|
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, ... |
93-761 |
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: 1265.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITG 172
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 173 ESGAGKTENTKKVIAYFAHVGATSKKEEvKKDTKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGKL 252
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKK-ESGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 253 AGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGLKDKLLL**DVHEFHFVSQGKTGIAGVDDGEELVVTDTAFDV 332
Cdd:cd01377 160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 333 LGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGRNIT 412
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 413 QVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVLEQ 492
Cdd:cd01377 320 QVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 493 EEYKREGIEWEFIDFGLDLQACIELIEKP-MGLLSIMEEESMFPKATDQTFLEKLKTNHLGKSPNFikpKPPKPNQTEAH 571
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNF---KKPKPKKSEAH 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 572 FAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHpglgGGDDKGGKGGRKKGSGFQTVSGLYREQL 651
Cdd:cd01377 477 FILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDY----EESGGGGGKKKKKGGSFRTVSQLHKEQL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 652 NKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILAPNAVPKGFV 731
Cdd:cd01377 553 NKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFD 632
|
650 660 670
....*....|....*....|....*....|
gi 556079866 732 DAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd01377 633 DGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
93-761 |
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: 1196.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITG 172
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 173 ESGAGKTENTKKVIAYFAHVGATSKKEEVKKdtKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGKL 252
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAK--SKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 253 AGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGLKDKLLL**DVHEFHFVSQGKTGIAGVDDGEELVVTDTAFDV 332
Cdd:cd14909 159 AGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 333 LGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGRNIT 412
Cdd:cd14909 239 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 413 QVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVLEQ 492
Cdd:cd14909 319 QVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 493 EEYKREGIEWEFIDFGLDLQACIELIEKPMGLLSIMEEESMFPKATDQTFLEKLKTNHLGKSPNFIKPKPPKPNQTEAHF 572
Cdd:cd14909 399 EEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQAAHF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 573 AIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHPGLGGGDDKGGKGGRKKGSGFQTVSGLYREQLN 652
Cdd:cd14909 479 AIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKKGGGFATVSSAYKEQLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 653 KLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILAPNAVpKGFVD 732
Cdd:cd14909 559 SLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGI-QGEED 637
|
650 660
....*....|....*....|....*....
gi 556079866 733 AKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd14909 638 PKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
74-773 |
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: 1000.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 74 NPPKFEKCEDMSSLTYLNDASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSD 153
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 154 GAYMDMLANRENQSMLITGESGAGKTENTKKVIAYFAHVGATSkkeevkkdTKKGNLEDQVVQTNPVLESFGNAKTVRND 233
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSN--------TEVGSVEDQILESNPILEAFGNAKTLRNN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 234 NSSRFGKFIRIHFGPMGKLAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGLKDKLLL**dVHEFHFVSQGKTG 313
Cdd:smart00242 153 NSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQGGCL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 314 -IAGVDDGEELVVTDTAFDVLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEA-DGTEEGERVAHLLGLNAADLYK 391
Cdd:smart00242 232 tVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTvKDKEELSNAAELLGVDPEELEK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 392 NLLKPRIKVGTEFVTQGRNITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQHFIGVLDIAGFEIFDHNSFEQMC 471
Cdd:smart00242 312 ALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLC 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 472 INFTNEKLQQFFNHHMFVLEQEEYKREGIEWEFIDFGlDLQACIELIE-KPMGLLSIMEEESMFPKATDQTFLEKLKtNH 550
Cdd:smart00242 392 INYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKLN-QH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 551 LGKSPNFIKPKppkpNQTEAHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHPglgggddkgg 630
Cdd:smart00242 470 HKKHPHFSKPK----KKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGV---------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 631 kGGRKKGSGFQTVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMI 710
Cdd:smart00242 536 -SNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLP 614
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556079866 711 YPDFKQRYTILAPNAVPKGFVDAKNVSEKVIEAIQLDANDFRFGHSKIFFRAGVLGRLEEMRD 773
Cdd:smart00242 615 FDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
93-761 |
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: 999.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITG 172
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 173 ESGAGKTENTKKVIAYFAHVGA---TSKKEEVKKDTKKG-NLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGP 248
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAAlgdGPGKKAQFLATKTGgTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 249 MGKLAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGLKDKLLL**DVHEFHFVSQGKTGIAGVDDGEELVVTDT 328
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 329 AFDVLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQG 408
Cdd:cd14927 241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 409 RNITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMF 488
Cdd:cd14927 321 QSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 489 VLEQEEYKREGIEWEFIDFGLDLQACIELIEKPMGLLSIMEEESMFPKATDQTFLEKLKTNHLGKSPNFIKPKPPKPNQT 568
Cdd:cd14927 401 ILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKRKY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 569 EAHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDH--PGLGGGDDKGGKGGRKKGSGFQTVSGL 646
Cdd:cd14927 481 EAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYvgSDSTEDPKSGVKEKRKKAASFQTVSQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 647 YREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILAPNAV 726
Cdd:cd14927 561 HKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAI 640
|
650 660 670
....*....|....*....|....*....|....*.
