRIKDLEAQRAQLQA-----GQPCPLCGSTSHPAVEAYQALEPGVNQSRLdALEKEVK---KLGEEGAALRGQLDAL 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1346 REQFeeeQEAKAELQRGMSKANSEVAQWRTKYETDAIQRT------------EELEESKKKLAQRLQ---EAEEQIEAVN 1410
Cdd:PRK10246 557 TKQL---QRDESEAQSLRQEEQALTQQWQAVCASLNITLQpqddiqpwldaqEEHERQLRLLSQRHElqgQIAAHNQQII 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1411 SKCASLEKTKQRLQGEVEDLMIDVERANALAANLDKKQRNFdkvlAEWKQKYEEgQAELEGAQKEARSLSTELFKMKNSY 1490
Cdd:PRK10246 634 QYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLATRQQEA----QSWQQRQNE-LTALQNRIQQLTPLLETLPQSDDLP 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1491 EE----TLDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEKS-----KKAVETEKAEIQTALEEAEgTLEHEESKIL 1561
Cdd:PRK10246 709 HSeetvALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQfdtalQASVFDDQQAFLAALLDEE-TLTQLEQLKQ 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1562 RVQLELNQVKSeidrkLAEKDEeiEQIKRNSQRITDSMQSTLDSE-----VRSRNDALRIKKKMEGDLNEmeiQLshanR 1636
Cdd:PRK10246 788 NLENQRQQAQT-----LVTQTA--QALAQHQQHRPDGLDLTVTVEqiqqeLAQLAQQLRENTTRQGEIRQ---QL----K 853
|
730 740
....*....|....*....|....*
gi 288856329 1637 QAAEAQKQLRNVQAQLKDAQLHLDD 1661
Cdd:PRK10246 854 QDADNRQQQQALMQQIAQATQQVED 878
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1040-1493 |
1.33e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1040 LEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSEEKLKKKDfetsQLLSKIEDEQSLgAQLQKKIKELQARIEE 1119
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE----KLLQLLPLYQEL-EALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1120 LEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQA 1199
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1200 DSVAELgeqidNLQRVKQKLEKEKSEYK------------MEIDDLSSNMEAVAKAKANLekmcrtLEDQLSEIKSKNDE 1267
Cdd:COG4717 231 QLENEL-----EAAALEERLKEARLLLLiaaallallglgGSLLSLILTIAGVLFLVLGL------LALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1268 NLRQINDLSAQRARLQTENGEFGRQLEEKEALVSQLTRGKQAFTQQIEELKRQIEEEVKAKNALAHAVQSARHDCDLLRE 1347
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1348 QFEEEQE--AKAELQRGMSKANSEVAQWRTKYETDAIQRTEELE-ESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQ 1424
Cdd:COG4717 380 GVEDEEElrAALEQAEEYQELKEELEELEEQLEELLGELEELLEaLDEEELEEELEELEEELEELEEELEELREELAELE 459
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 288856329 1425 GEVEDLMIDVEranalaanldkkqrnfdkvLAEWKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEET 1493
Cdd:COG4717 460 AELEQLEEDGE-------------------LAELLQELEELKAELRELAEEWAALKLALELLEEAREEY 509
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1104-1339 |
1.46e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1104 AQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAggataaqiemnkkrEAEFQKLRRDLEES 1183
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL--------------EQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1184 TLQHEATAAALRKKQAdsvaELGEQIDNLQRVKQKLEKE---KSEYKMEIDDLSSNMEAVAKA-KANLEKMCRT---LED 1256
Cdd:COG4942 89 EKEIAELRAELEAQKE----ELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPArREQAEELRADlaeLAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1257 QLSEIKSKNDENLRQINDLSAQRARLQtengefgRQLEEKEALVSQLTRGKQAFTQQIEELKRQIEEEVKAKNALAHAVQ 1336
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALE-------ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
...
gi 288856329 1337 SAR 1339
Cdd:COG4942 238 AAA 240
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1294-1777 |
1.50e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1294 EEKEALVSQLTRGKQAFTQQIEELKRQIEEEvKAKNALAHAVQSARHDcdlLREQFEEEQEAKAELQRGMSKANSEVAQW 1373
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEA-EEKEEEYAELQEELEE---LEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1374 rtkyetDAIQRTEELEESKKKLAQRLQEAEEQIEAVnskcASLEKTKQRLQGEVEDLMIDVERANALAANLDKKQrnfdk 1453
Cdd:COG4717 129 ------PLYQELEALEAELAELPERLEELEERLEEL----RELEEELEELEAELAELQEELEELLEQLSLATEEE----- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1454 vLAEWKQKYEEGQAELEGAQKEARSLSTELfkmknsyeetldqlETLKRENKNL--QQEISDLTEQLGETGKS------I 1525
Cdd:COG4717 194 -LQDLAEELEELQQRLAELEEELEEAQEEL--------------EELEEELEQLenELEAAALEERLKEARLLlliaaaL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1526 HELEKSKKAVETEKAEIQTALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEEIEQIKRNSQRITDSmQSTLDS 1605
Cdd:COG4717 259 LALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLP-PDLSPE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1606 EVRSRNDALRIKKKMEGDLNEMEIQLSHANRQaAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAMVERR------ 1679
Cdd:COG4717 338 ELLELLDRIEELQELLREAEELEEELQLEELE-QEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQleellg 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1680 ---NTLMQSEIEELRAALEQTERGRKVAEQELVDASERVGLLHSQNTSLLNtkkklEADLVQIQSEVEDTVQEARNAEDK 1756
Cdd:COG4717 417 eleELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE-----DGELAELLQELEELKAELRELAEE 491
|
490 500
....*....|....*....|.
gi 288856329 1757 AKKAITDAAMMAEELKKEQDT 1777
Cdd:COG4717 492 WAALKLALELLEEAREEYREE 512
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1418-1898 |
1.83e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1418 KTKQRLQGEVEDLMIDVERANALAANLDKKQRNfdkvLAEWKQKYEEGQAELEGAQKEARSLSTELfkmknSYEETLDQL 1497
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEE----LEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1498 ETLKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAVETEKAEIQTALEEAEGTLEHEESKILRVQLELNQVKSEIDRK 1577
Cdd:COG4717 135 EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1578 LAEKDEEIEQIKRNSQRITDSMQSTLDSEVRSRNDALRIkkkmegDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQL 1657
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL------IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1658 HLDDAVRGQEDMKEQVAMVERRNTLMQSEIEELRAALEQTERGRKVAEQELVDASERVGLLHSQNTSLLNTKKklEADLV 1737
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE--ELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1738 QIQSEVEDTVQEArNAEDKAkkAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENlamkggKKQLQKL 1817
Cdd:COG4717 367 ELEQEIAALLAEA-GVEDEE--ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL------EEELEEL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1818 ESRVRELESEVEAEQRRGADAVKGVRKYE--RRVKELTYQTEEDKKNVNRLQDLVDKLQLKVKAYKRQSEEAEE------ 1889
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREerlppv 517
|
490
....*....|.
gi 288856329 1890 --QANSHLSKL 1898
Cdd:COG4717 518 leRASEYFSRL 528
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
944-1611 |
2.25e-06 |
|
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: 53.13 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 944 KLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAQDESIGKLTKEKKALQ--EAHQQTLDDLQAEEDKVNT 1021
Cdd:TIGR01612 1108 KYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDdpEEIEKKIENIVTKIDKKKN 1187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1022 LTKSKTKLEQQVDDLEG---SLEQEKKLRMD------------LERAKRKLEGDLKLAQESIMDLENDKQQSEEklkkkd 1086
Cdd:TIGR01612 1188 IYDEIKKLLNEIAEIEKdktSLEEVKGINLSygknlgklflekIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPE------ 1261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1087 fetsqllskIEDEQSLGAQLQKKIKELQARIEeleeeieaeraaraKVEKQRADLSRELEEISERLEEAggataAQIEMN 1166
Cdd:TIGR01612 1262 ---------IENEMGIEMDIKAEMETFNISHD--------------DDKDHHIISKKHDENISDIREKS-----LKIIED 1313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1167 KKREAEFQKLRRDLEESTLQHEataaalrKKQADSVAELGE-----QIDNLQRVKQKLEKEKsEYKMEIDDLSSNmeaVA 1241
Cdd:TIGR01612 1314 FSEESDINDIKKELQKNLLDAQ-------KHNSDINLYLNEianiyNILKLNKIKKIIDEVK-EYTKEIEENNKN---IK 1382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1242 KAKANLEKMCRTLED--QLSEIKSKN---------DENLRQINDLSAQRARLQTENGEFGRQLEEKEALVSQLTRgkqaf 1310
Cdd:TIGR01612 1383 DELDKSEKLIKKIKDdiNLEECKSKIestlddkdiDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFK----- 1457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1311 TQQIEELKRQIEEEVKAKNAlahavqSARHDCDLlreqfeeeqeakAELQRGMSKANsevaqwrtKYETDAIQRTEELEE 1390
Cdd:TIGR01612 1458 NIEMADNKSQHILKIKKDNA------TNDHDFNI------------NELKEHIDKSK--------GCKDEADKNAKAIEK 1511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1391 SKKKLAQRLQEAEEQIE-----AVNSKCASLEKTKQRLQGEVEDLMIDVERANALAANLDKKQRNFDKVLAEWKQKYEEG 1465
Cdd:TIGR01612 1512 NKELFEQYKKDVTELLNkysalAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKS 1591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1466 QAELEGAQKEARSLSTELFKMKNSYEETLDQLetlkRENKNLQQEISDLT-----EQLGETGKSIHELEKSKKAVETEKA 1540
Cdd:TIGR01612 1592 NKAAIDIQLSLENFENKFLKISDIKKKINDCL----KETESIEKKISSFSidsqdTELKENGDNLNSLQEFLESLKDQKK 1667
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 288856329 1541 EIqtalEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEEIEQIKRNS-QRITDSMQSTLDSEVRSRN 1611
Cdd:TIGR01612 1668 NI----EDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKEEiESIKELIEPTIENLISSFN 1735
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1313-1553 |
3.00e-06 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 50.87 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1313 QIEELKRQIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVaqwrtkyeTDAIQRTEELEESK 1392
Cdd:pfam06008 20 NLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAES--------ERTLGHAKELAEAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1393 KKLAQRLQEAEEQIEAVNSKCASL-EKTKQRLQGEVEDLMIDVEranalAANLDKKQRNFDKVLAEWKQKYEEGQAELEG 1471
Cdd:pfam06008 92 KNLIDNIKEINEKVATLGENDFALpSSDLSRMLAEAQRMLGEIR-----SRDFGTQLQNAEAELKAAQDLLSRIQTWFQS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1472 AQKEARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLteqLGETGKSIHELEKSKKAVETEKAEIQTALEEAEG 1551
Cdd:pfam06008 167 PQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRL---NLANQANLREFQRKKEEVSEQKNQLEETLKTARD 243
|
..
gi 288856329 1552 TL 1553
Cdd:pfam06008 244 SL 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1479-1715 |
3.20e-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: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1479 LSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAVETEKAEIQTALEEAEGTLEhees 1558
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1559 kilrvqlELNQVKSEIDRKLAEKDEEIEQIKRNSQRITD--------SMQSTLDSEVRSR--NDALRIKKKMEGDLNEME 1628
Cdd:COG4942 87 -------ELEKEIAELRAELEAQKEELAELLRALYRLGRqpplalllSPEDFLDAVRRLQylKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1629 IQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMkeqVAMVERRNTLMQSEIEELRAALEQTERGRKVAEQEL 1708
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
....*..
gi 288856329 1709 VDASERV 1715
Cdd:COG4942 237 AAAAERT 243
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1621-1838 |
3.77e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1621 EGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAMVERRNTLMQSEIEELRAALEQT--- 1697
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1698 --ERGRKVAE----------QELVDASERVGLLHSQNTSLLNTKKKLEADLVQIQSEVEDTVQEARNAEDKAKKAITDaa 1765
Cdd:COG3883 95 lyRSGGSVSYldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE-- 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 288856329 1766 mmAEELKKEQdtsahlERMKKNLEVTVKDLQHRLDEAENLAMKGGKKQLQKLESRVRELESEVEAEQRRGADA 1838
Cdd:COG3883 173 --LEAQQAEQ------EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1105-1429 |
4.43e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 51.66 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1105 QLQKKIKELQARIEELEEEIEaeraaraKVEKQRADLSRELEEiSERLEEAGGATAAQIEMNKKREAEFQKL--RRDLEE 1182
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQE-------RLRQEKEEKAREVER-RRKLEEAEKARQAEMDRQAAIYAEQERMamEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1183 STLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEYKMEiddlssnMEAVAKAKANLEKMCRTLEDQLSEIK 1262
Cdd:pfam17380 351 ERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQE-------LEAARKVKILEEERQRKIQQQKVEME 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1263 S--KNDENLRQIndlsaqrarlqtengEFGRQLEEKEALVSQLTRGKQAFTQQIEELKRQIEEEVKAKNALAHAVQSARH 1340
Cdd:pfam17380 424 QirAEQEEARQR---------------EVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKR 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1341 DCDLLREQFEEEQEAKAE-----------LQRGMSKANSEVAQWRTKYETDAIQRTEELEESKKKLAQRLQEAEEQieav 1409
Cdd:pfam17380 489 AEEQRRKILEKELEERKQamieeerkrklLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEE---- 564
|
330 340
....*....|....*....|
gi 288856329 1410 NSKCASLEKTKQRLQGEVED 1429
Cdd:pfam17380 565 RSRLEAMEREREMMRQIVES 584
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
891-1105 |
4.73e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 891 LAVASESENLSDAEERCEGLIKSKIQLEAKLKETTERLED-EEEINaELTAKKRKLEDECSELKKDIDDLELTLAKVEKE 969
Cdd:COG3883 2 LALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDAlQAELE-ELNEEYNELQAELEALQAEIDKLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 970 KHATENKVKNLTEEMAAQDESIGKLTkekkALQEAhqQTLDDL-----------QAEEDKVNTLTKSKTKLEQQVDDLEG 1038
Cdd:COG3883 81 IEERREELGERARALYRSGGSVSYLD----VLLGS--ESFSDFldrlsalskiaDADADLLEELKADKAELEAKKAELEA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 288856329 1039 SLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSEEKLKKKDFETSQLLSKIEDEQSLGAQ 1105
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1164-1878 |
4.96e-06 |
|
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: 51.98 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1164 EMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQIDNlqRVKQKLEKEKSEYKMEIDDLSSNMEAVAKA 1243
Cdd:TIGR01612 700 DLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDIIVEIKKHIHG--EINKDLNKILEDFKNKEKELSNKINDYAKE 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1244 KANLEKMcrtlEDQLSEIKSK-NDE-NLRQINDLSAQRARLQTEngEFGRQLEEKEALVSQLtrgkqaftqqIEELKRQI 1321
Cdd:TIGR01612 778 KDELNKY----KSKISEIKNHyNDQiNIDNIKDEDAKQNYDKSK--EYIKTISIKEDEIFKI----------INEMKFMK 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1322 EEEVKAKNALAHAVQSARHDCDLLREQFEE-EQEAKAELqrgmskANSEVAQWRTKYeTDAIQRTEELEESKKKLAQR-- 1398
Cdd:TIGR01612 842 DDFLNKVDKFINFENNCKEKIDSEHEQFAElTNKIKAEI------SDDKLNDYEKKF-NDSKSLINEINKSIEEEYQNin 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1399 -LQEAEEQIEAVNSKCASLEK--TKQRLQGEVEDLMIDVERANALAANLDKKQrnFDKVLAEWKQKYEEGQAELEGAQKE 1475
Cdd:TIGR01612 915 tLKKVDEYIKICENTKESIEKfhNKQNILKEILNKNIDTIKESNLIEKSYKDK--FDNTLIDKINELDKAFKDASLNDYE 992
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1476 ARSlsTELFKMKNSYEETL---------DQLETLKRENKNLQQEISDLTEQLGETGKSIH--------ELEKS-KKAVET 1537
Cdd:TIGR01612 993 AKN--NELIKYFNDLKANLgknkenmlyHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHtsiyniidEIEKEiGKNIEL 1070
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1538 EKAEIqtaLEEAEGTLEHeeskilrvqleLNQVKSEIDRKLAEKDEEIEQIKRNSQ--RITDSMQsTLDSEVRSRNDAL- 1614
Cdd:TIGR01612 1071 LNKEI---LEEAEINITN-----------FNEIKEKLKHYNFDDFGKEENIKYADEinKIKDDIK-NLDQKIDHHIKALe 1135
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1615 RIKKKMEGDLNEMEIQLSHANRQAAEA--QKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAMVerrntlmqSEIEELRA 1692
Cdd:TIGR01612 1136 EIKKKSENYIDEIKAQINDLEDVADKAisNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEI--------AEIEKDKT 1207
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1693 ALEQTERGRKVAEQELVDAS-ERVGLLHSQNTSLLNTKKKLEADLVQIQSEVEDTVQEARNAEDkakkaiTDAAMMAEEL 1771
Cdd:TIGR01612 1208 SLEEVKGINLSYGKNLGKLFlEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMD------IKAEMETFNI 1281
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1772 KKEQDTSAHLERMKKNLEVT---VKDLQHRLDEAENLAMKGGKKQLQKLESRVRELESEVEAEQRRGAD-----AVKGVR 1843
Cdd:TIGR01612 1282 SHDDDKDHHIISKKHDENISdirEKSLKIIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANiynilKLNKIK 1361
|
730 740 750
....*....|....*....|....*....|....*
gi 288856329 1844 KYERRVKELTYQTEEDKKNVNRLQDLVDKLQLKVK 1878
Cdd:TIGR01612 1362 KIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIK 1396
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
927-1326 |
5.35e-06 |
|
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: 51.75 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 927 RLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAQDESIGKLTKEKKALQEAHQ 1006
Cdd:pfam10174 353 RLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSS 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1007 Q------TLDDLQAEEDKV-NTLTKSKTKLEQQVDDlegSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSE 1079
Cdd:pfam10174 433 NtdtaltTLEEALSEKERIiERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLA 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1080 EKLKKKDFETSQLLSKIEDEQSLGAQLQ---KKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEIsERLEEAG 1156
Cdd:pfam10174 510 SSGLKKDSKLKSLEIAVEQKKEECSKLEnqlKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEV-ERLLGIL 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1157 GATAAQIEMNKKREAEFQKLR----RDLEESTLQHEATAAALRKKQADSVAELGEQIDNLQRVKQK---------LEKEK 1223
Cdd:pfam10174 589 REVENEKNDKDKKIAELESLTlrqmKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQlqleelmgaLEKTR 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1224 SEYKMEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEI-KSKNDENLRQINDLSAQRARLQTENGEFGRQLEEkealVSQ 1302
Cdd:pfam10174 669 QELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEIlEMKQEALLAAISEKDANIALLELSSSKKKKTQEE----VMA 744
|
410 420
....*....|....*....|....
gi 288856329 1303 LTRGKQAFTQQieeLKRQIEEEVK 1326
Cdd:pfam10174 745 LKREKDRLVHQ---LKQQTQNRMK 765
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1003-1187 |
5.46e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.92 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1003 EAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSEEKL 1082
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1083 KK----KDFEtsQLLSKIEDEQSLGAQLQKKIKELQarieeleEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGA 1158
Cdd:COG1579 83 GNvrnnKEYE--ALQKEIESLKRRISDLEDEILELM-------ERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170 180
....*....|....*....|....*....
gi 288856329 1159 TAAQIEmnkKREAEFQKLRRDLEESTLQH 1187
Cdd:COG1579 154 LEAELE---ELEAEREELAAKIPPELLAL 179
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
650-677 |
5.91e-06 |
|
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: 48.50 E-value: 5.91e-06
10 20
....*....|....*....|....*...
gi 288856329 650 SSQFRENLGKLMTNLRSTHPHFVRCLIP 677
Cdd:cd01363 143 FEIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
893-1907 |
6.07e-06 |
|
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: 51.59 E-value: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 893 VASESENLSDAEERCEGLIKSKIqlEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKE--- 969
Cdd:TIGR01612 520 VPSKNIIGFDIDQNIKAKLYKEI--EAGLKESYELAKNWKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEiiy 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 970 ----KHATENKVKNLTEE-------------MAAQDESIGKLTKE-------------------KKALQEAHQQTLDDLQ 1013
Cdd:TIGR01612 598 inklKLELKEKIKNISDKneyikkaidlkkiIENNNAYIDELAKIspyqvpehlknkdkiystiKSELSKIYEDDIDALY 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1014 AE-------------EDKVNtLTKSKTKLEQQVDDLEGSLEQEKKLRM-DLERAKRKLEGDLKLAQESIM-DLENDKQQS 1078
Cdd:TIGR01612 678 NElssivkenaidntEDKAK-LDDLKSKIDKEYDKIQNMETATVELHLsNIENKKNELLDIIVEIKKHIHgEINKDLNKI 756
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1079 EEKLKKKDfetSQLLSKIEDEQSLGAQLQK---KIKELQARIEELEEEIEAERAARakveKQRADLSRELEEISERLEEA 1155
Cdd:TIGR01612 757 LEDFKNKE---KELSNKINDYAKEKDELNKyksKISEIKNHYNDQINIDNIKDEDA----KQNYDKSKEYIKTISIKEDE 829
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1156 GGATAAQIEMNK----KREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAElgeqiDNLQRVKQKLEKEKS---EYKM 1228
Cdd:TIGR01612 830 IFKIINEMKFMKddflNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEISD-----DKLNDYEKKFNDSKSlinEINK 904
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1229 EIDDLSSNMEAVAKAKANLeKMCRTLEDQLSEIKSKNDenlrQINDLSAQRARLQTENGEFGRQLEEK--EALVSQLTRG 1306
Cdd:TIGR01612 905 SIEEEYQNINTLKKVDEYI-KICENTKESIEKFHNKQN----ILKEILNKNIDTIKESNLIEKSYKDKfdNTLIDKINEL 979
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1307 KQAFTQ-QIEELKRQIEEEVKAKNALAHAVQSARHdcDLLREQFEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRT 1385
Cdd:TIGR01612 980 DKAFKDaSLNDYEAKNNELIKYFNDLKANLGKNKE--NMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNII 1057
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1386 EELEESKKKLAQRLQeaEEQIEAVNSKCASLEKTKQRLQG-EVEDLmidVERANALAANLDKKQRNFDKVLaewKQKYEE 1464
Cdd:TIGR01612 1058 DEIEKEIGKNIELLN--KEILEEAEINITNFNEIKEKLKHyNFDDF---GKEENIKYADEINKIKDDIKNL---DQKIDH 1129
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1465 GQAELEGAQKEARSLSTELFKMKNSYEETLDQleTLKREN-KNLQQEISDLTEQLgETGKSIHElekSKKAVETEKAEI- 1542
Cdd:TIGR01612 1130 HIKALEEIKKKSENYIDEIKAQINDLEDVADK--AISNDDpEEIEKKIENIVTKI-DKKKNIYD---EIKKLLNEIAEIe 1203
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1543 --QTALEEAEG-TLEHEES--KILRVQLELNQVKSEIDRKLAEKD-EEIEQIKRNSQRITDSMQSTLD--SEVRSRN--- 1611
Cdd:TIGR01612 1204 kdKTSLEEVKGiNLSYGKNlgKLFLEKIDEEKKKSEHMIKAMEAYiEDLDEIKEKSPEIENEMGIEMDikAEMETFNish 1283
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1612 ----DALRIKKKME---GDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAMVERRNtlMQ 1684
Cdd:TIGR01612 1284 dddkDHHIISKKHDeniSDIREKSLKIIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNILKLNK--IK 1361
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1685 SEIEELRAALEQTERGRKVAEQELvDASERVGLLHSQNTSLLNTKKKLEADLvqiqsEVEDTVQEARNAEDKAKKAITDA 1764
Cdd:TIGR01612 1362 KIIDEVKEYTKEIEENNKNIKDEL-DKSEKLIKKIKDDINLEECKSKIESTL-----DDKDIDECIKKIKELKNHILSEE 1435
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1765 AMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENLA---MKGGKKQLQKLESRVRELESEVEAEQRRGADAVKG 1841
Cdd:TIGR01612 1436 SNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNAtndHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKEL 1515
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 288856329 1842 VRKYERRVKEL--TYQTEEDKKNVNRLQDLVDKLQLKVKAYKRQSEEAEEQANSHLSKLRKVQHELEE 1907
Cdd:TIGR01612 1516 FEQYKKDVTELlnKYSALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIED 1583
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1106-1818 |
6.23e-06 |
|
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: 51.36 E-value: 6.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1106 LQKKIKELQARIEE-LEEEIEAERAARAKVEKQRADLSRELE-EISERLEEAGGATAAQIEMNKKREaEFQKLRRDLEEs 1183
Cdd:pfam10174 1 LQAQLRDLQRENELlRRELDIKESKLGSSMNSIKTFWSPELKkERALRKEEAARISVLKEQYRVTQE-ENQHLQLTIQA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1184 tLQHEATAaalrkkQADSVAELGEQIDNLQRVKQKLEKEKSEYKMEIDDLSSNMEAVAKakaNLEKMCRTLEDQLSEIKS 1263
Cdd:pfam10174 79 -LQDELRA------QRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAK---ELFLLRKTLEEMELRIET 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1264 KN------DENLRQINDL---SAQRARLQTENGEFGRQLEEKEALVSQLtrgkQAFTQQIEELKRQIEEEVKAKNALAHA 1334
Cdd:pfam10174 149 QKqtlgarDESIKKLLEMlqsKGLPKKSGEEDWERTRRIAEAEMQLGHL----EVLLDQKEKENIHLREELHRRNQLQPD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1335 VQSARhdcdLLREQFEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEELEE-------SK------KKLAQRLQE 1401
Cdd:pfam10174 225 PAKTK----ALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQmevykshSKfmknkiDQLKQELSK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1402 AEEQIEAVNSKCASLEK----TKQRLQGEVEDLMIDVERAN-------ALAANLDKKQRNFDKvlaewKQKYeegqaeLE 1470
Cdd:pfam10174 301 KESELLALQTKLETLTNqnsdCKQHIEVLKESLTAKEQRAAilqtevdALRLRLEEKESFLNK-----KTKQ------LQ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1471 GAQKEARSLSTELFKMKnsyeetlDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAVETEKAEIQTALEEAE 1550
Cdd:pfam10174 370 DLTEEKSTLAGEIRDLK-------DMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLE 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1551 GTLEHEESKILRvqlelnqVKSEIDRKLAEKDEEIEQIKRNSQ-----------RITDSMQSTLDSEVRSRNDALRIKKK 1619
Cdd:pfam10174 443 EALSEKERIIER-------LKEQREREDRERLEELESLKKENKdlkekvsalqpELTEKESSLIDLKEHASSLASSGLKK 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1620 mEGDLNEMEIQLSHANRQAAEAQKQLRNVQaqlkdaqlHLDDAVRGQEDMKEQVAMVERRNTLM-------QSEIEELRA 1692
Cdd:pfam10174 516 -DSKLKSLEIAVEQKKEECSKLENQLKKAH--------NAEEAVRTNPEINDRIRLLEQEVARYkeesgkaQAEVERLLG 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1693 ALEQTERGRKVAEQELVDASERVGLLH-SQNTSLLNTKKKLEADLVQIQSEVEDTVQEARNAEDKAKKAITDAAMMAEEL 1771
Cdd:pfam10174 587 ILREVENEKNDKDKKIAELESLTLRQMkEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEK 666
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 288856329 1772 KKEQdtsahLERMKKNLEVTVKDLQHRLDEAENLAMKGGKKQLQKLE 1818
Cdd:pfam10174 667 TRQE-----LDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILE 708
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1344-1763 |
6.34e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.05 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1344 LLREQFEEEQEAKAELQRGMSKANSEVAQWRTKYETDaiqrTEELEESKKKLAQRLQEAEEQIeavnskcaslektkQRL 1423
Cdd:pfam07888 31 LLQNRLEECLQERAELLQAQEAANRQREKEKERYKRD----REQWERQRRELESRVAELKEEL--------------RQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1424 QGEVEDLMIDVERANALAANLDKKQRNFDKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLETLKRE 1503
Cdd:pfam07888 93 REKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1504 NKNLQQEIsdlteqlgetgksihelekskKAVETEKAEIQTALEEAEGTLEHEESKILRVQLELNQVKSEID---RKLAE 1580
Cdd:pfam07888 173 RKQLQAKL---------------------QQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTtahRKEAE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1581 KDEEIEQIKRNSQRITDSMQST--LDSEVRSrndALRIKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQL-KDAQL 1657
Cdd:pfam07888 232 NEALLEELRSLQERLNASERKVegLGEELSS---MAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWaQERET 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1658 HLDDAVRGQEDMKEQVAMVERRNTLMQSEIEElRAALEqTERGRKvAEQELVDASERVGLLHSQNTSLLNTKKKLEadlv 1737
Cdd:pfam07888 309 LQQSAEADKDRIEKLSAELQRLEERLQEERME-REKLE-VELGRE-KDCNRVQLSESRRELQELKASLRVAQKEKE---- 381
|
410 420
....*....|....*....|....*.
gi 288856329 1738 QIQSEVEDTVQEARNAEDKAKKAITD 1763
Cdd:pfam07888 382 QLQAEKQELLEYIRQLEQRLETVADA 407
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
936-1233 |
1.06e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 936 AELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHAtENKVKNLTEE---MAAQDESIGKLTKEKKALQEAHQQtLDDL 1012
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREA-LQRLAEYSWDeidVASAEREIAELEAELERLDASSDD-LAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1013 QAEEDKvntltksktkLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSEEKLKKKDFETsql 1092
Cdd:COG4913 691 EEQLEE----------LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA--- 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1093 LSKIEDEQSLGAQLQKKIKELQarieeleeeieaeraarAKVEKQRADLSRELEEISERLEEAGGATAAQIEmnkkREAE 1172
Cdd:COG4913 758 ALGDAVERELRENLEERIDALR-----------------ARLNRAEEELERAMRAFNREWPAETADLDADLE----SLPE 816
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 288856329 1173 FQKLRRDLEESTL-QHEATAAALRKKQAdsvaelGEQIDNLQrvkQKLEKEKSEYKMEIDDL 1233
Cdd:COG4913 817 YLALLDRLEEDGLpEYEERFKELLNENS------IEFVADLL---SKLRRAIREIKERIDPL 869
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1675-1920 |
1.06e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1675 MVERRNTLmqSEIEELRAALEQTERgrkvAEQELVDASERVGLLhsqntsllntkkkleADLVQIQSEVEDTVQEARNAE 1754
Cdd:COG4913 217 MLEEPDTF--EAADALVEHFDDLER----AHEALEDAREQIELL---------------EPIRELAERYAAARERLAELE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1755 D-----KAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENLAMKGGKKQLQklesrvrELESEVE 1829
Cdd:COG4913 276 YlraalRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLE-------QLEREIE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1830 AEQRRGADAVKGVRKYERRVKELTYQTEEDKKNVNRLQDLVDKLqlkVKAYKRQSEEAEEQANSHLSKLRKVQHELEEAE 1909
Cdd:COG4913 349 RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL---LEALEEELEALEEALAEAEAALRDLRRELRELE 425
|
250
....*....|..
gi 288856329 1910 -ERADIAESQVN 1920
Cdd:COG4913 426 aEIASLERRKSN 437
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1351-1632 |
1.44e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 49.96 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1351 EEQEAKAELQRGMSKANSEVAQWRTKYETDAI----QRTEELEESKKKLAQRLQEAEEQIEavnskcaslEKTKQRLQGE 1426
Cdd:COG5185 239 QDPESELEDLAQTSDKLEKLVEQNTDLRLEKLgenaESSKRLNENANNLIKQFENTKEKIA---------EYTKSIDIKK 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1427 VEDLMIDVERANALAANLDKKQRNFDKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMKNS------YEETLDQLETL 1500
Cdd:COG5185 310 ATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELsksseeLDSFKDTIEST 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1501 KRENKNLQQEISDLTEQLGETgksiheLEKSKKAVETEKAEIQTALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAE 1580
Cdd:COG5185 390 KESLDEIPQNQRGYAQEILAT------LEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQS 463
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 288856329 1581 KDEEIEQIKRNSQRitdSMQSTLDSEVRSRNDALR-IKKKMEGDLNEMEIQLS 1632
Cdd:COG5185 464 RLEEAYDEINRSVR---SKKEDLNEELTQIESRVStLKATLEKLRAKLERQLE 513
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1554-1926 |
1.46e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1554 EHEESKILRVQLELNQVKSEIDRKLAEKDE-------EIEQIKRNSQRITDSMQSTLDSEVRSRNdALRIKKKME---GD 1623
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRRQLAAEQYrlvemarELAELNEAESDLEQDYQAASDHLNLVQT-ALRQQEKIEryqAD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1624 LNEMEIQLSHANRQAAEAQkqlrnvqaqlkdaqlhlddavrgqedmkEQVAMVERRNTLMQSEIEELRAALEQTergrkv 1703
Cdd:PRK04863 357 LEELEERLEEQNEVVEEAD----------------------------EQQEENEARAEAAEEEVDELKSQLADY------ 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1704 aeQELVDASERVGLLHSQNTSLLNTKKKLEADLVQIQSEVEDTVQEARNAEdkakKAITDAAMMAEElkKEQDTSAHLER 1783
Cdd:PRK04863 403 --QQALDVQQTRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKE----QEATEELLSLEQ--KLSVAQAAHSQ 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1784 MKKNLEV---------------TVKDLQHRLDEAENLAmkggkKQLQKLESRVRELESEVEAEQRrgadAVKGVRKYERR 1848
Cdd:PRK04863 475 FEQAYQLvrkiagevsrseawdVARELLRRLREQRHLA-----EQLQQLRMRLSELEQRLRQQQR----AERLLAEFCKR 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1849 VkELTYQTEEDkknvnrLQDLVDKLQLKVKAYKRQSEEAEEQANSHLSKLRKVQHELEEAEERADI---AESQVNKLRAK 1925
Cdd:PRK04863 546 L-GKNLDDEDE------LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLREQ 618
|
.
gi 288856329 1926 S 1926
Cdd:PRK04863 619 S 619
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
917-1341 |
1.69e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 49.30 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 917 LEAKLKETTERLEDEEEINAELTAKKRKLEDECSEL---KKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAQDESIGK 993
Cdd:pfam19220 8 LRVRLGEMADRLEDLRSLKADFSQLIEPIEAILRELpqaKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 994 LTKEKKALQEAHQQTldDLQAEEDKVNTLTKsktklEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLEN 1073
Cdd:pfam19220 88 LVARLAKLEAALREA--EAAKEELRIELRDK-----TAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1074 DKQQSEEKLKKKDFETSQLLSKIEDEQSLGAQLQKKIKELqarieeleeeieaeraarakvEKQRADLSRELEEISERLE 1153
Cdd:pfam19220 161 ELATARERLALLEQENRRLQALSEEQAAELAELTRRLAEL---------------------ETQLDATRARLRALEGQLA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1154 EAggataaqiemnkkrEAEFQKLRRDLEE--STLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKlekekseykmeid 1231
Cdd:pfam19220 220 AE--------------QAERERAEAQLEEavEAHRAERASLRMKLEALTARAAATEQLLAEARNQLR------------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1232 DLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDENLRQINDLSAQRARLQTENGEFGRQLEEKEAL------------ 1299
Cdd:pfam19220 273 DRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAAleraeeriasls 352
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 288856329 1300 --VSQLTR----GKQAFTQQIEELKRQIEEEvKAKNALAH-AVQSARHD 1341
Cdd:pfam19220 353 drIAELTKrfevERAALEQANRRLKEELQRE-RAERALAQgALEIARES 400
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1481-1674 |
1.73e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1481 TELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAVETEKAEIQTALEEAEGTLEheesKI 1560
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG----ER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1561 LRVQLELNQVKSEIDRKLAEKD--------EEIEQIKRNSQRITDSMQSTLDSEVRSRNDALRIKKKMEGDLNEMEIQLS 1632
Cdd:COG3883 92 ARALYRSGGSVSYLDVLLGSESfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 288856329 1633 HANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVA 1674
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1452-1644 |
1.78e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1452 DKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEISD-------LTEQLGETGKS 1524
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEaeaeieeRREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1525 -----------------------IHELEKSKKAVETEKAEI------QTALEEAEGTLEHEESKILRVQLELNQVKSEID 1575
Cdd:COG3883 95 lyrsggsvsyldvllgsesfsdfLDRLSALSKIADADADLLeelkadKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 288856329 1576 RKLAEKDEEIEQIKRNSQRITDSMQStLDSEVRSRNDALRIKKKMEGDLNEMEIQLSHANRQAAEAQKQ 1644
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAE-LEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1755-1928 |
2.00e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1755 DKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENLamkggkKQLQKLESRVRELESEVEAEQRR 1834
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL------LQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1835 GADAVKGVRKYERRVKELTYQTEEDKKNVNRLQDLVDKLQLkvkAYKRQSEEAEEQANSHLSKLRKVQHELEEAEERADI 1914
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL---ATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170
....*....|....
gi 288856329 1915 AESQVNKLRAKSRD 1928
Cdd:COG4717 225 LEEELEQLENELEA 238
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
911-1349 |
2.05e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.90 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 911 IKSKIQleaKLKETTERLEDEEEINAELTAKKRKLED---ECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAQ 987
Cdd:PRK01156 317 IDAEIN---KYHAIIKKLSVLQKDYNDYIKKKSRYDDlnnQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 988 DESIGKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSL------------------EQEKKLRMD 1049
Cdd:PRK01156 394 SEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMemlngqsvcpvcgttlgeEKSNHIINH 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1050 LERAKRKLEGDLKLAQESIMDLENDKQQseeKLKKKDFETSQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERA 1129
Cdd:PRK01156 474 YNEKKSRLEEKIREIEIEVKDIDEKIVD---LKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEE 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1130 ARAKVEkqradlSRELEEISERLEEAGGATAA----QIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAEL 1205
Cdd:PRK01156 551 IKNRYK------SLKLEDLDSKRTSWLNALAVisliDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREI 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1206 GEQIDNLQRVKQKLEkeksEYKMEIDDLSSNMEAVAKAKANLEkmcrTLEDQLSEIKSKndenLRQIND-LSAQRARLQT 1284
Cdd:PRK01156 625 ENEANNLNNKYNEIQ----ENKILIEKLRGKIDNYKKQIAEID----SIIPDLKEITSR----INDIEDnLKKSRKALDD 692
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 288856329 1285 ENGEfgrqLEEKEALVSQLTRGKQAFTQQIEELKRQIEEEVKAKNALAhavqsarhDCDLLREQF 1349
Cdd:PRK01156 693 AKAN----RARLESTIEILRTRINELSDRINDINETLESMKKIKKAIG--------DLKRLREAF 745
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1193-1449 |
2.07e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1193 ALRKKQADSVAE-LGEQIDNLQRVKQKLEKEKSEYKMEIDDLSSNMEAvakakanlekmcRTLEDQLSEIKSkndenlrQ 1271
Cdd:COG3206 167 ELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEA------------KLLLQQLSELES-------Q 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1272 INDLSAQRARLQTENGEFGRQLEEKEALVSQLTR--GKQAFTQQIEELKRQIEEEVKAKNALAHAVQSarhdcdlLREQF 1349
Cdd:COG3206 228 LAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIA-------LRAQI 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1350 EE-EQEAKAELQRGMSKANSEVAQwrtkyetdaiqrteeleeskkkLAQRLQEAEEQIEAVNSKCASLektkQRLQGEVE 1428
Cdd:COG3206 301 AAlRAQLQQEAQRILASLEAELEA----------------------LQAREASLQAQLAQLEARLAEL----PELEAELR 354
|
250 260
....*....|....*....|.