gi 556079866 727 PK-GFVDAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd14927 641 PDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
82-761 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 987.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 82 EDMSSLTYLNDASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLA 161
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 162 NRENQSMLITGESGAGKTENTKKVIAYFAHVGATSKKEEVkkdtkkGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKF 241
Cdd:pfam00063 82 DKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNV------GRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 242 IRIHFGPMGKLAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAgLKDKLLL**DVHEFHFVSQ-GKTGIAGVDDG 320
Cdd:pfam00063 156 IEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASA-QLKKELRLTNPKDYHYLSQsGCYTIDGIDDS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 321 EELVVTDTAFDVLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKV 400
Cdd:pfam00063 235 EEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 401 GTEFVTQGRNITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQ-KRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKL 479
Cdd:pfam00063 315 GRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTiEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 480 QQFFNHHMFVLEQEEYKREGIEWEFIDFGlDLQACIELIE-KPMGLLSIMEEESMFPKATDQTFLEKLKTNHlGKSPNFI 558
Cdd:pfam00063 395 QQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHFQ 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 559 KPKPpkpnQTEAHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHPGLGGGDDKGGKGG---RK 635
Cdd:pfam00063 473 KPRL----QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKStpkRT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 636 KGSGFQTVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFK 715
Cdd:pfam00063 549 KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFV 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 556079866 716 QRYTILAPNAVPKGFVDAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:pfam00063 629 QRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
93-761 |
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: 968.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITG 172
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 173 ESGAGKTENTKKVIAYFAHVGATSKKEEvkkdTKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGKL 252
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSS----DGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 253 AGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGLKDKLLL**DVHEFHFVSQGKTGIAGVDDGEELVVTDTAFDV 332
Cdd:cd14934 157 AGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 333 LGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGRNIT 412
Cdd:cd14934 237 LGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNME 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 413 QVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVLEQ 492
Cdd:cd14934 317 QCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 493 EEYKREGIEWEFIDFGLDLQACIELIEKPMGLLSIMEEESMFPKATDQTFLEKLKTNHLGKSPNFIKPKPPKPNQTEAHF 572
Cdd:cd14934 397 EEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKGPEAHF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 573 AIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDhpglggGDDKGGKGGRKKGSGFQTVSGLYREQLN 652
Cdd:cd14934 477 ELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKE------EEAPAGSKKQKRGSSFMTVSNFYREQLN 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 653 KLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILAPNAVPKGFVD 732
Cdd:cd14934 551 KLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQGFVD 630
|
650 660
....*....|....*....|....*....
gi 556079866 733 AKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd14934 631 NKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
94-761 |
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: 959.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 94 SVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITGE 173
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 174 SGAGKTENTKKVIAYFAHVGATSKKEEVKKDTKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGKLA 253
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 254 GADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGLKDKLLL**DVHEFHFVSQGKTGIAGVDDGEELVVTDTAFDVL 333
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 334 GFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGRNITQ 413
Cdd:cd14913 242 GFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 414 VTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVLEQE 493
Cdd:cd14913 322 VHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 494 EYKREGIEWEFIDFGLDLQACIELIEKPMGLLSIMEEESMFPKATDQTFLEKLKTNHLGKSPNFIKPKPPKpNQTEAHFA 573
Cdd:cd14913 402 EYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVK-GRAEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 574 IVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHpGLGGGDDKGGKGGRKKGSGFQTVSGLYREQLNK 653
Cdd:cd14913 481 LIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATF-ATADADSGKKKVAKKKGSSFQTVSALFRENLNK 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 654 LMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILAPNAVPKG-FVD 732
Cdd:cd14913 560 LMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGqFID 639
|
650 660
....*....|....*....|....*....