gi 288856329 1429 DLMIDVERANALAANLDKKQR 1449
Cdd:COG3206 355 RLEREVEVARELYESLLQRLE 375
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1327-1470 |
2.40e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.01 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1327 AKNALAHAVQSARHDCDLLREqfEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEELEESKKKLAQRlqeaEEQi 1406
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQK----EEN- 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 288856329 1407 eaVNSKCASLEKTKQRLQGEVEdlmidveranalaaNLDKKQRNFDKVLAEWKQKYEEGQAELE 1470
Cdd:PRK12704 98 --LDRKLELLEKREEELEKKEK--------------ELEQKQQELEKKEEELEELIEEQLQELE 145
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1486-1922 |
2.48e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 49.08 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1486 MKNSYEETLDQLETLKRE--NKNLQQEISDLtEQLGETGKSIHELEKSKK----AVETEKAEIQTALEEAEGTLE----H 1555
Cdd:pfam06160 4 LRKKIYKEIDELEERKNElmNLPVQEELSKV-KKLNLTGETQEKFEEWRKkwddIVTKSLPDIEELLFEAEELNDkyrfK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1556 EESKILR-VQLELNQVKSEIDRKLAEKDEEIEQIKRNSQRITDSMQS--TLDSEVRSRNDAL-RIKKKMEGDLNEMEIQL 1631
Cdd:pfam06160 83 KAKKALDeIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKyrELRKTLLANRFSYgPAIDELEKQLAEIEEEF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1632 SH-----ANRQAAEAQKQLRNVQAQLKDAQlhlddavrgqEDMKEQVAMVERRNTLMQSEIEELRAALEQ-TERGRKVA- 1704
Cdd:pfam06160 163 SQfeeltESGDYLEAREVLEKLEEETDALE----------ELMEDIPPLYEELKTELPDQLEELKEGYREmEEEGYALEh 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1705 ---EQELVDASERVgllhSQNTSLLNTK--KKLEADLVQIQSEVeDTVQEARNAEDKAKKaitdaammaeELKKEQDT-S 1778
Cdd:pfam06160 233 lnvDKEIQQLEEQL----EENLALLENLelDEAEEALEEIEERI-DQLYDLLEKEVDAKK----------YVEKNLPEiE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1779 AHLERMKKNLEVTVKDLQH-----RLDEAENLAMKGGKKQLQKLESRVRELE------------------------SEVE 1829
Cdd:pfam06160 298 DYLEHAEEQNKELKEELERvqqsyTLNENELERVRGLEKQLEELEKRYDEIVerleekevayselqeeleeileqlEEIE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1830 AEQRRGADAVKGVRKYERRVKELTYQTEEDKKNVNRlqdLVDKLQL-----KVKAYKRQSEEAEEQANSHLSKLR----K 1900
Cdd:pfam06160 378 EEQEEFKESLQSLRKDELEAREKLDEFKLELREIKR---LVEKSNLpglpeSYLDYFFDVSDEIEDLADELNEVPlnmdE 454
|
490 500
....*....|....*....|..
gi 288856329 1901 VQHELEEAEERADIAESQVNKL 1922
Cdd:pfam06160 455 VNRLLDEAQDDVDTLYEKTEEL 476
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
882-1083 |
2.57e-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: 49.25 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 882 LLQEKNDLQLAVASESENLSDAEERCEGLIKSKIQLEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLEL 961
Cdd:TIGR04523 445 LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKE 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 962 TLAKVEKEKHATENKVK----------------NLTEEMAAQDESIGKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKS 1025
Cdd:TIGR04523 525 KIEKLESEKKEKESKISdledelnkddfelkkeNLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE 604
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 288856329 1026 KTKLEQQVDDLEGSLEQEKK-------LRMDLERAKRKLEGDLKLAQESIMDLENDKQQSEEKLK 1083
Cdd:TIGR04523 605 IEEKEKKISSLEKELEKAKKeneklssIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIK 669
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1621-1930 |
2.99e-05 |
|
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: 49.40 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1621 EGDLNEMEIQLSHANRQAAEAQKQLRNVQaqLKDAQLhlddavrgqEDMKEQVAMVERRNTLMQSEIEELRAALEQTerg 1700
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELE--KKHQQL---------CEEKNALQEQLQAETELCAEAEEMRARLAAR--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1701 RKVAEQELVDASERVGLLHSQNTSLLNTKKKLEADLVQIQSEVEDtvQEARNAEDKAKKAITDAAM--MAEELKKEQDTS 1778
Cdd:pfam01576 70 KQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE--EEAARQKLQLEKVTTEAKIkkLEEDILLLEDQN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1779 AHLERMKKNLEVTVKDLQHRLDEAENLAmKGGKKQLQKLESRVRELESEVEAEQRRGADAVKGVRKYERRVKELTYQTEE 1858
Cdd:pfam01576 148 SKLSKERKLLEERISEFTSNLAEEEEKA-KSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAE 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 288856329 1859 DKKNVNRLQDLVDKLQLKVKAYKRQSEEAEEQANSHLSKLRKVQHELEEAEERADIAESQVNKLRAKSRDSG 1930
Cdd:pfam01576 227 LQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLG 298
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1418-1759 |
3.50e-05 |
|
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: 48.75 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1418 KTKQRLQGEVEDLMIDVERANALAANLDKKQRNFDKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLD-Q 1496
Cdd:pfam15964 300 QTIERLTKERDDLMSALVSVRSSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQKERLEKELAsQ 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1497 LETLKRENKNLQQEISDLTEQLGET----GKSIHELEKSKKAVETEKAEIQTALEEAEGTLEHEESKILRVQLELNQVKS 1572
Cdd:pfam15964 380 QEKRAQEKEALRKEMKKEREELGATmlalSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQLN 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1573 EIDRKLAEKDEEIEQIKRNSQRITDsmqsTLDSEVrsrndalrikKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQL 1652
Cdd:pfam15964 460 QTKMKKDEAEKEHREYRTKTGRQLE----IKDQEI----------EKLGLELSESKQRLEQAQQDAARAREECLKLTELL 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1653 KDA--QLHLDDAVRGQ------EDMKEQVAMVERRNTLMQSEIEELRAALEQTERgrkvaeqelvdasERVGLLHSQNTS 1724
Cdd:pfam15964 526 GESehQLHLTRLEKESiqqsfsNEAKAQALQAQQREQELTQKMQQMEAQHDKTVN-------------EQYSLLTSQNTF 592
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 288856329 1725 LLNTK-------KKLEADLVQIQSEVEDTVQEARNAEDKAKK 1759
Cdd:pfam15964 593 IAKLKeecctlaKKLEEITQKSRSEVEQLSQEKEYLQDRLEK 634
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
882-1113 |
3.63e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 49.13 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 882 LLQEKNDLQLAVASESENLSDAEERCEGLIKSKI-------QLEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKK 954
Cdd:PLN02939 161 ILTEKEALQGKINILEMRLSETDARIKLAAQEKIhveileeQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 955 DIDDLELTLAKVEKekhaTENKVKNLTEEMAAQDESIGKLTKEKKALQEAHQQtLDDLQAEE--DKVNTLTKSKTKLEQQ 1032
Cdd:PLN02939 241 DIQFLKAELIEVAE----TEERVFKLEKERSLLDASLRELESKFIVAQEDVSK-LSPLQYDCwwEKVENLQDLLDRATNQ 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1033 VDDLEGSLEQEKKLRMDLErakrKLEGDLKLAQES-----IMDLENDKQQS-EEKLKKKDFETsqlLSKIEDEQSLGAQL 1106
Cdd:PLN02939 316 VEKAALVLDQNQDLRDKVD----KLEASLKEANVSkfssyKVELLQQKLKLlEERLQASDHEI---HSYIQLYQESIKEF 388
|
....*..
gi 288856329 1107 QKKIKEL 1113
Cdd:PLN02939 389 QDTLSKL 395
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1346-1565 |
3.72e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1346 REQFEEE-QEAKAELQrgmsKANSEVAQWRTKYE-TDAIQRTEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRL 1423
Cdd:COG3206 177 LEFLEEQlPELRKELE----EAEAALEEFRQKNGlVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1424 QGEVEDLMidverANALAANLDKKQRNFDKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLD-QLETLKR 1502
Cdd:COG3206 253 PDALPELL-----QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEaELEALQA 327
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 288856329 1503 ENKNLQQEISDLTEQLGETGKSIHELEKSKKAVETEKAEIQTALEEAEGTLEHEESKILRVQL 1565
Cdd:COG3206 328 REASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRV 390
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
846-1114 |
5.25e-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: 48.48 E-value: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 846 ETEKELATMKEDFVKCKEDLAKAEAKKKELEEKMVALLQEKNDLQLAVASESENLSDAEERCEGLIKSKIQLEAKLKETT 925
Cdd:TIGR04523 367 EKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 926 ERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAQDESIGKLTKEKKALQEah 1005
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKE-- 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1006 qqtlddlqaeedKVNTLTKSKTKLEQQVDDLEGSLEQEK--KLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSEEKLK 1083
Cdd:TIGR04523 525 ------------KIEKLESEKKEKESKISDLEDELNKDDfeLKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID 592
|
250 260 270
....*....|....*....|....*....|.
gi 288856329 1084 KKDFETSQLLSKIEDEQSLGAQLQKKIKELQ 1114
Cdd:TIGR04523 593 QKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1463-1738 |
5.69e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.37 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1463 EEGQAELEGAQKeARSLSTELFKMKNSYEETLDQL---ETLKRENKNLQQEISDLTEQLGETGKsihELEKSKKAVETEK 1539
Cdd:PRK11281 39 ADVQAQLDALNK-QKLLEAEDKLVQQDLEQTLALLdkiDRQKEETEQLKQQLAQAPAKLRQAQA---ELEALKDDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1540 AEI--QTALEEAEGTLEHEESKILRVQLELNQVKSEI-------DRKLAEKDEEIEQIkrnsQRITDSMQSTLDSEVRSR 1610
Cdd:PRK11281 115 RETlsTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLvslqtqpERAQAALYANSQRL----QQIRNLLKGGKVGGKALR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1611 NDAlriKKKMEGDLNEMEIQLSHaNRQAAEAQKQLRNV-QAQlkdaqlhlddavrgQEDMKEQVAMVERRNTLMQSEIEE 1689
Cdd:PRK11281 191 PSQ---RVLLQAEQALLNAQNDL-QRKSLEGNTQLQDLlQKQ--------------RDYLTARIQRLEHQLQLLQEAINS 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 288856329 1690 LRaaLEQTErgRKVAEQELVDASERVG---LLHSQntslLNTKKKLEADLVQ 1738
Cdd:PRK11281 253 KR--LTLSE--KTVQEAQSQDEAARIQanpLVAQE----LEINLQLSQRLLK 296
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1200-1504 |
5.97e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1200 DSVAELGEQIDNLQRVKQKLEKEKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDENLRQINDLSAQR 1279
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1280 ARLQTENGEFGRQLEEKEALVSQLTRGKqaftQQIEELKRQIEEEVKaknalahAVQSARHDCDLLREQFEE--EQEAKA 1357
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAG----GSIDKLRKEIERLEW-------RQQTEVLSPEEEKELVEKikELEKEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1358 ELQRGMSKANSEVAQWRTKYETDAIQRtEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERA 1437
Cdd:COG1340 150 EKAKKALEKNEKLKELRAELKELRKEA-EEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADEL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 288856329 1438 NALAANLDKKQRNFDKVLAEWKQKYEEgqAELEGAQKEARSLSTELF-KMKNSYEETLDQLETLKREN 1504
Cdd:COG1340 229 HEEIIELQKELRELRKELKKLRKKQRA--LKREKEKEELEEKAEEIFeKLKKGEKLTTEELKLLQKSG 294
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1566-1788 |
6.01e-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: 47.45 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1566 ELNQVKSEIDRKLAEKDEEIEQIKRNSQRITDSMQStLDSEVRSRNDALRikkKMEGDLNEMEIQLSHANRQAAEAQKQL 1645
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA-LERRIAALARRIR---ALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1646 RNVQAQLKD------------------AQLHLDDAVRGQEDMKeqvAMVERRNTLMQsEIEELRAALEQTERGRKVAEQE 1707
Cdd:COG4942 100 EAQKEELAEllralyrlgrqpplalllSPEDFLDAVRRLQYLK---YLAPARREQAE-ELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1708 LVDASERVGLLHSQNTSLLNTKKKLEADLVQIQSEVEDTVQEARNAEDKAKKAItDAAMMAEELKKEQDTSAHLERMKKN 1787
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI-ARLEAEAAAAAERTPAAGFAALKGK 254
|
.
gi 288856329 1788 L 1788
Cdd:COG4942 255 L 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1692-1921 |
6.28e-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: 47.45 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1692 AALEQTERGRKVAEQELVDASERVGLLHSQNTSLLNTKKKLEADLVQIQSEVEDTVQEARNAEDKAKKAITDAAMMAEEL 1771
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1772 KKEQDTSAH----LERMKKNLEVTVKDLQHRLDEAENLAMKgGKKQLQKLESRVRELESEVEAEQRRGADAVKGVRKYER 1847
Cdd:COG4942 100 EAQKEELAEllraLYRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 288856329 1848 RVKELTYQTEEDKKNVNRLQDLVDKLQLKVKAYKRQSEEAEEQANSHLSKLRKVQHELEEAEERADIAESQVNK 1921
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1294-1588 |
7.45e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 47.61 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1294 EEKEALVSQLtRGKQAFtqQIEELKRQIEEEVKAKnalahavqsarhdcdlLREQFEEEQEAKAELQRGMSKANSEVaqw 1373
Cdd:PRK05771 16 SYKDEVLEAL-HELGVV--HIEDLKEELSNERLRK----------------LRSLLTKLSEALDKLRSYLPKLNPLR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1374 rtkyETDAIQRTEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLM------IDVERAN------ALA 1441
Cdd:PRK05771 74 ----EEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwgnfdLDLSLLLgfkyvsVFV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1442 ANLDKkqRNFDKVLAEWKQKYEEGQAELEG-------AQKEARSLSTELFKmKNSYEE-TLDQLETLKRENKNLQQEISD 1513
Cdd:PRK05771 150 GTVPE--DKLEELKLESDVENVEYISTDKGyvyvvvvVLKELSDEVEEELK-KLGFERlELEEEGTPSELIREIKEELEE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1514 LTEQLGETgksIHELEKSKKAVETekaEIQTALEEAEGTLEHEE--SKILR----VQLE-------LNQVKSEIDRKLAE 1580
Cdd:PRK05771 227 IEKERESL---LEELKELAKKYLE---ELLALYEYLEIELERAEalSKFLKtdktFAIEgwvpedrVKKLKELIDKATGG 300
|
330
....*....|....*.
gi 288856329 1581 K--------DEEIEQI 1588
Cdd:PRK05771 301 SayvefvepDEEEEEV 316
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1253-1409 |
7.80e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1253 TLEDQLSEIKSKNDENLRQINDLSAQRARLQTENGEFGRQLEEKEALVSQLTRGKQAFTQQIEELKRQIEEEVKAK--NA 1330
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEA 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 288856329 1331 LAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEELEESKKKLAQRLQEAEEQIEAV 1409
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1486-1922 |
8.21e-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: 48.02 E-value: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1486 MKNSYE--ETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAVETEK-------AEIQTALEEAEgtlehe 1556
Cdd:COG3096 274 MRHANErrELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYqaasdhlNLVQTALRQQE------ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1557 esKILRVQLELnqvkSEIDRKLAEKDEEIEQikRNSQRitdsmqstldSEVRSRNDAlrikkkMEGDLNEMEIQLshANR 1636
Cdd:COG3096 348 --KIERYQEDL----EELTERLEEQEEVVEE--AAEQL----------AEAEARLEA------AEEEVDSLKSQL--ADY 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1637 QAAEAQKQLRNVQAQlkdaqlhldDAVRGQEDMKEQVAMVERRNTLMQSEIEELRAALEQTERGRKVAEQELVDASERvg 1716
Cdd:COG3096 402 QQALDVQQTRAIQYQ---------QAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAA-- 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1717 llHSQNtsllntKKKLEAdLVQIQSEVEdtvqeARNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLevtvkdlq 1796
Cdd:COG3096 471 --RRQF------EKAYEL-VCKIAGEVE-----RSQAWQTARELLRRYRSQQALAQRLQQLRAQLAELEQRL-------- 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1797 HRLDEAENLAMKGGKKQLQKLESR--VRELESEVEAEQRR----GADAVKGVRKYERRVKELTYQTEEDKKNVNR---LQ 1867
Cdd:COG3096 529 RQQQNAERLLEEFCQRIGQQLDAAeeLEELLAELEAQLEEleeqAAEAVEQRSELRQQLEQLRARIKELAARAPAwlaAQ 608
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 288856329 1868 DLVDKLQLKVKAYKRQSEEAEEQANSHLSKLRKVQHELEEAEERADIAESQVNKL 1922
Cdd:COG3096 609 DALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERL 663
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1213-1585 |
9.96e-05 |
|
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: 47.33 E-value: 9.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1213 QRVKQKLEKEKSEYkmeiddLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDENLRQINDLSAQRA-RLQTENgefgr 1291
Cdd:pfam05667 242 KRKRTKLLKRIAEQ------LRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTeKLQFTN----- 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1292 qleEKEALVSQLTRGkqafTQQIEELKRQIEEEVKAknalahavqsarhdcdlLREQFEEEQEAKAELQRGMSKANSEVA 1371
Cdd:pfam05667 311 ---EAPAATSSPPTK----VETEEELQQQREEELEE-----------------LQEQLEDLESSIQELEKEIKKLESSIK 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1372 QwrTKYETDAIQRT-EELEES---KKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVED----LMIDVERANALAAN 1443
Cdd:pfam05667 367 Q--VEEELEELKEQnEELEKQykvKKKTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKhrvpLIEEYRALKEAKSN 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1444 -LDKKQRNFDKvLAEWKQKYEEGQAELegaqkearslstelfKMKnsyEETLDQLETlkrENKNLQQEI--SDLTEQLGE 1520
Cdd:pfam05667 445 kEDESQRKLEE-IKELREKIKEVAEEA---------------KQK---EELYKQLVA---EYERLPKDVsrSAYTRRILE 502
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 288856329 1521 TGKSIHElekskkavetEKAEIQTALEEAEGtleheeskilrVQLELNQVKSEIDRKLAEKDEEI 1585
Cdd:pfam05667 503 IVKNIKK----------QKEEITKILSDTKS-----------LQKEINSLTGKLDRTFTVTDELV 546
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1727-1928 |
1.00e-04 |
|
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: 46.68 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1727 NTKKKLEADLVQIQSEVEDTVQEARNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAEnla 1806
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1807 mkggkkqlQKLESRVRELESEVEAEQRRG--------------ADAVKGVRKYERRVKELTYQTEEDKKNVNRLQDLVDK 1872
Cdd:COG4942 97 --------AELEAQKEELAELLRALYRLGrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 288856329 1873 LQLKVKAYKRQSEEAEEQANSHLSKLRKVQHELEEAEERADIAESQVNKLRAKSRD 1928
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1633-1838 |
1.04e-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: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1633 HANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAMVERRNTLMQSEIEELRAALEQtergrkvAEQELVDAS 1712
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE-------AEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1713 ERVG--LLHSQNTSLLNTkkKLEA--------DLVQIQSEVEDTVQEARNAEDKAKKAITDAAMMAEELKKEQDTsahLE 1782
Cdd:COG3883 86 EELGerARALYRSGGSVS--YLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE---LE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 288856329 1783 RMKKNLEVTVKDLQHRLDEAENLaMKGGKKQLQKLESRVRELESEVEAEQRRGADA 1838
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEAL-LAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
882-1232 |
1.12e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 882 LLQEKNDLQLAVASESENLSDAEERCEGLIKSKIQLEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLEL 961
Cdd:COG4372 15 LFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 962 TLAKVEKEKHATENKVKNLTEEMAAQDESIGKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLE 1041
Cdd:COG4372 95 ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1042 QEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSEEKLKKKDFETSQLLSKIEDEQSLGAQLQKKIKELQARIEELE 1121
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1122 EEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQADS 1201
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAI 334
|
330 340 350
....*....|....*....|....*....|.
gi 288856329 1202 VAELGEQIDNLQRVKQKLEKEKSEYKMEIDD 1232
Cdd:COG4372 335 LLAELADLLQLLLVGLLDNDVLELLSKGAEA 365
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1579-1809 |
1.16e-04 |
|
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: 46.68 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1579 AEKDEEIEQIKRNSQRItDSMQSTLDSEVRSRNDALRIKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLH 1658
Cdd:COG4942 20 DAAAEAEAELEQLQQEI-AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1659 LDdavRGQEDMKEQVA---MVERRNTLM-------QSEIEELRAALEQTERGRKVAEQELVDASERvglLHSQNTSLLNT 1728
Cdd:COG4942 99 LE---AQKEELAELLRalyRLGRQPPLAlllspedFLDAVRRLQYLKYLAPARREQAEELRADLAE---LAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1729 KKKLEADLVQIQSEVEDTVQEARNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENLAMK 1808
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
.
gi 288856329 1809 G 1809
Cdd:COG4942 253 G 253
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1147-1414 |
1.20e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 47.25 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1147 EISERLEEAGGATAAqiemnKKR-EAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELgeqidnLQRVKQKLEKEKSE 1225
Cdd:PRK05035 437 EIRAIEQEKKKAEEA-----KARfEARQARLEREKAAREARHKKAAEARAAKDKDAVAAA------LARVKAKKAAATQP 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1226 YKMEIDDLSSNMEAVAKAKAnlekmcRTLEDQlseikskndenlrqindlsAQRARLQTENGEfgrqLEEKEALVSQLTR 1305
Cdd:PRK05035 506 IVIKAGARPDNSAVIAAREA------RKAQAR-------------------ARQAEKQAAAAA----DPKKAAVAAAIAR 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1306 GKQAFTQQIEELKRQIEEEVKAKNALAHAVqsARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRT 1385
Cdd:PRK05035 557 AKAKKAAQQAANAEAEEEVDPKKAAVAAAI--ARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQAN 634
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 288856329 1386 EELEES---------------KKKLAQRLQEAEEQIEAVNSKCA 1414
Cdd:PRK05035 635 AEPEEPvdprkaavaaaiaraKARKAAQQQANAEPEEAEDPKKA 678
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1748-1928 |
1.22e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1748 QEARNAED----KAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAEnlamkggkKQLQKLESRVRE 1823
Cdd:COG1196 207 RQAEKAERyrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELE--------AELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1824 LESEVEAEQRRGADAVKGVRKYERRVKELTYQTEEDKKNVNRLQDLVDKLQLKVKAYKRQSEEAEEQANSHLSKLRKVQH 1903
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180
....*....|....*....|....*
gi 288856329 1904 ELEEAEERADIAESQVNKLRAKSRD 1928
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEE 383
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1255-1481 |
1.31e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1255 EDQLSEIKSKNDENLRQINDLSAQRARLQTENGEFGRQLEEKEALVSQLTRGKQAFTQQIEELKRQIEEEVKAKNALAHA 1334
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1335 VQSARHDCDLLR--------EQFEEEQEAKAELQRGMSKANSEVAQWRTKYE---TDAIQRTEELEESKKKLAQRLQEAE 1403
Cdd:COG3883 95 LYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEakkAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 288856329 1404 EQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANALAANLDKKQRNFDKVLAEWKQKYEEGQAELEGAQKEARSLST 1481
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1574-1928 |
1.40e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.20 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1574 IDRKLAEKDEEIEQIKRNSQRITDSM--QSTLDSEVRSRNDALRIKKKMEGDLNemeiQLSHANRQAAEAQKQLRNVQAQ 1651
Cdd:PLN02939 61 SNSKLQSNTDENGQLENTSLRTVMELpqKSTSSDDDHNRASMQRDEAIAAIDNE----QQTNSKDGEQLSDFQLEDLVGM 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1652 LKDAQ---LHLDDA-VRGQEDMKEQVAMVERrntlMQSEIEELRAALEQTERGRKVAEQELVDAsERVGLLHSQNTSLLN 1727
Cdd:PLN02939 137 IQNAEkniLLLNQArLQALEDLEKILTEKEA----LQGKINILEMRLSETDARIKLAAQEKIHV-EILEEQLEKLRNELL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1728 TKKKLEADLVQIQSEVEDTVQEarnaEDKAKKAitDAAMMAEELKKEQDTS---AHLERMKKNLEVTVKDLQHRLDEAEN 1804
Cdd:PLN02939 212 IRGATEGLCVHSLSKELDVLKE----ENMLLKD--DIQFLKAELIEVAETEervFKLEKERSLLDASLRELESKFIVAQE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1805 LAMKGGKKQLQKLESRVRELESEVEAEQRRGADAV---KGVRKYERRVKELTYQTEEdkKNVNRLQ-DLVDKLQLKVKAY 1880
Cdd:PLN02939 286 DVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAAlvlDQNQDLRDKVDKLEASLKE--ANVSKFSsYKVELLQQKLKLL 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 288856329 1881 KRQSEEAEEQANSHlsklrkVQHELEEAEERADIAESQVNKLRAKSRD 1928
Cdd:PLN02939 364 EERLQASDHEIHSY------IQLYQESIKEFQDTLSKLKEESKKRSLE 405
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1373-1921 |
1.47e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 46.56 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1373 WRTkYETDAIQRTEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANAlaanlDKKQRNFD 1452
Cdd:pfam05701 26 WKA-HRIQTVERRKLVELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQT-----EEAQAKQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1453 KVLAEWK-QKYEEGqaeleGAQKEARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGETGK----SIHE 1527
Cdd:pfam05701 100 SELAKLRvEEMEQG-----IADEASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKraeeAVSA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1528 LEKSKKAVETEKAEIQTALEEAEGT----LEHEESKIlRVQLELNQVKSEIDRKLAEKDEEIEQIkRNSQRITDSMQSTL 1603
Cdd:pfam05701 175 SKEIEKTVEELTIELIATKESLESAhaahLEAEEHRI-GAALAREQDKLNWEKELKQAEEELQRL-NQQLLSAKDLKSKL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1604 DSevrsrNDALRIKKK------MEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAvrgqedmKEQVAMVE 1677
Cdd:pfam05701 253 ET-----ASALLLDLKaelaayMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKA-------KDEVNCLR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1678 RRNTLMQSEIEELRAALEQTERGRKVAEQelvdaservgllhsqntsllnTKKKLEADLVQIQSEVEdTVQEarnaedKA 1757
Cdd:pfam05701 321 VAAASLRSELEKEKAELASLRQREGMASI---------------------AVSSLEAELNRTKSEIA-LVQA------KE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1758 KKAitdAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENlamkgGKKQLQKLESRVRELESEVEA---EQRR 1834
Cdd:pfam05701 373 KEA---REKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQ-----AKAAASTVESRLEAVLKEIEAakaSEKL 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1835 GADAVKGVRKYER---------RVKELTYQTEEDKKNVNRLQDLVDKLQLKVKAYKRQSEEAEEQANSHLSKLRKVQHEL 1905
Cdd:pfam05701 445 ALAAIKALQESESsaestnqedSPRGVTLSLEEYYELSKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKLEEVNREM 524
|
570
....*....|....*.
gi 288856329 1906 EEAEERADIAESQVNK 1921
Cdd:pfam05701 525 EERKEALKIALEKAEK 540
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
926-1096 |
1.48e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 46.61 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 926 ERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATEnkvKNLTEEMAA---QDESIG---KLTKEKK 999
Cdd:PRK11637 75 AQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQE---RLLAAQLDAafrQGEHTGlqlILSGEES 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1000 ALQEAHQQTLDDL-QAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQS 1078
Cdd:PRK11637 152 QRGERILAYFGYLnQARQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKD 231
|
170
....*....|....*...
gi 288856329 1079 EEKLKKKDFETSQLLSKI 1096
Cdd:PRK11637 232 QQQLSELRANESRLRDSI 249
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
884-1081 |
1.65e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 884 QEKNDLQLAVASESENLSDAEERCEGLIKSKIQLEAKLKETTERLedeEEINAELTAKKRKLEDECSELKKDIDDLELT- 962
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI---DKLQAEIAEAEAEIEERREELGERARALYRSg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 963 -----LAKVEKEKHATE--NKVKNLTEEMAAQDESIGKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDD 1035
Cdd:COG3883 100 gsvsyLDVLLGSESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 288856329 1036 LEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSEEK 1081
Cdd:COG3883 180 QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1022-1551 |
1.86e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 46.27 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1022 LTKSKTKLEQQVDDLEGSLEQEKKLRMDLERA----KRKLEGDLKLAQESIMDLENDKQQSEEKLKKKDFETSQLLSKIE 1097
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKasalKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1098 DEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEIsERLEEaggataaQIEMNKKREAEFQKLR 1177
Cdd:pfam05557 84 YLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSEL-EELQE-------RLDLLKAKASEAEQLR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1178 RDLEEStlQHEATAAALRKK--------QADSVAELG------EQIDNLQRVKQKLEKEKSEY----------KMEIDDL 1233
Cdd:pfam05557 156 QNLEKQ--QSSLAEAEQRIKelefeiqsQEQDSEIVKnskselARIPELEKELERLREHNKHLnenienklllKEEVEDL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1234 SSNMEAVAKAKANLEKMCRTLEDQLSEIKS------KNDENLRQINDLSAQRARLQT-------ENGEFGRQLEEKEALV 1300
Cdd:pfam05557 234 KRKLEREEKYREEAATLELEKEKLEQELQSwvklaqDTGLNLRSPEDLSRRIEQLQQreivlkeENSSLTSSARQLEKAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1301 SQLTRGKQAFTQQIEELKRQIEEEVKAKNALAHAVQSARHDCDLLREQFEeeqeakaelqrgmsKANSEVAQwrTKYETD 1380
Cdd:pfam05557 314 RELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILE--------------SYDKELTM--SNYSPQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1381 AIQRTEELEESKKKLAQRLQEAEEQIEAvnskcASLEKTKQRLQGEVEDLMIDVERANALAANLDKKQRNFDKVlaewKQ 1460
Cdd:pfam05557 378 LLERIEEAEDMTQKMQAHNEEMEAQLSV-----AEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSL----RR 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1461 KYEEGQAELEGAQKEARSLSTEL--------FKMKNS-------------YEETLDQLETLKRENKNLQQEISDLTEQLg 1519
Cdd:pfam05557 449 KLETLELERQRLREQKNELEMELerrclqgdYDPKKTkvlhlsmnpaaeaYQQRKNQLEKLQAEIERLKRLLKKLEDDL- 527
|
570 580 590
....*....|....*....|....*....|..
gi 288856329 1520 ETGKSIHelEKSKKAVETEKAEIQTALEEAEG 1551
Cdd:pfam05557 528 EQVLRLP--ETTSTMNFKEVLDLRKELESAEL 557
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1752-1931 |
2.20e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1752 NAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENLAMKGGKKqLQKLESRVRELE---SEV 1828
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREE-LEKLEKEVKELEelkEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1829 EAEQRRGADAVKGVRKYERRVKELTYQTEEDKKNVNRLQDLVDKLQlKVKAYKRQSEEAEEQANSHLSKLRKVQHELEEA 1908
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL 319
|
170 180
....*....|....*....|...
gi 288856329 1909 EERADIAESQVNKLRAKSRDSGK 1931
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEE 342
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1561-1803 |
2.58e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1561 LRVQLELNQvkSEIDRKLAEKDEEIEQIKRNSQRITDSMQstldsEVRSRNDALRIkkkmEGDLNEMEIQLSHANRQAAE 1640
Cdd:COG3206 162 LEQNLELRR--EEARKALEFLEEQLPELRKELEEAEAALE-----EFRQKNGLVDL----SEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1641 AQKQLRNVQAQLkdaqlhldDAVRGQEDMKEQVAMVERRNTLMQseieELRAALEQtergrkvAEQELVDASERVGLLHS 1720
Cdd:COG3206 231 ARAELAEAEARL--------AALRAQLGSGPDALPELLQSPVIQ----QLRAQLAE-------LEAELAELSARYTPNHP 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1721 QntsLLNTKKKLEADLVQIQSEVEDTVQEARNAEDKAKKAITDAAMMAEELKKE----QDTSAHLERMKKNLEVTVK--- 1793
Cdd:COG3206 292 D---VIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARlaelPELEAELRRLEREVEVARElye 368
|
250
....*....|
gi 288856329 1794 DLQHRLDEAE 1803
Cdd:COG3206 369 SLLQRLEEAR 378
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
950-1274 |
2.73e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 950 SELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAQDESIGKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKSKTKL 1029
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1030 EQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSEEKLKKKDFETSQLLSKIEDEQSLGAQLQKK 1109
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1110 IKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEESTLQHEA 1189
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1190 TAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDENL 1269
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
....*
gi 288856329 1270 RQIND 1274
Cdd:COG4372 347 LVGLL 351
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1103-1859 |
3.19e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.10 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1103 GAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATA---AQIEMNKKREAEFQKLRRD 1179
Cdd:COG3096 342 ALRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAdyqQALDVQQTRAIQYQQAVQA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1180 LEESTLQHEA---TAAALRKKQADSVAELGEQIDNLQRVKQKL---EKEKSEYK--ME----IDDLSSNMEAVAKAKANL 1247
Cdd:COG3096 422 LEKARALCGLpdlTPENAEDYLAAFRAKEQQATEEVLELEQKLsvaDAARRQFEkaYElvckIAGEVERSQAWQTARELL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1248 EKM--CRTLEDQLSEIKSKndenLRQINDLSAQRARLQTENGEFGRQLEEKEALVSQLTRGKQAFTQQIEELKRQIEEEV 1325
Cdd:COG3096 502 RRYrsQQALAQRLQQLRAQ----LAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAV 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1326 KAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQR--GMSKANSEVAQWRTKYETDAIQRTEELEESKKKLAQRLQEAE 1403
Cdd:COG3096 578 EQRSELRQQLEQLRARIKELAARAPAWLAAQDALERlrEQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALE 657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1404 EQIEAVN----SKCASLEKTKQRLQGEV-----EDLMI--------------------DVERANALAANLDKK------- 1447
Cdd:COG3096 658 SQIERLSqpggAEDPRLLALAERLGGVLlseiyDDVTLedapyfsalygparhaivvpDLSAVKEQLAGLEDCpedlyli 737
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1448 QRN---FDKVLAEWKqkyeegqaELEGA---QKEARSL------STELFKMKnSYEEtldQLETLKRENKNLQQEISDLT 1515
Cdd:COG3096 738 EGDpdsFDDSVFDAE--------ELEDAvvvKLSDRQWrysrfpEVPLFGRA-AREK---RLEELRAERDELAEQYAKAS 805
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1516 EQLGETGKSIHELEK---SKKAV------ETEKAEIQTALEEAEGTLEHEESKILRVQLELNQVKSEID--RKLAE---- 1580
Cdd:COG3096 806 FDVQKLQRLHQAFSQfvgGHLAVafapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQllNKLLPqanl 885
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1581 -KDEEIEqikrnsQRITDsmqstLDSEVRSRNDALRIKKKMEGDLNEMEIQLS--------HANRQAA--EAQKQLRNVQ 1649
Cdd:COG3096 886 lADETLA------DRLEE-----LREELDAAQEAQAFIQQHGKALAQLEPLVAvlqsdpeqFEQLQADylQAKEQQRRLK 954
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1650 AQLkDAqlhLDDAVRGQEDM--KEQVAMVERRNTLmqseIEELRAALEQTERGRKVAEQELVDASERvgllHSQNTSLLn 1727
Cdd:COG3096 955 QQI-FA---LSEVVQRRPHFsyEDAVGLLGENSDL----NEKLRARLEQAEEARREAREQLRQAQAQ----YSQYNQVL- 1021
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1728 tkkkleADLVQIQSEVEDTVQEA-RNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKN-LEvtvKDLQHRldEAEnl 1805
Cdd:COG3096 1022 ------ASLKSSRDAKQQTLQELeQELEELGVQADAEAEERARIRRDELHEELSQNRSRRSqLE---KQLTRC--EAE-- 1088
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 288856329 1806 aMKGGKKQLQKLESRVRELESEVEAEQRRGADAVKGVRKY--ERRV--KELTYQTEED 1859
Cdd:COG3096 1089 -MDSLQKRLRKAERDYKQEREQVVQAKAGWCAVLRLARDNdvERRLhrRELAYLSADE 1145
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1189-1418 |
3.22e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1189 ATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEYKMEIDDLSsnmEAVAKAKANLEKmcrtLEDQLSEIKskndEN 1268
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQ---AELEALQAEIDK----LQAEIAEAE----AE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1269 LRQINDLSAQRARLQTENGEFGRQLE------------EKEALVSQLTRGKQAFTQQIEELKRQIEEevkAKNALAHAVQ 1336
Cdd:COG3883 81 IEERREELGERARALYRSGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEA---KKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1337 SarhdcdlLREQFEEEQEAKAELQRGMSKANSEVAQWRTKyETDAIQRTEELEESKKKLAQRLQEAEEQIEAVNSKCASL 1416
Cdd:COG3883 158 E-------LEALKAELEAAKAELEAQQAEQEALLAQLSAE-EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
..