gi 556079866 733 AKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd14913 640 SKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
93-761 |
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: 913.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITG 172
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 173 ESGAGKTENTKKVIAYFAHVGATSKKEEvkkdtKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGKL 252
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKK-----KLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 253 AGADIETYLLEKARVISQQPAERSYHIFYQLMSGKiAGLKDKLLL**DVHEFHFVSQGKTGIAGVDDGEELVVTDTAFDV 332
Cdd:cd14929 156 SSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGK-KELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMDI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 333 LGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGRNIT 412
Cdd:cd14929 235 LGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 413 QVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVLEQ 492
Cdd:cd14929 315 QVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 493 EEYKREGIEWEFIDFGLDLQACIELIEKPMGLLSIMEEESMFPKATDQTFLEKLKTNHLGKSPNFIKPKPPKPNqTEAHF 572
Cdd:cd14929 395 EEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKK-FEAHF 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 573 AIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHpGLGGGDDKGGKGGRKKGSGFQTVSGLYREQLN 652
Cdd:cd14929 474 ELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENY-ISTDSAIQFGEKKRKKGASFQTVASLHKENLN 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 653 KLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILAPNAVPKG-FV 731
Cdd:cd14929 553 KLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSkFV 632
|
650 660 670
....*....|....*....|....*....|
gi 556079866 732 DAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd14929 633 SSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
94-761 |
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: 894.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 94 SVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITGE 173
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 174 SGAGKTENTKKVIAYFAHVGATSKKEEVKKDTKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGKLA 253
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 254 GADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGLKDKLLL**DVHEFHFVSQGKTGIAGVDDGEELVVTDTAFDVL 333
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 334 GFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGRNITQ 413
Cdd:cd14917 242 GFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 414 VTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVLEQE 493
Cdd:cd14917 322 VIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 494 EYKREGIEWEFIDFGLDLQACIELIEKPMGLLSIMEEESMFPKATDQTFLEKLKTNHLGKSPNFIKPKPPKpNQTEAHFA 573
Cdd:cd14917 402 EYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIK-GKPEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 574 IVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHpGLGGGDDKGGKGGRKKGSGFQTVSGLYREQLNK 653
Cdd:cd14917 481 LIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANY-AGADAPIEKGKGKAKKGSSFQTVSALHRENLNK 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 654 LMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILAPNAVPKG-FVD 732
Cdd:cd14917 560 LMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGqFID 639
|
650 660
....*....|....*....|....*....
gi 556079866 733 AKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd14917 640 SRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
94-761 |
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: 882.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 94 SVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITGE 173
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 174 SGAGKTENTKKVIAYFAHVGAT-SKKEEVKKDTKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGKL 252
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTgDKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 253 AGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGLKDKLLL**DVHEFHFVSQGKTGIAGVDDGEELVVTDTAFDV 332
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAIDI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 333 LGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGRNIT 412
Cdd:cd14923 242 LGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNVQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 413 QVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVLEQ 492
Cdd:cd14923 322 QVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 493 EEYKREGIEWEFIDFGLDLQACIELIEKPMGLLSIMEEESMFPKATDQTFLEKLKTNHLGKSPNFIKPKPPKpNQTEAHF 572
Cdd:cd14923 402 EEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAK-GKAEAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 573 AIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHPGLGG-GDDKGGKGGRKKGSGFQTVSGLYREQL 651
Cdd:cd14923 481 SLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAgDSGGSKKGGKKKGSSFQTVSAVFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 652 NKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILAPNAVPKG-F 730
Cdd:cd14923 561 NKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGqF 640
|
650 660 670
....*....|....*....|....*....|.
gi 556079866 731 VDAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd14923 641 IDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
94-761 |
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: 876.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 94 SVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITGE 173
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 174 SGAGKTENTKKVIAYFAHVGATSKKEEVK-KDTKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGKL 252
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAIGDRSKKEnPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 253 AGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGLKDKLLL**DVHEFHFVSQGKTGIAGVDDGEELVVTDTAFDV 332
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFDV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 333 LGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGRNIT 412
Cdd:cd14916 242 LGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 413 QVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVLEQ 492
Cdd:cd14916 322 QVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 493 EEYKREGIEWEFIDFGLDLQACIELIEKPMGLLSIMEEESMFPKATDQTFLEKLKTNHLGKSPNFIKPKPPKPNQtEAHF 572
Cdd:cd14916 402 EEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQ-EAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 573 AIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHPGLGGGDDKGGKGGRKKGSGFQTVSGLYREQLN 652
Cdd:cd14916 481 SLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKGSSFQTVSALHRENLN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 653 KLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILAPNAVPKG-FV 731
Cdd:cd14916 561 KLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGqFI 640
|
650 660 670
....*....|....*....|....*....|
gi 556079866 732 DAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd14916 641 DSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
94-761 |
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: 866.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 94 SVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITGE 173
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 174 SGAGKTENTKKVIAYFAHVGAT--SKKEEVKKDTKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGK 251
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTgeKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 252 LAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGLKDKLLL**DVHEFHFVSQGKTGIAGVDDGEELVVTDTAFD 331
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 332 VLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGRNI 411
Cdd:cd14910 242 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 412 TQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVLE 491
Cdd:cd14910 322 QQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 492 QEEYKREGIEWEFIDFGLDLQACIELIEKPMGLLSIMEEESMFPKATDQTFLEKLKTNHLGKSPNFIKPKPPKpNQTEAH 571
Cdd:cd14910 402 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAK-GKVEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 572 FAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHPGLGGGDDKGGKGGRKKGSGFQTVSGLYREQL 651
Cdd:cd14910 481 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEGGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 652 NKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILAPNAVPKG-F 730
Cdd:cd14910 561 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqF 640
|
650 660 670
....*....|....*....|....*....|.