gi 288856329 1417 EK 1418
Cdd:COG3883 230 AA 231
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1133-1282 |
3.25e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1133 KVEKQRADLSRELEEISERLEEAggatAAQIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQ-----ADSVAELGE 1207
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAAL----EARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnNKEYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 288856329 1208 QIDNLQRVKQKLEKEKSEYKMEIDDLSsnmEAVAKAKANLEKMCRTLEDQLSEIKSKNDENLRQINDLSAQRARL 1282
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELE---EELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
911-1186 |
3.33e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.50 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 911 IKSKIQLEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDID--------------DLELTLAKVEKEKHATENK 976
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDrqaaiyaeqermamERERELERIRQEERKRELE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 977 vKNLTEEMAAQDESIGKLTKEKKALQEAHQQTLDDLQA-------EEDKVNTLTKSKTKLEQQVDDLEGSLEQEKKlRMD 1049
Cdd:pfam17380 364 -RIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAarkvkilEEERQRKIQQQKVEMEQIRAEQEEARQREVR-RLE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1050 LERAkRKLEGDLKLAQESIMDLENDKQQSEEKLKKKdfetsQLLSKIEDEQSLGAQLQKKI--KELQARIEELEEEIEAE 1127
Cdd:pfam17380 442 EERA-REMERVRLEEQERQQQVERLRQQEEERKRKK-----LELEKEKRDRKRAEEQRRKIleKELEERKQAMIEEERKR 515
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 288856329 1128 RAARAKVEKQRADLSREleeisERLEEAGGATAAQIEMNKKREAEFQKLRRDLEESTLQ 1186
Cdd:pfam17380 516 KLLEKEMEERQKAIYEE-----ERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE 569
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
982-1756 |
3.56e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.71 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 982 EEMAAQDESIGKLTKEKKALQEAHQQTLDDLQAEED---KVNTLTKSKTKLEQQVDDLEgsleqekklrmDLERAKRKLE 1058
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQAASDhlnLVQTALRQQEKIERYQEDLE-----------ELTERLEEQE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1059 GDLKLAQESIMDLENDKQQSEEklkkkdfETSQLLSKIED-EQSLGAQLQKKIKELQARIEELEEEIEAeraarakvekQ 1137
Cdd:COG3096 368 EVVEEAAEQLAEAEARLEAAEE-------EVDSLKSQLADyQQALDVQQTRAIQYQQAVQALEKARALC----------G 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1138 RADLSreLEEISERLEEAggATAAQIEMNKKREAEfQKLRrDLEESTLQHEATAAALRK-------KQADSVA-ELGEQI 1209
Cdd:COG3096 431 LPDLT--PENAEDYLAAF--RAKEQQATEEVLELE-QKLS-VADAARRQFEKAYELVCKiageverSQAWQTArELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1210 DNLQRVKQKLEKEKSEYKmeidDLSSNMEAVAKAKANLEKMCRTLEDQLSEIkskndenlrqiNDLSAQRARLQTENGEF 1289
Cdd:COG3096 505 RSQQALAQRLQQLRAQLA----ELEQRLRQQQNAERLLEEFCQRIGQQLDAA-----------EELEELLAELEAQLEEL 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1290 GRQLEEKEALVSQLTRGKQAFTQQIEELKRQIEEEVKAKNALAHavqsarhdcdlLREQFEEEQEAKAELQRGMSKAnse 1369
Cdd:COG3096 570 EEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALER-----------LREQSGEALADSQEVTAAMQQL--- 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1370 vaqwrtkyetdaIQRTEELEESKKKLAQRLQEAEEQIEAVN----SKCASLEKTKQRLQGEV-----EDLMI-------- 1432
Cdd:COG3096 636 ------------LEREREATVERDELAARKQALESQIERLSqpggAEDPRLLALAERLGGVLlseiyDDVTLedapyfsa 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1433 ------------DVERANALAANLDKK-------QRN---FDKVLAEWKqkyeegqaELEGA---QKEARSL------ST 1481
Cdd:COG3096 704 lygparhaivvpDLSAVKEQLAGLEDCpedlyliEGDpdsFDDSVFDAE--------ELEDAvvvKLSDRQWrysrfpEV 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1482 ELFKMKnSYEEtldQLETLKRENKNLQQEISDLTEQLGETGKSIHELEK---SKKAV------ETEKAEIQTALEEAEGT 1552
Cdd:COG3096 776 PLFGRA-AREK---RLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvgGHLAVafapdpEAELAALRQRRSELERE 851
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1553 LEHEESKILRVQLELNQVKSEI--------------DRKLAEKDEEIEQ-----------IKRNSQRIT--DSMQSTLDS 1605
Cdd:COG3096 852 LAQHRAQEQQLRQQLDQLKEQLqllnkllpqanllaDETLADRLEELREeldaaqeaqafIQQHGKALAqlEPLVAVLQS 931
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1606 ------------------------------EVRSR------NDALRIKKKmEGDLNE-MEIQLSHANRQAAEAQKQLRNV 1648
Cdd:COG3096 932 dpeqfeqlqadylqakeqqrrlkqqifalsEVVQRrphfsyEDAVGLLGE-NSDLNEkLRARLEQAEEARREAREQLRQA 1010
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1649 QAQLKDAQLHLDDAVRGQEDMKEQVAMVERrntlmqsEIEEL--RAALEQTERGRkvaeqelvdasERVGLLHSQNTSLL 1726
Cdd:COG3096 1011 QAQYSQYNQVLASLKSSRDAKQQTLQELEQ-------ELEELgvQADAEAEERAR-----------IRRDELHEELSQNR 1072
|
890 900 910
....*....|....*....|....*....|
gi 288856329 1727 NTKKKLEADLVQIQSEVEDTVQEARNAEDK 1756
Cdd:COG3096 1073 SRRSQLEKQLTRCEAEMDSLQKRLRKAERD 1102
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
885-1092 |
3.59e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.39 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 885 EKNDLQLAVASESENLSDAEErcegliKSKIQLEAKLKETTERLEDEEEINAELTakkrKLEDECSELKKDIDDLELTLA 964
Cdd:PHA02562 189 KIDHIQQQIKTYNKNIEEQRK------KNGENIARKQNKYDELVEEAKTIKAEIE----ELTDELLNLVMDIEDPSAALN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 965 KVEKEKHATENKVKNLTEEM----------------AAQDESIGKLTKEKKALQ---EAHQQTLDDLQAEEDKVNTLTKS 1025
Cdd:PHA02562 259 KLNTAAAKIKSKIEQFQKVIkmyekggvcptctqqiSEGPDRITKIKDKLKELQhslEKLDTAIDELEEIMDEFNEQSKK 338
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 288856329 1026 ----KTKLEQQVDDLEGSLEQEKKLRMDLERAKRKL---EGDLKLAQESIMDLENDKQQSEEKLKKKDFETSQL 1092
Cdd:PHA02562 339 llelKNKISTNKQSLITLVDKAKKVKAAIEELQAEFvdnAEELAKLQDELDKIVKTKSELVKEKYHRGIVTDLL 412
|
|
| EcCorA_ZntB-like |
cd12821 |
Escherichia coli CorA-Salmonella typhimurium ZntB_like family; A family of the MIT superfamily ... |
1297-1409 |
4.03e-04 |
|
Escherichia coli CorA-Salmonella typhimurium ZntB_like family; A family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. Members of this family are found in all three kingdoms of life. It is a functionally diverse family, including the Mg2+ transporters Escherichia coli and Salmonella typhimurium CorAs (which can also transport Co2+, and Ni2+ ), and the Zn2+ transporter Salmonella typhimurium ZntB which mediates the efflux of Zn2+ (and Cd2+). It also includes two Saccharomyces cerevisiae members: the inner membrane Mg2+ transporters Mfm1p/Lpe10p, and Mrs2p, and a family of Arabidopsis thaliana members (AtMGTs) some of which are localized to distinct tissues, and not all of which can transport Mg2+. Structures of the intracellular domain of Vibrio parahaemolyticus and Salmonella typhimurium ZntB form funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport through Salmonella typhimurium CorA, and Mrs2p. Natural variants such as GVN and GIN, such as occur in some ZntB family proteins, may be associated with the transport of different divalent cations, such as zinc and cadmium. The functional diversity of MIT transporters may also be due to minor structural differences regulating gating, substrate selection, and transport.
Pssm-ID: 213355 [Multi-domain] Cd Length: 285 Bit Score: 44.62 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1297 EALVSQLTRGKQAFTQQIEELKRQIEEEVKAKnALAHAVqSARHDCDLLREQFEEEQEAKAELQRGMSKANSEvaqwrTK 1376
Cdd:cd12821 110 GAIIKALLTGIDQFEEKLEELEWDLLEGNNAI-KLDRIL-ELRRELLRLTNLIEPQQEVLMALQEAFAELLFS-----ED 182
|
90 100 110
....*....|....*....|....*....|....*
gi 288856329 1377 YET--DAIQRTEELEESKKKLAQRLQEAEEQIEAV 1409
Cdd:cd12821 183 EEElrRTLDRIERLLQLIEEYEQELDTLQDIEEVV 217
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1573-1937 |
4.21e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1573 EIDRKLAEKDEEIEQIKRNSQRITDSMQSTLDSEVRSRNDALRIKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQL 1652
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1653 KDAQLHLDDAVRGQEDMKEQVAMVERRNTLMQSEIEELRAALEQTERGRKVAEQELVDASERVGLLHSQNTSLLNTKKKL 1732
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1733 EADLVQIQSEVEDTVQEARNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENLAMKGGKK 1812
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1813 QLQKLESRVRELESEVEAEQRRGADAVKGVRKYERRVKELTYQTEEDKKNVNRLQDLVDKLQLKVKAYKRQSEEAEEQAN 1892
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 288856329 1893 SHLSKLRKVQHELEEAEERADIAESQVNKLRAKSRDSGKGKDAAE 1937
Cdd:COG4372 323 ELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1283-1810 |
4.43e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.33 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1283 QTENGEFGRQLEEKEALVSQltrgkqAFTQQIEELKRQIEEEVKAKNALAHAvqsarhdcdllREQFEEEQEAKAELQRG 1362
Cdd:COG3096 252 QSDRDLFKHLITEATNYVAA------DYMRHANERRELSERALELRRELFGA-----------RRQLAEEQYRLVEMARE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1363 MskansevaqwrtkyetdaiqrtEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTkQRLQGEVEDLMIDVERANAlaa 1442
Cdd:COG3096 315 L----------------------EELSARESDLEQDYQAASDHLNLVQTALRQQEKI-ERYQEDLEELTERLEEQEE--- 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1443 nldkkqrnfdkVLAEWKQKYEEGQAELEGAQKEARSLSTELfkmkNSYEETLDQLETlkrenknlqqeisdlteqlgetg 1522
Cdd:COG3096 369 -----------VVEEAAEQLAEAEARLEAAEEEVDSLKSQL----ADYQQALDVQQT----------------------- 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1523 ksihelekskKAVETEKAeiQTALEEAEGTLEHEEskilrvqLELNQVKSEIDRKLAEKDEEIEQIKRNSQRITDSmqst 1602
Cdd:COG3096 411 ----------RAIQYQQA--VQALEKARALCGLPD-------LTPENAEDYLAAFRAKEQQATEEVLELEQKLSVA---- 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1603 lDSEVRSRNDALRIKKKMEGdlnemEIQLSHANRQAAEAQKQLRNVQAQLKDAQ---LHLDDA---VRGQEDMKEQVAMV 1676
Cdd:COG3096 468 -DAARRQFEKAYELVCKIAG-----EVERSQAWQTARELLRRYRSQQALAQRLQqlrAQLAELeqrLRQQQNAERLLEEF 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1677 ERRNTLMQSEIEELRAALEQTERGRKVAEQELVDASERVGLLHSQntsllntkkkLEADLVQIQsEVEDTVQEARNAEDK 1756
Cdd:COG3096 542 CQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQ----------LEQLRARIK-ELAARAPAWLAAQDA 610
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 288856329 1757 AKKAitdAAMMAEELKKEQDTSAHLERMKKNL-EVTV-KDL-----QHRLDEAENLAMKGG 1810
Cdd:COG3096 611 LERL---REQSGEALADSQEVTAAMQQLLERErEATVeRDElaarkQALESQIERLSQPGG 668
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
848-1698 |
5.04e-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: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 848 EKELATMKEDFVKCKED------------------------LAKAEAKKKELEEKMVALLQEKNDLQLAVASESENLSDA 903
Cdd:TIGR01612 764 EKELSNKINDYAKEKDElnkykskiseiknhyndqinidniKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDD 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 904 eerceglIKSKIQLEAKLKET-TERLEDEEEINAELTAK-KRKLEDE-CSELKKDIDD----LELTLAKVEKEKH--ATE 974
Cdd:TIGR01612 844 -------FLNKVDKFINFENNcKEKIDSEHEQFAELTNKiKAEISDDkLNDYEKKFNDskslINEINKSIEEEYQniNTL 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 975 NKVKNLTEEMAAQDESIGKLTKEKKALQEAHQQTLDDL-------QAEEDKV-NTLTKSKTKLEQQVDDLegSLEQEKKL 1046
Cdd:TIGR01612 917 KKVDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIkesnlieKSYKDKFdNTLIDKINELDKAFKDA--SLNDYEAK 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1047 RMDLERAKRKLEGDLKLAQESIMdlendKQQSEEKLKKkdfeTSQLLSKIED--------EQSLGAQLQKKIKELQARIE 1118
Cdd:TIGR01612 995 NNELIKYFNDLKANLGKNKENML-----YHQFDEKEKA----TNDIEQKIEDanknipniEIAIHTSIYNIIDEIEKEIG 1065
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1119 ELEEEIEAERaarakVEKQRADLSrELEEISERLEEAGGATAAQiEMNKKREAEFQKLRRDLEESTLQHEATAAAL---R 1195
Cdd:TIGR01612 1066 KNIELLNKEI-----LEEAEINIT-NFNEIKEKLKHYNFDDFGK-EENIKYADEINKIKDDIKNLDQKIDHHIKALeeiK 1138
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1196 KKQADSVAELGEQIDNLQRVKQK-LEKEKSEykmEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKsKNDENLRQIND 1274
Cdd:TIGR01612 1139 KKSENYIDEIKAQINDLEDVADKaISNDDPE---EIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIE-KDKTSLEEVKG 1214
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1275 LSAQRArlQTENGEFGRQLEEKEALVSQLTRGKQAFTQQIEELKRQ---------IEEEVKAK-NAL--------AHAVQ 1336
Cdd:TIGR01612 1215 INLSYG--KNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKspeienemgIEMDIKAEmETFnishdddkDHHII 1292
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1337 SARHDCDL---------LREQFEEE---QEAKAELQRGMS---KANSEVAQWRTKYET---------------DAIQRTE 1386
Cdd:TIGR01612 1293 SKKHDENIsdirekslkIIEDFSEEsdiNDIKKELQKNLLdaqKHNSDINLYLNEIANiynilklnkikkiidEVKEYTK 1372
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1387 ELEESKKKLAQRLQEAEEQIEAVNSKcASLEKTKQRLQGEVEDLMID--------------------------------- 1433
Cdd:TIGR01612 1373 EIEENNKNIKDELDKSEKLIKKIKDD-INLEECKSKIESTLDDKDIDecikkikelknhilseesnidtyfknadennen 1451
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1434 -------VERANALAANLDKKQRN-----FDKVLAEWKQKYEEGQAELEGAQKEARSL--STELFK-------------- 1485
Cdd:TIGR01612 1452 vlllfknIEMADNKSQHILKIKKDnatndHDFNINELKEHIDKSKGCKDEADKNAKAIekNKELFEqykkdvtellnkys 1531
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1486 ---MKNSYEETLDQLETLKRENKNLQQEIsdlTEQLGETGKSIHELEKSKKAVETEKA---EIQTALEEAEGTLEHEESK 1559
Cdd:TIGR01612 1532 alaIKNKFAKTKKDSEIIIKEIKDAHKKF---ILEAEKSEQKIKEIKKEKFRIEDDAAkndKSNKAAIDIQLSLENFENK 1608
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1560 ILRVqlelnqvkSEIDRKLAEKDEEIEQIKRnsqRITDSMQSTLDSEVRSRNDALrikkkmeGDLNEMEIQLSHANRQAA 1639
Cdd:TIGR01612 1609 FLKI--------SDIKKKINDCLKETESIEK---KISSFSIDSQDTELKENGDNL-------NSLQEFLESLKDQKKNIE 1670
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*....
gi 288856329 1640 EAQKQLRNVQAQLKDAQLHLDdavrgQEDMKEQVAMVERRNTLMQSEIEELRAALEQTE 1698
Cdd:TIGR01612 1671 DKKKELDELDSEIEKIEIDVD-----QHKKNYEIGIIEKIKEIAIANKEEIESIKELIE 1724
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1298-1594 |
5.13e-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: 45.00 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1298 ALVSQLTRGKQAFTQQIEELKRQIEEEV--KAKNALAHAVQSARHDCDLLREQFEE------EQEAKAELQRGMSKANSE 1369
Cdd:NF033838 88 ALNKKLSDIKTEYLYELNVLKEKSEAELtsKTKKELDAAFEQFKKDTLEPGKKVAEatkkveEAEKKAKDQKEEDRRNYP 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1370 VAQWRT----KYETDAIQRTEELEESKKKL-----AQRLQEAEEQIEAVNSKCASLEKTK-QRLQGEVE-DLMIDVERAN 1438
Cdd:NF033838 168 TNTYKTleleIAESDVEVKKAELELVKEEAkeprdEEKIKQAKAKVESKKAEATRLEKIKtDREKAEEEaKRRADAKLKE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1439 ALAANLDKKQRnfDKVLAEWKQKYEEGQAELEGAQKEARSLSTELfkmknsYEETLDQlETLKRENKNLQQEISdlTEQL 1518
Cdd:NF033838 248 AVEKNVATSEQ--DKPKRRAKRGVLGEPATPDKKENDAKSSDSSV------GEETLPS-PSLKPEKKVAEAEKK--VEEA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1519 GETGKSIHELEK------SKKAVETEKAEIQTALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKdEEIEQIKRNS 1592
Cdd:NF033838 317 KKKAKDQKEEDRrnyptnTYKTLELEIAESDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAEA-TRLEKIKTDR 395
|
..
gi 288856329 1593 QR 1594
Cdd:NF033838 396 KK 397
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1357-1803 |
6.04e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 44.51 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1357 AELQRGMSKANSEVAQWRTKYETDAIQRtEELEESKKKLAQRLQEAEEQIEAVNSKCASlEKTKQRLQGEVEDLM----- 1431
Cdd:COG5278 79 EPYEEARAEIDELLAELRSLTADNPEQQ-ARLDELEALIDQWLAELEQVIALRRAGGLE-AALALVRSGEGKALMdeira 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1432 IDVERANALAANLDKKQRNFDKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEI 1511
Cdd:COG5278 157 RLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1512 SDLTEQLGETGKSIHELEKSKKAVETEKAEIQTALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEEIEQIKRN 1591
Cdd:COG5278 237 ALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1592 SQRITDSMQSTLDSEVRSRNDALRIKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKE 1671
Cdd:COG5278 317 AAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIA 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1672 QVAMVERRNTLMQSEIEELRAALEQTERGRKVAEQELVDASERVGLLHSQNTSLLNTKKKLEADLVQIQSEVEDTVQEAR 1751
Cdd:COG5278 397 AAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAA 476
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 288856329 1752 NAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAE 1803
Cdd:COG5278 477 LAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASA 528
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1314-1699 |
6.43e-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: 44.46 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1314 IEELKRQIEEE------VKAKNALAHA----------VQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRTKY 1377
Cdd:pfam06160 65 IEELLFEAEELndkyrfKKAKKALDEIeellddieedIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFSY 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1378 ETDAiqrtEELEESKKKLAQRLQEAEEQIEAVNSKCAS--LEKTKQRLqGEVEDLMIDVEranalaANLDKKQRNFDKVL 1455
Cdd:pfam06160 145 GPAI----DELEKQLAEIEEEFSQFEELTESGDYLEARevLEKLEEET-DALEELMEDIP------PLYEELKTELPDQL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1456 AEWKQKYEegQAELEGAQKEARSLSTELFKMKNSYEETLDQLETL-----KRENKNLQQEISDLTEQLgetgksihELE- 1529
Cdd:pfam06160 214 EELKEGYR--EMEEEGYALEHLNVDKEIQQLEEQLEENLALLENLeldeaEEALEEIEERIDQLYDLL--------EKEv 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1530 KSKKAVETEKAEIQTALEEAEGTLEHEESKILRVQL-----------------ELNQVK-----------------SEID 1575
Cdd:pfam06160 284 DAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQsytlnenelervrglekQLEELEkrydeiverleekevaySELQ 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1576 RKLAEKDEEIEQIKRNSQRITDSMQSTLDSEVRSRNDALRIKKKME------------GDLNEMEIQLSHANRQAAEAQK 1643
Cdd:pfam06160 364 EELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELReikrlveksnlpGLPESYLDYFFDVSDEIEDLAD 443
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 288856329 1644 QLRN-------VQAQLKDAQLHLDDAVRGQEDMKEQVAMVERrntLMQ------SEIEELRAALEQTER 1699
Cdd:pfam06160 444 ELNEvplnmdeVNRLLDEAQDDVDTLYEKTEELIDNATLAEQ---LIQyanryrSSNPEVAEALTEAEL 509
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1432-1749 |
6.70e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.89 E-value: 6.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1432 IDVERANALAANLDKKQRNFdkvlaewKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEI 1511
Cdd:PLN02939 100 ASMQRDEAIAAIDNEQQTNS-------KDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1512 SDLTEQLGETGKSIHELEKSKKAVETEKAEIQTALEEAEGTLEHEESKILRVQLELNQVKSEidrKLAEKDeEIEQIKRN 1591
Cdd:PLN02939 173 NILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEE---NMLLKD-DIQFLKAE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1592 SQRITDSMQS--TLDSEvrsrndalriKKKMEGDLNEMEIQLSHANRQAAE-AQKQLRNVQAQLKDAQLHLDDAVrgqeD 1668
Cdd:PLN02939 249 LIEVAETEERvfKLEKE----------RSLLDASLRELESKFIVAQEDVSKlSPLQYDCWWEKVENLQDLLDRAT----N 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1669 MKEQVAMVERRNTLMQSEIEELRAALEQTergrKVAEQelvdASERVGLLHSQNTSLlntKKKLEADLVQIQSEV---ED 1745
Cdd:PLN02939 315 QVEKAALVLDQNQDLRDKVDKLEASLKEA----NVSKF----SSYKVELLQQKLKLL---EERLQASDHEIHSYIqlyQE 383
|
....
gi 288856329 1746 TVQE 1749
Cdd:PLN02939 384 SIKE 387
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1456-1912 |
6.76e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.96 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1456 AEWKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAV 1535
Cdd:TIGR00618 183 LMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1536 ETEKAEIQTaleeaegtLEHEESKILRVQLELNQVKSEIdrKLAEKDEEIEQIKRNSQRITDSMQSTLDSEVRSR-NDAL 1614
Cdd:TIGR00618 263 KQLRARIEE--------LRAQEAVLEETQERINRARKAA--PLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLmKRAA 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1615 RIKKKMEGDLNEMEIQLSHA----NRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAMVERRNTLMQSEI--E 1688
Cdd:TIGR00618 333 HVKQQSSIEEQRRLLQTLHSqeihIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQatI 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1689 ELRAALEQTERGRKV-AEQELVDASERVGLLHSQNTSLLNTKKKLEADLVQIQSEVEDTVQEARNAEDKAKKAITDAAMM 1767
Cdd:TIGR00618 413 DTRTSAFRDLQGQLAhAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVV 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1768 AEELKKEQDTSAHLERMKKNLEVTVKDL------QHRLDEAENLAMKGGKK------QLQKLESRVRELESEVEAEQRRg 1835
Cdd:TIGR00618 493 LARLLELQEEPCPLCGSCIHPNPARQDIdnpgplTRRMQRGEQTYAQLETSeedvyhQLTSERKQRASLKEQMQEIQQS- 571
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 288856329 1836 adavkgVRKYERRVKELTYQTEEDKKNVNRLQDLVDKLQLKVKAYKRQSEEAEEQANSHLSKLRKVQHELEEAEERA 1912
Cdd:TIGR00618 572 ------FSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA 642
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1454-1776 |
7.08e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1454 VLAEWKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEKSKK 1533
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1534 AVETEKAEIQTALEEaegtLEHEESKILRVQLELNQVKSEIDRKLAEKDEEIEQIKRNSQRITDSMQSTLDSEVRSRNDA 1613
Cdd:COG4372 105 SLQEEAEELQEELEE----LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1614 LRIKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAMVERRNTLMQSEIEELRAA 1693
Cdd:COG4372 181 AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1694 LEQTERGRKVAEQELVDASERVGLLHSQNTSLLNTKKKLEADLVQIQSEVEDTVQEARNAEDKAKKAITDAAMMAEELKK 1773
Cdd:COG4372 261 EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
...
gi 288856329 1774 EQD 1776
Cdd:COG4372 341 DLL 343
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1238-1566 |
7.14e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1238 EAVAKAKANLEKMCRTLEDQLSEIKSKNDENLRQINDLSAQRARLQTENGEFGRQLEEKEALVSQLTRGKQAFTQQIEEL 1317
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1318 KRQIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRTKYeTDAIQRTEELEESKKKLAQ 1397
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI-AEREEELKELEEQLESLQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1398 RLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANALAANLDKKQRNFDKVLAEWKQKYEEGQAELEGAQKEAR 1477
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1478 SLSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAVETEKAEIQTALEEAEGTLEHEE 1557
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
....*....
gi 288856329 1558 SKILRVQLE 1566
Cdd:COG4372 325 AKKLELALA 333
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1631-1927 |
7.28e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1631 LSHANR------QAAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAMVE--------RRNTLM------------Q 1684
Cdd:COG3096 274 MRHANErrelseRALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEqdyqaasdHLNLVQtalrqqekieryQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1685 SEIEELRAALEQTERGRKVAEQELVDASERVGLLHSQNTSLlntKKKLeADLVQ---IQSEVEDTVQEARNAEDKAKKAI 1761
Cdd:COG3096 354 EDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSL---KSQL-ADYQQaldVQQTRAIQYQQAVQALEKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1762 TDAAMMAEELKKEQdtsAHLERMKKNLEVTVKDLQHRLDEAEnlamkGGKKQLQKLESRVRELESEVEAEQrrgadAVKG 1841
Cdd:COG3096 430 GLPDLTPENAEDYL---AAFRAKEQQATEEVLELEQKLSVAD-----AARRQFEKAYELVCKIAGEVERSQ-----AWQT 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1842 VRKYERRVKELTYQTEEDKKNVNRLQDLVDKLQLKVKAyKRQSEEAEEQANSHLSKLRKVQHELEEAEERADIAESQVNK 1921
Cdd:COG3096 497 ARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNA-ERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAE 575
|
....*.
gi 288856329 1922 LRAKSR 1927
Cdd:COG3096 576 AVEQRS 581
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
923-1326 |
7.47e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 923 ETTERLEDEEEINAEL-TAKKRKL-EDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAQDESIGKLTKEKKA 1000
Cdd:PRK11281 30 ASNGDLPTEADVQAQLdALNKQKLlEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1001 LQEAHQQTLDDLqaeedkvntltkSKTKLEQQVDDLEGSLEQEKK-----------LRMDLERAKRKLEGDLKLAQEsIM 1069
Cdd:PRK11281 110 NDEETRETLSTL------------SLRQLESRLAQTLDQLQNAQNdlaeynsqlvsLQTQPERAQAALYANSQRLQQ-IR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1070 DLENDKQQSEEKLkkkdfeTSQLLSKIEDEQS-LGAQLQKKIKELQARIEELEEEieaeraarakvEKQRADLSrelEEI 1148
Cdd:PRK11281 177 NLLKGGKVGGKAL------RPSQRVLLQAEQAlLNAQNDLQRKSLEGNTQLQDLL-----------QKQRDYLT---ARI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1149 SeRLEEAggATAAQIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQI------------DNLqRVK 1216
Cdd:PRK11281 237 Q-RLEHQ--LQLLQEAINSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLlkateklntltqQNL-RVK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1217 QKLEkekseykmeiddlssnmeavakakaNLEKMCRTLEDQ---------LSEIKSKNDENLRQ---INDLSAQRARL-- 1282
Cdd:PRK11281 313 NWLD-------------------------RLTQSERNIKEQisvlkgsllLSRILYQQQQALPSadlIEGLADRIADLrl 367
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 288856329 1283 -QTENGEFGRQLEEKEALVSQLTRG-KQAFTqqiEELKRQIEEEVK 1326
Cdd:PRK11281 368 eQFEINQQRDALFQPDAYIDKLEAGhKSEVT---DEVRDALLQLLD 410
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
843-1057 |
8.18e-04 |
|
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: 43.98 E-value: 8.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 843 KSAETEKELATMKEDFVKCKEDLAKAEAKKKELEEKMVALLQEKNDLQLAVASESENLSDAEERCEGLIKSKIQLEAKLK 922
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 923 ETTERL----------------------EDEEEINAELTAKKRKLEdecsELKKDIDDLELTLAKVEKEKHATENKVKNL 980
Cdd:COG4942 101 AQKEELaellralyrlgrqpplalllspEDFLDAVRRLQYLKYLAP----ARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 288856329 981 TEEMAAQDESIGKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQ--EKKLRMDLERAKRKL 1057
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAaaERTPAAGFAALKGKL 255
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1383-1551 |
9.05e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 43.59 E-value: 9.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1383 QRTEELEESKKKLAQRLQEA--EEQIEAVNSKCASLEKTKQR----------LQGEVEDL---MIDVE-RANALAANLDK 1446
Cdd:pfam09787 14 QKAARILQSKEKLIASLKEGsgVEGLDSSTALTLELEELRQErdllreeiqkLRGQIQQLrteLQELEaQQQEEAESSRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1447 KQRNFDKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLE----------TLKRENKNLQQEISDLTE 1516
Cdd:pfam09787 94 QLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREaeieklrnqlTSKSQSSSSQSELENRLH 173
|
170 180 190
....*....|....*....|....*....|....*
gi 288856329 1517 QLGETgksIHELEKSKKAVETEKAEIQTALEEAEG 1551
Cdd:pfam09787 174 QLTET---LIQKQTMLEALSTEKNSLVLQLERMEQ 205
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
882-1019 |
9.21e-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: 9.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 882 LLQEKNDLQLAVASESENLSDAEERCEGLIKSKIQLEAKLKETTERLE-DEEEINAELTAKKRK-LEDECSELKKDIDDL 959
Cdd:COG1579 29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkYEEQLGNVRNNKEYEaLQKEIESLKRRISDL 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 960 ELTLAKVEKEKHATENKVKNLTEEMAAQDESIGKLTKEKKALQEAHQQTLDDLQAEEDKV 1019
Cdd:COG1579 109 EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1709-1937 |
1.07e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1709 VDASERVGLLHSQNTSLLNTKKKLEADLVQIQSEVEDTVQEARNAEDKAKKAITDAAMMAEELKKEQdtsAHLERMKKNL 1788
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1789 EVTVKDLQHRLDEAENLAMKGGKKQLQKLESRVRELESEVEAEQRRgadavkgVRKYERRVKELTYQTEEDKKNVNRLQD 1868
Cdd:COG3883 89 GERARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADL-------LEELKADKAELEAKKAELEAKLAELEA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 288856329 1869 LVDKLQLKVKAYKRQSEEAEEQANSHLSKLRKVQHELEEAEERADIAESQVNKLRAKSRDSGKGKDAAE 1937
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1007-1322 |
1.09e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1007 QTLDDLQAEEDKVNT---LTKSKTKLEQQVDDLeGSLEQEKKLRMDLERAKRKLEGDLKLAQE---SIMDLE---NDKQQ 1077
Cdd:COG3206 71 SGLSSLSASDSPLETqieILKSRPVLERVVDKL-NLDEDPLGEEASREAAIERLRKNLTVEPVkgsNVIEISytsPDPEL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1078 SEEKLKK--KDFETSQLLSKIEDEQSLGAQLQKKIKELQARieeleeeieaeraaRAKVEKQRADLSRELEEISerLEEA 1155
Cdd:COG3206 150 AAAVANAlaEAYLEQNLELRREEARKALEFLEEQLPELRKE--------------LEEAEAALEEFRQKNGLVD--LSEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1156 GGATAAQIemnkkreAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQIDNlqRVKQKLEKEKSEYKMEIDDLSs 1235
Cdd:COG3206 214 AKLLLQQL-------SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELS- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1236 nmeavAKAKANLEKMcRTLEDQLSEIKSKNDENLRQI-NDLSAQRARLQTENGEFGRQLEEKEALVSQLTRgKQaftQQI 1314
Cdd:COG3206 284 -----ARYTPNHPDV-IALRAQIAALRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARLAELPE-LE---AEL 353
|
....*...
gi 288856329 1315 EELKRQIE 1322
Cdd:COG3206 354 RRLEREVE 361
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1420-1573 |
1.10e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.47 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1420 KQRLQGEVEDLMIDVERANALAANLDKKQRNFDKVLAEWKQKYEEGQAELEGAQKEARSL----STELFKMKNsyeetld 1495
Cdd:smart00787 139 MKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELedcdPTELDRAKE------- 211
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 288856329 1496 QLETLKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAVETEKAEIQTALEEAEGtleHEESKILRVQLELNQVKSE 1573
Cdd:smart00787 212 KLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG---FTFKEIEKLKEQLKLLQSL 286
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1492-1929 |
1.13e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1492 ETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHElekSKKAVETEKAEIQTALEEAEGTLEHeeskiLRVQLELNQVK 1571
Cdd:TIGR00618 184 MEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHE---RKQVLEKELKHLREALQQTQQSHAY-----LTQKREAQEEQ 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1572 SEIDRKLAEKDEEIEQIKrnsqritdsmqsTLDSEVRSRNDALRIKKKMEGDLNEMEiQLSHANRQAAEAQKQLRNVQAQ 1651
Cdd:TIGR00618 256 LKKQQLLKQLRARIEELR------------AQEAVLEETQERINRARKAAPLAAHIK-AVTQIEQQAQRIHTELQSKMRS 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1652 LKDAQLHLDDAVRGQEDMKEQVAMVerrNTLMQSEIEELRAALEQTERgRKVAEQELVDaSERVGLLHSQNTSLLNTKKK 1731
Cdd:TIGR00618 323 RAKLLMKRAAHVKQQSSIEEQRRLL---QTLHSQEIHIRDAHEVATSI-REISCQQHTL-TQHIHTLQQQKTTLTQKLQS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1732 LEADLVQIQSEVEDtvQEARNAEDKAKKAITDAAMMAEELKKE-----QDTSAHLERMKKNLEVTVKDLQHRLDEAENLa 1806
Cdd:TIGR00618 398 LCKELDILQREQAT--IDTRTSAFRDLQGQLAHAKKQQELQQRyaelcAAAITCTAQCEKLEKIHLQESAQSLKEREQQ- 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1807 mKGGKKQLQKLESRVRELESEVEAEQRRGADAVKGVRKYERRVKELTYQTEEDKKNVNRLQDLVDKLQlkvkaykrqseE 1886
Cdd:TIGR00618 475 -LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLE-----------T 542
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 288856329 1887 AEEQANSHLSKLRKVQHELEEAEERADIAESQVNKLRAKSRDS 1929
Cdd:TIGR00618 543 SEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKED 585
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1496-1702 |
1.18e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1496 QLETLKRENKNLQQEISDLTEQLGEtgksiheLEKSKKAVETEKAEIQTALEEAEGTLEHEESKILRVQLELNQVKSEID 1575
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAA-------LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1576 RKLAEKdeEIEQIKRNsqritdsmqstldsevrsrndalriKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDA 1655
Cdd:COG1579 91 YEALQK--EIESLKRR-------------------------ISDLEDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 288856329 1656 QLHLDDAVrgQEDMKEQVAMVERRNTLMQSEIEELRAALEQTERGRK 1702
Cdd:COG1579 144 KAELDEEL--AELEAELEELEAEREELAAKIPPELLALYERIRKRKN 188
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1050-1209 |
1.18e-03 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 43.98 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1050 LERAKRKLEGDLKLAQESIMDLENDKQQSEEKLKkkdfETSQLLSKIEdeqSLGAQLQKKIKELQarieeleeeieaeRA 1129
Cdd:COG1193 502 IERARELLGEESIDVEKLIEELERERRELEEERE----EAERLREELE---KLREELEEKLEELE-------------EE 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1130 ARAKVEKQRADLSRELEEISERLEEaggaTAAQIEMNKKREAEFQKLRRDLEEstLQHEATAAALRKKQADSVAELGEQI 1209
Cdd:COG1193 562 KEEILEKAREEAEEILREARKEAEE----LIRELREAQAEEEELKEARKKLEE--LKQELEEKLEKPKKKAKPAKPPEEL 635
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1177-1433 |
1.20e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1177 RRDLEESTLQhEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEYKMEIDDLSsnmeavAKAKANLEkmcrtled 1256
Cdd:PHA02562 152 RRKLVEDLLD-ISVLSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQR------KKNGENIA-------- 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1257 qlsEIKSKNDENLRQINDLSAQRARLQTENGEFGRQLEEKEALVSQLTRGKQAFTQQIEELKR----------------Q 1320
Cdd:PHA02562 217 ---RKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyekggvcptctqQ 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1321 IEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANsevaQWRTKYETD--AIQRTEELEESKKKLAQR 1398
Cdd:PHA02562 294 ISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLL----ELKNKISTNkqSLITLVDKAKKVKAAIEE 369
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 288856329 1399 LQEA-----------EEQIEAVNSKCASLEKTKQRLqGEVEDLMID 1433
Cdd:PHA02562 370 LQAEfvdnaeelaklQDELDKIVKTKSELVKEKYHR-GIVTDLLKD 414
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1416-1710 |
1.29e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.57 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1416 LEKTKQ-RLQGEVEDLMIDVERANALAANLDKKQRNFDK---VLAEWKQKYEEGQAELEGAQKEARslstelfkmknsye 1491
Cdd:pfam17380 293 FEKMEQeRLRQEKEEKAREVERRRKLEEAEKARQAEMDRqaaIYAEQERMAMERERELERIRQEER-------------- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1492 etldqletlKRENKNLQQEisdlteQLGETGKSIHELEKSKKAVETEKAEIQTALEEAEgtleheESKILrvqlelnqvK 1571
Cdd:pfam17380 359 ---------KRELERIRQE------EIAMEISRMRELERLQMERQQKNERVRQELEAAR------KVKIL---------E 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1572 SEIDRKLAEKDEEIEQIKRNSQRITDSMQSTLDSEvRSRndalrikkkmegdlnEME-IQLSHANRQaaEAQKQLRNVQA 1650
Cdd:pfam17380 409 EERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEE-RAR---------------EMErVRLEEQERQ--QQVERLRQQEE 470
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1651 QLKDAQLHLDDAVRGQEDMKEQvamverRNTLMQSEIEELRAALEQTERGRKVAEQELVD 1710
Cdd:pfam17380 471 ERKRKKLELEKEKRDRKRAEEQ------RRKILEKELEERKQAMIEEERKRKLLEKEMEE 524
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
884-1091 |
1.31e-03 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 43.99 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 884 QEKNDLQLAVASESENLSDAEERCEGLIKSKIQLEAKLKETTERLEDEEEINAE-------------LTAKKRKLEDECS 950
Cdd:pfam18971 614 KAQKDLEKSLRKREHLEKEVEKKLESKSGNKNKMEAKAQANSQKDEIFALINKEanrdaraiaytqnLKGIKRELSDKLE 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 951 ELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAQDESIGkLTKEKKALQEAHQQTLDDLQAEEDK-VNTLTKSKTKL 1029
Cdd:pfam18971 694 KISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDLG-INPEWISKVENLNAALNEFKNGKNKdFSKVTQAKSDL 772
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 288856329 1030 EQQVDDLEGSLEQEKKL-RMDLERAKRKLEGDLKLAQESIMDLEN--DKQQSEEKLKKKDFETSQ 1091
Cdd:pfam18971 773 ENSVKDVIINQKVTDKVdNLNQAVSVAKAMGDFSRVEQVLADLKNfsKEQLAQQAQKNEDFNTGK 837
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1022-1182 |
1.36e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1022 LTKSKTKLEQQVDDLEGSLEQEKKLRM-----DLERAKRKLEGDLKLAQESIMDLENDKQQSEEKLKKKdfetSQLLSKI 1096
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIKKEALleakeEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRK----LELLEKR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1097 EDEqslgaqLQKKIKELQARIEEleeeieaeraarakVEKQRADLSRELEEISERLEEAGGATAAQI------EMNKKRE 1170
Cdd:PRK12704 109 EEE------LEKKEKELEQKQQE--------------LEKKEEELEELIEEQLQELERISGLTAEEAkeilleKVEEEAR 168
|
170
....*....|..
gi 288856329 1171 AEFQKLRRDLEE 1182
Cdd:PRK12704 169 HEAAVLIKEIEE 180
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1091-1242 |
1.61e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1091 QLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEA----GGATAAQIEMN 1166
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYeeqlGNVRNNKEYEA 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 288856329 1167 KKREAEFQKLRR-DLEESTLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEYKMEIDDLSSNMEAVAK 1242
Cdd:COG1579 94 LQKEIESLKRRIsDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1767-1925 |
1.65e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 43.77 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1767 MAEELKKEQDTSAHL-ERMKKNLEvTVKDLQHRLDEAENLAMKGGKKQLQKLeSRVRELESEVEAEQRR---GADAVK-- 1840
Cdd:PLN03188 1066 LAEELRTELDASRALaEKQKHELD-TEKRCAEELKEAMQMAMEGHARMLEQY-ADLEEKHIQLLARHRRiqeGIDDVKka 1143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1841 ----GVRKYERR-----VKELTYQTEEDKKNVNRLQDLVDKLQLKVkaykRQSEEAEEQANSHLSKLRKVQHELEEAEER 1911
Cdd:PLN03188 1144 aaraGVRGAESKfinalAAEISALKVEREKERRYLRDENKSLQAQL----RDTAEAVQAAGELLVRLKEAEEALTVAQKR 1219
|
170 180
....*....|....*....|.
gi 288856329 1912 ADIAE-------SQVNKLRAK 1925
Cdd:PLN03188 1220 AMDAEqeaaeayKQIDKLKRK 1240
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1308-1485 |
1.69e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1308 QAFTQQIEELKRQIEEevkaknaLAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRTKyetdaiqrtee 1387
Cdd:COG1579 13 QELDSELDRLEHRLKE-------LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR----------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1388 LEESKKKLAQrlQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANALAANLDKKQRNFDKVLAEWKQKYEEGQA 1467
Cdd:COG1579 75 IKKYEEQLGN--VRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
170
....*....|....*...
gi 288856329 1468 ELEGAQKEARSLSTELFK 1485
Cdd:COG1579 153 ELEAELEELEAEREELAA 170
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1522-1837 |
1.83e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.35 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1522 GKSIHELEKSKKAVETEKAEIQTALEEAEGTLEHEESKILRVQLELNQ-----------VKSEIDRKLAEKDEEIEQIKR 1590
Cdd:PLN02939 41 GFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQkstssdddhnrASMQRDEAIAAIDNEQQTNSK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1591 NSQRITD-----------SMQSTL----DSEVRSRNDALRI---KKKMEGDLNEMEIQLSHANRQAAEAQKQlrNVQAQL 1652
Cdd:PLN02939 121 DGEQLSDfqledlvgmiqNAEKNIlllnQARLQALEDLEKIlteKEALQGKINILEMRLSETDARIKLAAQE--KIHVEI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1653 KDAQLHL---DDAVRGQED------MKEQVAMVERRNTLMQSEIEELRAALEqtergrkvaeqELVDASERVGLLHSQNT 1723
Cdd:PLN02939 199 LEEQLEKlrnELLIRGATEglcvhsLSKELDVLKEENMLLKDDIQFLKAELI-----------EVAETEERVFKLEKERS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1724 SLLNTKKKLEADLVQIQSEVE-----------DTVQEARNAEDKAKKAITDAAMMaeeLKKEQDTSAHLERMKKNLEVT- 1791
Cdd:PLN02939 268 LLDASLRELESKFIVAQEDVSklsplqydcwwEKVENLQDLLDRATNQVEKAALV---LDQNQDLRDKVDKLEASLKEAn 344
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 288856329 1792 --------VKDLQHRLDEAENLAMKGGKK---QLQKLESRVRE----LESEVEAEQRRGAD 1837
Cdd:PLN02939 345 vskfssykVELLQQKLKLLEERLQASDHEihsYIQLYQESIKEfqdtLSKLKEESKKRSLE 405
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1380-1687 |
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 288856329 1380 DAIQRTEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANAL-AANLDKKQRNFDKV-LAE 1457
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALkDDNDEETRETLSTLsLRQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1458 WKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLETlkrenkNLQ--QEISDLTEQLGETGKSIHELEKSKKAV 1535
Cdd:PRK11281 126 LESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYA------NSQrlQQIRNLLKGGKVGGKALRPSQRVLLQA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1536 ETEKAEIQTALEEAE----------GTLEHEES--KILRVQLELNQVKSEIDRKLAEKDEEIEQIKRNSQRITDSMQSTL 1603
Cdd:PRK11281 200 EQALLNAQNDLQRKSlegntqlqdlLQKQRDYLtaRIQRLEHQLQLLQEAINSKRLTLSEKTVQEAQSQDEAARIQANPL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1604 dsevrsrndalrIKKkmEGDLNemeIQLSHANRQAAEAQKQLrnVQAQLKDAQLhLDDAVRGQEDMKEQVAMVerRNTLM 1683
Cdd:PRK11281 280 ------------VAQ--ELEIN---LQLSQRLLKATEKLNTL--TQQNLRVKNW-LDRLTQSERNIKEQISVL--KGSLL 337
|
....
gi 288856329 1684 QSEI 1687
Cdd:PRK11281 338 LSRI 341
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1143-1336 |
2.33e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1143 RELEEISERLEEAGGATAAQIEMNKKREA--EFQKLRRDLEESTLQHEATAAALRKKqadsvaeLGEQIDNLQRVKQKLE 1220
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAkeEIHKLRNEFEKELRERRNELQKLEKR-------LLQKEENLDRKLELLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1221 KEKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIkskndenlrqindlsaqrARLQTEngefgrqlEEKEALV 1300
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI------------------SGLTAE--------EAKEILL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 288856329 1301 SQLtrgKQAFTQQIEELKRQIEEEVK------AKNALAHAVQ 1336
Cdd:PRK12704 161 EKV---EEEARHEAAVLIKEIEEEAKeeadkkAKEILAQAIQ 199
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
886-1098 |
2.59e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.92 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 886 KNDLQ-LAVASESENLSDAEERCEGLiksKIQLEAKLKETTERLEDEEEINAeltakkRKLEDECSELKKDIDDLELTLA 964
Cdd:PLN03229 534 KYKLDmLNEFSRAKALSEKKSKAEKL---KAEINKKFKEVMDRPEIKEKMEA------LKAEVASSGASSGDELDDDLKE 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 965 KVEKEKHATENKVKNLTEEMAAQDESIgkltkEKKALQEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEK 1044
Cdd:PLN03229 605 KVEKMKKEIELELAGVLKSMGLEVIGV-----TKKNKDTAEQTPPPNLQEKIESLNEEINKKIERVIRSSDLKSKIELLK 679
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 288856329 1045 klrmdLERAKRKLEGDLKLAQEsimdLENDKQQSEEKLKKKdFETSQLLSKIED 1098
Cdd:PLN03229 680 -----LEVAKASKTPDVTEKEK----IEALEQQIKQKIAEA-LNSSELKEKFEE 723
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
910-1045 |
2.83e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.93 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 910 LIKSKIQLEAK----------LKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTL-AKVEKEKHATENKVK 978
Cdd:smart00787 121 LVKTFARLEAKkmwyewrmklLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALeEELRQLKQLEDELED 200
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 288856329 979 NLTEEMAAQDESIGKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEKK 1045
Cdd:smart00787 201 CDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
908-1628 |
3.23e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.90 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 908 EGLIKSKIQLEAKLKETTERLEDEEEINAELTAK-KRKLEDECSELKKDIDDLELTLAKVEKEKhaTENKVKNLTEEMAA 986
Cdd:PTZ00440 900 EHLLNNKIDLKNKLEQHMKIINTDNIIQKNEKLNlLNNLNKEKEKIEKQLSDTKINNLKMQIEK--TLEYYDKSKENING 977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 987 QDESIGKLTKEKKALQEAHQQTLDDL----QAEEDKVNTL-TKSKTKLEQQVDDLEGSLEQEKKLRMD-----LERAKRK 1056
Cdd:PTZ00440 978 NDGTHLEKLDKEKDEWEHFKSEIDKLnvnyNILNKKIDDLiKKQHDDIIELIDKLIKEKGKEIEEKVDqyislLEKMKTK 1057
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1057 LEgdLKLAQESIMDLENDKQQSEEKLKKKDFETsqLLSKIEDEQSLGAQLQKKIKE----LQARIEELEEEIEAERAARA 1132
Cdd:PTZ00440 1058 LS--SFHFNIDIKKYKNPKIKEEIKLLEEKVEA--LLKKIDENKNKLIEIKNKSHEhvvnADKEKNKQTEHYNKKKKSLE 1133
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1133 KVEKQRADLSRELEEISERLEEAGGATAAQIEmnkkreaeFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQIDN- 1211
Cdd:PTZ00440 1134 KIYKQMEKTLKELENMNLEDITLNEVNEIEIE--------YERILIDHIVEQINNEAKKSKTIMEEIESYKKDIDQVKKn 1205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1212 --LQRVKQKLEKEKSEYKMEIDDLSSNMEA-VAKAKANLEKMCRTLE-DQLSEIKSKNDENLRQI--NDLSAQRARLQTE 1285
Cdd:PTZ00440 1206 msKERNDHLTTFEYNAYYDKATASYENIEElTTEAKGLKGEANRSTNvDELKEIKLQVFSYLQQVikENNKMENALHEIK 1285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1286 NGEFGRQLEEKEALVSQLTRGkqafTQQIEELKRQIEEEVKAKNALAHAVqsarhdcdllreqfeEEQEAKAELQRGMSK 1365
Cdd:PTZ00440 1286 NMYEFLISIDSEKILKEILNS----TKKAEEFSNDAKKELEKTDNLIKQV---------------EAKIEQAKEHKNKIY 1346
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1366 ANSEVAQWRTKYETdAIQRTEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRlqgevedlmIDVERANALAANLD 1445
Cdd:PTZ00440 1347 GSLEDKQIDDEIKK-IEQIKEEISNKRKEINKYLSNIKSNKEKCDLHVRNASRGKDK---------IDFLNKHEAIEPSN 1416
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1446 KKQRNFDKVlAEWKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLETLKRENK--NLQQEISDLTEQLGETGK 1523
Cdd:PTZ00440 1417 SKEVNIIKI-TDNINKCKQYSNEAMETENKADENNDSIIKYEKEITNILNNSSILGKKTKleKKKKEATNIMDDINGEHS 1495
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1524 SIHE-LEKSKKAVETEKAeiQTALEEAEGTLEHEESKILRVQLELN--QVKSEIdrklaekdEEIEQIKRNSQRI----T 1596
Cdd:PTZ00440 1496 IIKTkLTKSSEKLNQLNE--QPNIKREGDVLNNDKSTIAYETIQYNlgRVKHNL--------LNILNIKDEIETIlnkaQ 1565
|
730 740 750
....*....|....*....|....*....|...
gi 288856329 1597 DSMQSTLD-SEVRSRNDALRIKKKMEGDLNEME 1628
Cdd:PTZ00440 1566 DLMRDISKiSKIVENKNLENLNDKEADYVKYLD 1598
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1288-1550 |
3.27e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.37 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1288 EFGRQLEEKEALvsqltrgKQAFtQQIEELKRQIEEevkaknaLAHAVQSARHDCDLLREQFEEEQEAkaELQRGmskan 1367
Cdd:COG0497 149 AFAGLEELLEEY-------REAY-RAWRALKKELEE-------LRADEAERARELDLLRFQLEELEAA--ALQPG----- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1368 sEVAQWRTKYET--------DAIQRT-EELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQG---EVEDLMIDVE 1435
Cdd:COG0497 207 -EEEELEEERRRlsnaeklrEALQEAlEALSGGEGGALDLLGQALRALERLAEYDPSLAELAERLESaliELEEAASELR 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1436 RanaLAANLDkkqrnFD-KVLAEWkqkyEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEISDL 1514
Cdd:COG0497 286 R---YLDSLE-----FDpERLEEV----EERLALLRRLARKYGVTVEELLAYAEELRAELAELENSDERLEELEAELAEA 353
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 288856329 1515 TEQLGETGKSIHEL-----EKSKKAVETE-------KAEIQTALEEAE 1550
Cdd:COG0497 354 EAELLEAAEKLSAArkkaaKKLEKAVTAEladlgmpNARFEVEVTPLE 401
|
|
| TTKRSYEDQ |
pfam10212 |
Predicted coiled-coil domain-containing protein; This is the C-terminal 500 amino acids of a ... |
1390-1593 |
3.35e-03 |
|
Predicted coiled-coil domain-containing protein; This is the C-terminal 500 amino acids of a family of proteins with a predicted coiled-coil domain conserved from nematodes to humans. It carries a characteriztic TTKRSYEDQ sequence-motif. The function is not known.
Pssm-ID: 463001 Cd Length: 523 Bit Score: 42.12 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1390 ESKKKLAQRLQEAEEQIeavnskcASLEKTKQRLQGEVEDLMIDVERANALAANLDKKQRNFDKVLAEWKQKYEEGQAEL 1469
Cdd:pfam10212 302 ESREGLAQQVQQSQEKI-------AKLEQEKEHWMLEAQLLKIKLEKENQRIADLEKQLLKGSTSGQLPELVQSKATLPL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1470 EGAQKEARS--------LSTELFKMKNSYEETLDQLETLKREN---KNLQQEISDLTEQLGET-GKSIH----------E 1527
Cdd:pfam10212 375 TAKQGSEASsisekeptPSTSLIGMLTVTTDSEESSDEESREQlikSHYMARIAELTSQLQLAdSKAVHfhaecralakR 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1528 LEKSKKAVETEKAEIQTAleeaegtleheESKILRVQLELNQVKSE--------------IDRKLAEKDEEIEQIKRNSQ 1593
Cdd:pfam10212 455 LALAEKSKESLTEELKLA-----------NQNISRLQDELTTTKRSyedqlsmmsdhlcsMNETLTKQREEIDTLKMASK 523
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1208-1339 |
3.57e-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: 41.06 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1208 QIDNLQRVKQKLEKEKSEYKMEIDDLSSNMEAVAKAKANLEKMCRTLEDQLSEIKSKNDEN----------------LRQ 1271
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrnnkeyealQKE 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 288856329 1272 INDLSAQRARLQTENGEFGRQLEEKEALVSQLTRGKQAFTQQIEELKRQIEEEVKAKNALAHAVQSAR 1339
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1451-1588 |
3.57e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1451 FDKVLAEWKQKYEEGQAE--LEGAQKEARSLSTElfKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLgetgksihel 1528
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKriLEEAKKEAEAIKKE--ALLEAKEEIHKLRNEFEKELRERRNELQKLEKRL---------- 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1529 eKSKKAVETEKAEiqtALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEEIEQI 1588
Cdd:PRK12704 92 -LQKEENLDRKLE---LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1682-1924 |
3.71e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1682 LMQSEIEELRAALEQTERGRKVAEQELVDASERVGLLHSQNTSLLNTKKKLEADLVQIQSEVedtvqearnaeDKAKKAI 1761
Cdd:pfam00038 51 LYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDL-----------DEATLAR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1762 TDAAMMAEELKKEqdtsahLERMKKNLEVTVKDLQHRL-DEAENLAMKGGKKQlqKLESRVRELESEVEAEQRRgadavk 1840
Cdd:pfam00038 120 VDLEAKIESLKEE------LAFLKKNHEEEVRELQAQVsDTQVNVEMDAARKL--DLTSALAEIRAQYEEIAAK------ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1841 gvrkyERRVKELTYQT--EEDKKNVNRLQDLVDKLQLKVKAYKRQSEEAEEQANSHLSKLRKVQHELEEAEERADIAESQ 1918
Cdd:pfam00038 186 -----NREEAEEWYQSklEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLAD 260
|
....*.
gi 288856329 1919 VNKLRA 1924
Cdd:pfam00038 261 YQELIS 266
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
893-1008 |
3.84e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 893 VASESENLsdaEERCEGLIKSKIQLEAKLKETTERLEDEEEINAELTAKKRKLEDecsELKKDIDDLELTLAK-VEKEKH 971
Cdd:PRK00409 511 IGEDKEKL---NELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQE---EEDKLLEEAEKEAQQaIKEAKK 584
|
90 100 110
....*....|....*....|....*....|....*....
gi 288856329 972 ATENKVKNLTEEMAAQDESIG--KLTKEKKALQEAHQQT 1008
Cdd:PRK00409 585 EADEIIKELRQLQKGGYASVKahELIEARKRLNKANEKK 623
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1386-1542 |
3.90e-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: 42.35 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1386 EELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLmidvERANALAANLDKKQRNFDKVLAEWKQKYEeg 1465
Cdd:pfam05911 691 EQLKSEKENLEVELASCTENLESTKSQLQESEQLIAELRSELASL----KESNSLAETQLKCMAESYEDLETRLTELE-- 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1466 qAELEGAQKEARSLSTELFKMKNSYEETL-------DQLETLKR----------ENKNLQQ--EISDLTEQLGETGKSIH 1526
Cdd:pfam05911 765 -AELNELRQKFEALEVELEEEKNCHEELEakclelqEQLERNEKkessncdadqEDKKLQQekEITAASEKLAECQETIL 843
|
170
....*....|....*.
gi 288856329 1527 ELEKSKKAVETEKAEI 1542
Cdd:pfam05911 844 NLGKQLKALASPQDAS 859
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1723-1878 |
3.91e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1723 TSLLNTKKKLEADLVQIQSEVEDTVQEARNAEDKAKK---AITDAAMMAEELKKE--------------QDTSAHLERMK 1785
Cdd:PHA02562 223 DELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKlntAAAKIKSKIEQFQKVikmyekggvcptctQQISEGPDRIT 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1786 KNLEvTVKDLQHRLDEAENLAMKGGKK--QLQKLESRVRELESEVEAEQRRGADAVKGVRKYERRVKELTYQ----TEED 1859
Cdd:PHA02562 303 KIKD-KLKELQHSLEKLDTAIDELEEImdEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEfvdnAEEL 381
|
170
....*....|....*....
gi 288856329 1860 KKNVNRLQDLVDKLQLKVK 1878
Cdd:PHA02562 382 AKLQDELDKIVKTKSELVK 400
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1794-1925 |
4.01e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1794 DLQHRLDEAENLA--MKGGKKQLQKLESRVRELESEVEAEQRRGADAVKGVRKYERRVKELTYQTEEDKKNVNRLQDL-- 1869
Cdd:COG1579 11 DLQELDSELDRLEhrLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNke 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 288856329 1870 VDKLQLKVKAYKRQSEEAEEQANSHLSKLRKVQHELEEAEERADIAESQVNKLRAK 1925
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE 146
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1639-1831 |
4.12e-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: 41.06 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1639 AEAQKQLRNVQAQLkdaqLHLDDAVRGQEDMKEQVAMVERRNTLMQSEIEELRAALEQTERGRKVAEQELVDASERVgll 1718
Cdd:COG1579 3 PEDLRALLDLQELD----SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1719 hSQNTSLLNTKKKLEaDLVQIQSEVEDTVQEARNAEDKAKKAITDAAMMAEELKKEQdtsAHLERMKKNLEVTVKDLQHR 1798
Cdd:COG1579 76 -KKYEEQLGNVRNNK-EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELE---AELAELEAELEEKKAELDEE 150
|
170 180 190
....*....|....*....|....*....|...
gi 288856329 1799 LDEAEnlamkggkKQLQKLESRVRELESEVEAE 1831
Cdd:COG1579 151 LAELE--------AELEELEAEREELAAKIPPE 175
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1002-1913 |
4.15e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.12 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1002 QEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQekkLRMDLERAKRklegdlKLAQESIMDLENDKQQSEEK 1081
Cdd:NF041483 7 QESHRADDDHLSRFEAEMDRLKTEREKAVQHAEDLGYQVEV---LRAKLHEARR------SLASRPAYDGADIGYQAEQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1082 LKKKDFETSQLLSKIEDE-QSLGAQLQKKIKElqarieELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATA 1160
Cdd:NF041483 78 LRNAQIQADQLRADAERElRDARAQTQRILQE------HAEHQARLQAELHTEAVQRRQQLDQELAERRQTVESHVNENV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1161 AQIEMNKKREAefQKLRRDLEESTLQHEATAAALRkKQADSVAElgeqidnlqRVKQKLEKEKSEYKMEIDDLssnmeaV 1240
Cdd:NF041483 152 AWAEQLRARTE--SQARRLLDESRAEAEQALAAAR-AEAERLAE---------EARQRLGSEAESARAEAEAI------L 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1241 AKAKANLEKMCRTLEDQLSEIKSkNDENLRQINDLSAQRARLQTenGEFGRQLEEKEALVSQLTRGKQAftqQIEELKRQ 1320
Cdd:NF041483 214 RRARKDAERLLNAASTQAQEATD-HAEQLRSSTAAESDQARRQA--AELSRAAEQRMQEAEEALREARA---EAEKVVAE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1321 IEEEVKAKNALAHAVQSAR------HDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRTKYETDAiqRTEELEESKKK 1394
Cdd:NF041483 288 AKEAAAKQLASAESANEQRtrtakeEIARLVGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKA--RTVAAEDTAAQ 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1395 LAQRLQEAEEQIEAVN------SKCASLEKTKQRLQGEVEdlmidVERANALAANLDkkqrnfDKVLAEWKQKYEEGQAE 1468
Cdd:NF041483 366 LAKAARTAEEVLTKASedakatTRAAAEEAERIRREAEAE-----ADRLRGEAADQA------EQLKGAAKDDTKEYRAK 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1469 LEGAQKEARSLSTELFKMKnsyEETLDQLETLKRENKNlqqeisDLTEQLGETGKSIHELEKSKKAVETEKAEIQTALEE 1548
Cdd:NF041483 435 TVELQEEARRLRGEAEQLR---AEAVAEGERIRGEARR------EAVQQIEEAARTAEELLTKAKADADELRSTATAESE 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1549 AEGTLEHEESKILRVQLE--LNQVKSEIDRKLAEKDEEIEQIKRNSQRitdsmqstldSEVRSRNDALRikkkmegdlne 1626
Cdd:NF041483 506 RVRTEAIERATTLRRQAEetLERTRAEAERLRAEAEEQAEEVRAAAER----------AARELREETER----------- 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1627 meiqlSHANRQAAEAqkqlrnvqaqlkdaqlhlDDAVRGQEDMKEQVAMVERRNTLMQSEIEELR-AALEQTERGRkvae 1705
Cdd:NF041483 565 -----AIAARQAEAA------------------EELTRLHTEAEERLTAAEEALADARAEAERIRrEAAEETERLR---- 617
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1706 qelVDASERVGLLHSQntsllntkkkLEADLVQIQSEVEDTVQEAR-NAEDKAKKAITDAAMMAEELKKE-QDTS----- 1778
Cdd:NF041483 618 ---TEAAERIRTLQAQ----------AEQEAERLRTEAAADASAARaEGENVAVRLRSEAAAEAERLKSEaQESAdrvra 684
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1779 ---AHLERM----KKNLEVTVKDLQHRLDEAENLaMKGGKKQLQKLESRVRELESEVEAEQRR-----GADAVKGVRKYE 1846
Cdd:NF041483 685 eaaAAAERVgteaAEALAAAQEEAARRRREAEET-LGSARAEADQERERAREQSEELLASARKrveeaQAEAQRLVEEAD 763
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 288856329 1847 RRVKELTYQTEEDKKNVnrlQDLVDKLQlkvkaykrqseeaeEQANSHLSKLRK-VQHELE----EAEERAD 1913
Cdd:NF041483 764 RRATELVSAAEQTAQQV---RDSVAGLQ--------------EQAEEEIAGLRSaAEHAAErtrtEAQEEAD 818
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1441-1931 |
4.43e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.02 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1441 AANLDKKQRNFDKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGE 1520
Cdd:pfam05483 87 AEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCAR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1521 TGKSIHELEKSKKAVETEKAEIQTALEEAEGTLEHeeskiLRVQLElnQVKSEIDRKLAEKDEEIEQIKRNSQRitdsmq 1600
Cdd:pfam05483 167 SAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEE-----LRVQAE--NARLEMHFKLKEDHEKIQHLEEEYKK------ 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1601 stldsevrsrndalrikkkmegDLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAMVERRN 1680
Cdd:pfam05483 234 ----------------------EINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1681 TLMQSEIEELRAALEQTERGRKVAEQELVDASERVGLLHSQNTSLLNTKKKLEADLVQIQSEVEDTV----QEARNAEDK 1756
Cdd:pfam05483 292 DHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTcsleELLRTEQQR 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1757 AKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENL------------AMKGGKKQL---------- 1814
Cdd:pfam05483 372 LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLldekkqfekiaeELKGKEQELifllqareke 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1815 ---------------QKLESRVRELESEVEAEQ---------------------RRGADAVKGVRKYERRVKELTYQTEE 1858
Cdd:pfam05483 452 ihdleiqltaiktseEHYLKEVEDLKTELEKEKlknieltahcdklllenkeltQEASDMTLELKKHQEDIINCKKQEER 531
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 288856329 1859 DKKNVNRLQD----LVDKLQLKVKAYKRQSEEAEEQANSHLSKLRKVQHELEEAEERADIAESQVNKLRAKSRDSGK 1931
Cdd:pfam05483 532 MLKQIENLEEkemnLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNK 608
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1751-1913 |
4.50e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1751 RNAEDKAKKAITDAAMMAEELKKEqdtsahLERMKKNLEVTVKDLQHRL-DEAENlAMKGGKKQLQKLESRVRELESEVE 1829
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKE------AEAIKKEALLEAKEEIHKLrNEFEK-ELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1830 AEQRRgadavkgVRKYERRVKELTYQTEEDKKNVNRLQDLVDKLQLK-VKAYKR----QSEEAEEQAnshLSKLR-KVQH 1903
Cdd:PRK12704 100 RKLEL-------LEKREEELEKKEKELEQKQQELEKKEEELEELIEEqLQELERisglTAEEAKEIL---LEKVEeEARH 169
|
170
....*....|....*...
gi 288856329 1904 EL--------EEAEERAD 1913
Cdd:PRK12704 170 EAavlikeieEEAKEEAD 187
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
977-1113 |
4.70e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 977 VKNLTEEMAAQDESIGKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEqekklrmDLERAKRK 1056
Cdd:COG2433 373 IRGLSIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELE-------EKDERIER 445
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 288856329 1057 LEGDLKLAQESimdlENDKQQSEEKLKKKDFETSQLLSKIEDEQSLGAQLQKKIKEL 1113
Cdd:COG2433 446 LERELSEARSE----ERREIRKDREISRLDREIERLERELEEERERIEELKRKLERL 498
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1472-1707 |
4.87e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1472 AQKEARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEKskkavetEKAEIQTALEEAEG 1551
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA-------EIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1552 TLEheesKILRVQLELNQVKSEIDRKLAEKD--EEIEQIkRNSQRITDSMQSTLDSEVRSRNDALRIKKKMEGDLNEMEI 1629
Cdd:COG3883 87 ELG----ERARALYRSGGSVSYLDVLLGSESfsDFLDRL-SALSKIADADADLLEELKADKAELEAKKAELEAKLAELEA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 288856329 1630 QLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAMVERRNTLMQSEIEELRAALEQTERGRKVAEQE 1707
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1793-1937 |
5.82e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1793 KDLQHRLDEAEN----LAMKGGKKQLQKLESRVRELESEVEAEQRRGADAVKGVRKYERRVKELTYQTEEDKKNVNRLQD 1868
Cdd:COG1196 216 RELKEELKELEAelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 288856329 1869 LVDKLQLKVKAYKRQSEEAEEQANSHLSKLRKVQHELEEAEERADIAESQVNKLRAKSRDSGKGKDAAE 1937
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
898-1037 |
5.87e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 898 ENLSDAEERCEGLIKSKIQLEAKLKETTERLEDEEEinaELTAKKRKLEDECSELKKDIDDLeltLAKVEKEkhaTENKV 977
Cdd:PRK00409 509 KLIGEDKEKLNELIASLEELERELEQKAEEAEALLK---EAEKLKEELEEKKEKLQEEEDKL---LEEAEKE---AQQAI 579
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 978 KNLTEEMAAQDESIGKLTKEKKALQEAHQQTlDDLQAEEDKVNTLTKSKTKLEQQVDDLE 1037
Cdd:PRK00409 580 KEAKKEADEIIKELRQLQKGGYASVKAHELI-EARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
929-1179 |
6.98e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.45 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 929 EDEEEINAELTAKKRKLEDECSELkkdIDDLElTLAKVEKEKHATENKVKnlteemaaqdesigkltkeKKALQEAHQQT 1008
Cdd:PRK05771 35 DLKEELSNERLRKLRSLLTKLSEA---LDKLR-SYLPKLNPLREEKKKVS-------------------VKSLEELIKDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1009 LDDLQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEKKLR---MDLERAKRK-----LEGDLKLAQESIMDLENDKQQSEE 1080
Cdd:PRK05771 92 EEELEKIEKEIKELEEEISELENEIKELEQEIERLEPWGnfdLDLSLLLGFkyvsvFVGTVPEDKLEELKLESDVENVEY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1081 KLKKKDFETSQLLSKIEDEQSLGAQLQK---KIKELQARIEELEEEIEAERAARaKVEKQRADLSRELEEISERLEEAGG 1157
Cdd:PRK05771 172 ISTDKGYVYVVVVVLKELSDEVEEELKKlgfERLELEEEGTPSELIREIKEELE-EIEKERESLLEELKELAKKYLEELL 250
|
250 260
....*....|....*....|..
gi 288856329 1158 ATAAQIEMNKKREAEFQKLRRD 1179
Cdd:PRK05771 251 ALYEYLEIELERAEALSKFLKT 272
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1383-1749 |
7.26e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1383 QRTEELEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLMIDVERANALAANLDKKQRNFDKVLAEWKQKY 1462
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1463 EEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLTEQLGETGKSIHELEKSKKAVETEKAEI 1542
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1543 QTALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEEIEQIKRNSQRITDSMQSTLDSEVRSRNDALRIKKKMEG 1622
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1623 DLNEMEIQLSHANRQAAEAQKQLRNVQAQLKDAQLHLDDAVRGQEDMKEQVAMVERRNTLMQSEIEELRAALEQTERGRK 1702
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 288856329 1703 VAEQELVDASERVGLLHSQNTSLLNTKKKLEADLVQIQSEVEDTVQE 1749
Cdd:COG4372 323 ELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1779-1925 |
7.47e-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: 40.29 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1779 AHLERMKKNLEVTVKDLQHRLDEAENlAMKGGKKQLQKLESRVRELESEVEAEQRRGA------DAVKGVRKYERRVKEL 1852
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEA-RLEAAKTELEDLEKEIKRLELEIEEVEARIKkyeeqlGNVRNNKEYEALQKEI 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 288856329 1853 TYQTEEDKKNVNRLQDLVDKLQLKVKAYKRQSEEAEEQANSHLSKLRKVQHELEEAEERADIAESQVNKLRAK 1925
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1266-1596 |
7.74e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1266 DENLRQINDLSAQRARLQTEN---GEFGRQLEEkealvsqLTRGKQAFTQQIEELKRQIEeevKAKNALAHAVQSARHDC 1342
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQyrlVEMARELAE-------LNEAESDLEQDYQAASDHLN---LVQTALRQQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1343 DL--LREQFEEEQEAKAEL--QRGMSKANSEVAQwrtkyetdaiqrtEELEESKKKLA---QRLQEAEEQIEAVNSKCAS 1415
Cdd:PRK04863 356 DLeeLEERLEEQNEVVEEAdeQQEENEARAEAAE-------------EEVDELKSQLAdyqQALDVQQTRAIQYQQAVQA 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1416 LEKTKQRLQgeVEDLmiDVERANALAANLDKKQRNFDKVLAEWKQKYEEGQA---ELEGAQKEARSLSTELFK--MKNSY 1490
Cdd:PRK04863 423 LERAKQLCG--LPDL--TADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsQFEQAYQLVRKIAGEVSRseAWDVA 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1491 EETLDQLETLKRENKNLQQ---EISDLTEQLGETGKSIH---ELEKSKKAVETEKAEIQTALEEAEGTLEHeeskilrvq 1564
Cdd:PRK04863 499 RELLRRLREQRHLAEQLQQlrmRLSELEQRLRQQQRAERllaEFCKRLGKNLDDEDELEQLQEELEARLES--------- 569
|
330 340 350
....*....|....*....|....*....|..
gi 288856329 1565 leLNQVKSEIDRKLAEKDEEIEQIKRNSQRIT 1596
Cdd:PRK04863 570 --LSESVSEARERRMALRQQLEQLQARIQRLA 599
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
881-1043 |
7.94e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 39.74 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 881 ALLQEKNDLQLAVASESENLSDAEERCEGLIKSKIQLEAKLKETTERLEDE-EEINAELTAKKRKLED---------ECS 950
Cdd:cd00176 37 ALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRwEELRELAEERRQRLEEaldlqqffrDAD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 951 ELKKDIDDLELTLAKVEKEKHATE-----NKVKNLTEEMAAQDESIGKLTKEKKALQEAHQQtlDDLQAEEDKVNTLTKS 1025
Cdd:cd00176 117 DLEQWLEEKEAALASEDLGKDLESveellKKHKELEEELEAHEPRLKSLNELAEELLEEGHP--DADEEIEEKLEELNER 194
|
170
....*....|....*...
gi 288856329 1026 KTKLEQQVDDLEGSLEQE 1043
Cdd:cd00176 195 WEELLELAEERQKKLEEA 212
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1256-1654 |
8.07e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1256 DQLSEIKSKNDENLRQINDLSAQRARL-QTEngefgRQLEEKEALVSQLTrgkQAfTQQIEELKRQIEEeVKAKNALAHA 1334
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEQTLALLdKID-----RQKEETEQLKQQLA---QA-PAKLRQAQAELEA-LKDDNDEETR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1335 VQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRTKYEtdaiqRTE-ELEESkkklAQRLQEAEEQIEAVN-SK 1412
Cdd:PRK11281 116 ETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPE-----RAQaALYAN----SQRLQQIRNLLKGGKvGG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1413 CASLEKTKQRLQGEVE--DLMIDVERaNALAAN-----LDKKQRNFdkvLAEWKQKYEEGQAELEGAQKEAR-SLStelf 1484
Cdd:PRK11281 187 KALRPSQRVLLQAEQAllNAQNDLQR-KSLEGNtqlqdLLQKQRDY---LTARIQRLEHQLQLLQEAINSKRlTLS---- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1485 kmknsyEETLDQLETLKRENKN-----LQQEIS---DLTEQLGETGKSIHELekSKKAVETEK-----AEIQTALEEA-- 1549
Cdd:PRK11281 259 ------EKTVQEAQSQDEAARIqanplVAQELEinlQLSQRLLKATEKLNTL--TQQNLRVKNwldrlTQSERNIKEQis 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1550 --EGTLEHeeSKIL-RVQLELNQVKseIDRKLAEK--DEEIEQIKRNSQR------------ITDSMQSTLDSEVR-SRN 1611
Cdd:PRK11281 331 vlKGSLLL--SRILyQQQQALPSAD--LIEGLADRiaDLRLEQFEINQQRdalfqpdayidkLEAGHKSEVTDEVRdALL 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 288856329 1612 DALRIKKKMEGDLN-EMEIQLSHA-NRQAaeAQKQLRNVQAQLKD 1654
Cdd:PRK11281 407 QLLDERRELLDQLNkQLNNQLNLAiNLQL--NQQQLLSVSDSLQS 449
|
|
| PRK10361 |
PRK10361 |
DNA recombination protein RmuC; Provisional |
926-1109 |
8.27e-03 |
|
DNA recombination protein RmuC; Provisional
Pssm-ID: 182409 [Multi-domain] Cd Length: 475 Bit Score: 40.74 E-value: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 926 ERLEDEEEINAELTAKKRKL------EDECSELKkdiddleltlakvekekhateNKVKNLTEEMAAQDESIGKLTKEKK 999
Cdd:PRK10361 33 EQLAEREEMVAELSAAKQQItqsehwRAECELLN---------------------NEVRSLQSINTSLEADLREVTTRME 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1000 ALQeahqqtlddlQAEEDKVNTLTKSKTKLEQQVDDLEGSLEQEKKLRMDlERAKRKLEGDLKLAQESimdLENDKQQSE 1079
Cdd:PRK10361 92 AAQ----------QHADDKIRQMINSEQRLSEQFENLANRIFEHSNRRVD-EQNRQSLNSLLSPLREQ---LDGFRRQVQ 157
|
170 180 190
....*....|....*....|....*....|
gi 288856329 1080 EKLKKKDFETSQLLSKIEDEQSLGAQLQKK 1109
Cdd:PRK10361 158 DSFGKEAQERHTLAHEIRNLQQLNAQMAQE 187
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1314-1535 |
8.38e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1314 IEElKRQIEEEVKAKN-----ALAHAVQSARHdcdlLREQFEE-EQEAKAELQRGMSKAnsEVAQWRTKYETDAIQRTEE 1387
Cdd:COG2433 317 VEE-KLHLAREYGYDNdherdALAAALKAYDA----YKNKFERvEKKVPPDVDRDEVKA--RVIRGLSIEEALEELIEKE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1388 LEESKKKLAQRLQEAEEQIEAVNSKCASLEKTKQRLQGEVEDLmidveranalaanldkKQRnfdkvLAEWKQKYEEGQA 1467
Cdd:COG2433 390 LPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEEL----------------EAE-----LEEKDERIERLER 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 288856329 1468 ELEGAQKEARS---LSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLteqlgetgKSIHELEKSKKAV 1535
Cdd:COG2433 449 ELSEARSEERReirKDREISRLDREIERLERELEEERERIEELKRKLERL--------KELWKLEHSGELV 511
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1133-1327 |
8.70e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1133 KVEKQRADLSRELEEISERLEEAGGATAAQIEMNKKREAEFQKlrrDLEESTLQHEataaalrkkqaDSVAELGEQIDNL 1212
Cdd:PRK05771 47 KLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIK---DVEEELEKIE-----------KEIKELEEEISEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1213 QRVKQKLEKEKSE------YKMEIDDL--SSNMEA-VAKAKANLEKMCRTLEDQLSEIKSKNDEN--------------- 1268
Cdd:PRK05771 113 ENEIKELEQEIERlepwgnFDLDLSLLlgFKYVSVfVGTVPEDKLEELKLESDVENVEYISTDKGyvyvvvvvlkelsde 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1269 -LRQINDLSAQRARLQTEnGEFGRQLEEKEALVSQLTRGKQAFTQQIEELKRQIEEEVKA 1327
Cdd:PRK05771 193 vEEELKKLGFERLELEEE-GTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLA 251
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1738-1922 |
8.96e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 40.01 E-value: 8.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1738 QIQSEVEDTVQEARNAEDK---AKKAITDAAMMAEELKKE-QDTSAHLERMKKNLEVTvkdlQHRLDEAENLA------M 1807
Cdd:pfam00261 5 QIKEELDEAEERLKEAMKKleeAEKRAEKAEAEVAALNRRiQLLEEELERTEERLAEA----LEKLEEAEKAAdesergR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1808 KGGKKQLQKLESRVRELESEVEAEQRRGADAVKGVRKYERRVKELTYQTE--EDK--KNVNRLQDLVDKLQL---KVKAY 1880
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLEraEERaeLAESKIVELEEELKVvgnNLKSL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 288856329 1881 KRQSEEAEEQANSHLSKLRKVQHELEEAEERADIAESQVNKL 1922
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKL 202
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1163-1900 |
9.64e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1163 IEMNKKREAEFQKLrrdLEEST-------LQHEA-------TAAALRKKQADSVAELGEQIDNLQRVKQKLE---KEKSE 1225
Cdd:PRK04863 249 IRVTQSDRDLFKHL---ITESTnyvaadyMRHANerrvhleEALELRRELYTSRRQLAAEQYRLVEMARELAelnEAESD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1226 YKMEIDDLSSNMEAVAKAKANLEKMCRTLEDqLSEIKSKNDENLRQINDLSAQRARLQTEngeFGRQLEEKEALVSQLTR 1305
Cdd:PRK04863 326 LEQDYQAASDHLNLVQTALRQQEKIERYQAD-LEELEERLEEQNEVVEEADEQQEENEAR---AEAAEEEVDELKSQLAD 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1306 GKQAF-TQQIEELKRQieeevKAKNALahavQSARHDCDL--------------LREQFEEEQEAKAELQRGMSKANSEV 1370
Cdd:PRK04863 402 YQQALdVQQTRAIQYQ-----QAVQAL----ERAKQLCGLpdltadnaedwleeFQAKEQEATEELLSLEQKLSVAQAAH 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1371 AQWRTKYE-----TDAIQRTEELEESKKKLAQ--RLQEAEEQIEAVNSKCASLEktkQRLQgevedlmidveranalaan 1443
Cdd:PRK04863 473 SQFEQAYQlvrkiAGEVSRSEAWDVARELLRRlrEQRHLAEQLQQLRMRLSELE---QRLR------------------- 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1444 ldkKQRNFDKVLAEWKQKYEEGQAELEGAQKEARSLSTELFKMKNSYEETLDQLETLKRENKNLQQEISDLT-------- 1515
Cdd:PRK04863 531 ---QQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAarapawla 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1516 ---------EQLGETGKSIHELEKSKKavetekaeiQTALEEAEGTLEHEEskilrVQLELNQVKSEIDRKLAEKDEEIE 1586
Cdd:PRK04863 608 aqdalarlrEQSGEEFEDSQDVTEYMQ---------QLLERERELTVERDE-----LAARKQALDEEIERLSQPGGSEDP 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1587 QIKRNSQRITDSMQSTLDSEVrSRNDAlrikkkmeGDLNEMEIQLSHA--NRQAAEAQKQLRNVQAQLKDAQL------H 1658
Cdd:PRK04863 674 RLNALAERFGGVLLSEIYDDV-SLEDA--------PYFSALYGPARHAivVPDLSDAAEQLAGLEDCPEDLYLiegdpdS 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1659 LDDAVRGQEDMKEQVAMVERRNTLMQSEIEEL----RAA----LEQTERGRKVAEQELVDASERVGL---LHSQNTSLLN 1727
Cdd:PRK04863 745 FDDSVFSVEELEKAVVVKIADRQWRYSRFPEVplfgRAArekrIEQLRAEREELAERYATLSFDVQKlqrLHQAFSRFIG 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1728 TK-------------KKLEADLVQIQSEVED---TVQEARNAEDKAKKAITDAAMMAEELKKEQDTSaHLERmkknlevt 1791
Cdd:PRK04863 825 SHlavafeadpeaelRQLNRRRVELERALADhesQEQQQRSQLEQAKEGLSALNRLLPRLNLLADET-LADR-------- 895
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288856329 1792 VKDLQHRLDEAEN----LAMKGGK-KQLQKLESRVRELESEVEAEQRRGADAVKGVRKYERRVKELTY--------QTEE 1858
Cdd:PRK04863 896 VEEIREQLDEAEEakrfVQQHGNAlAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEvvqrrahfSYED 975
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 288856329 1859 DKKNVNRLQDLVDKLQLKVKAYKRQSEEAEEQANSHLSKLRK 1900
Cdd:PRK04863 976 AAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQ 1017
|
|
| |