gi 556079866 731 VDAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd14910 641 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
95-761 |
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: 858.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 95 VLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITGES 174
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 175 GAGKTENTKKVIAYFAHVGATSKKEEVKKDTKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGKLAG 254
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 255 ADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGLKDKLLL**DVHEFHFVSQGKTGIAGVDDGEELVVTDTAFDVLG 334
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 335 FTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGRNITQV 414
Cdd:cd14918 243 FTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 415 TASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVLEQEE 494
Cdd:cd14918 323 YNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 495 YKREGIEWEFIDFGLDLQACIELIEKPMGLLSIMEEESMFPKATDQTFLEKLKTNHLGKSPNFIKPKPPKpNQTEAHFAI 574
Cdd:cd14918 403 YKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVK-GKAEAHFSL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 575 VHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHpGLGGGDDKGGKGGRKKGSGFQTVSGLYREQLNKL 654
Cdd:cd14918 482 IHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY-ASAEADSGAKKGAKKKGSSFQTVSALFRENLNKL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 655 MATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILAPNAVPKG-FVDA 733
Cdd:cd14918 561 MTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGqFIDS 640
|
650 660
....*....|....*....|....*...
gi 556079866 734 KNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd14918 641 KKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
94-761 |
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: 858.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 94 SVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITGE 173
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 174 SGAGKTENTKKVIAYFAHVGAT--SKKEEVKKDTKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGK 251
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTgeKKKEEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 252 LAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGLKDKLLL**DVHEFHFVSQGKTGIAGVDDGEELVVTDTAFD 331
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 332 VLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGRNI 411
Cdd:cd14915 242 ILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 412 TQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVLE 491
Cdd:cd14915 322 QQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 492 QEEYKREGIEWEFIDFGLDLQACIELIEKPMGLLSIMEEESMFPKATDQTFLEKLKTNHLGKSPNFIKPKPPKpNQTEAH 571
Cdd:cd14915 402 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAK-GKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 572 FAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHPGLGGGDDKGGKGGRKKGSGFQTVSGLYREQL 651
Cdd:cd14915 481 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGGGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 652 NKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILAPNAVPKG-F 730
Cdd:cd14915 561 NKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqF 640
|
650 660 670
....*....|....*....|....*....|.
gi 556079866 731 VDAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd14915 641 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
94-761 |
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: 857.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 94 SVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITGE 173
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 174 SGAGKTENTKKVIAYFAHVGAT--SKKEEVKKDTKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGK 251
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTgeKKKEEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 252 LAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGLKDKLLL**DVHEFHFVSQGKTGIAGVDDGEELVVTDTAFD 331
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 332 VLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGRNI 411
Cdd:cd14912 242 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 412 TQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVLE 491
Cdd:cd14912 322 EQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 492 QEEYKREGIEWEFIDFGLDLQACIELIEKPMGLLSIMEEESMFPKATDQTFLEKLKTNHLGKSPNFIKPKPPKpNQTEAH 571
Cdd:cd14912 402 QEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVK-GKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 572 FAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHPGLGGGDD--KGGKGGRKKGSGFQTVSGLYRE 649
Cdd:cd14912 481 FSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAggGAKKGGKKKGSSFQTVSALFRE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 650 QLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILAPNAVPKG 729
Cdd:cd14912 561 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 640
|
650 660 670
....*....|....*....|....*....|...
gi 556079866 730 -FVDAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd14912 641 qFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
32-1110 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 852.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 32 VWVPDEKEGFILGNISST---KGDMV-TVDCPGGERV-FKKDQLQQV--NPPKFEKCEDMSSLTYLNDASVLHNLKERYY 104
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEafnKGKVTeEGKKEDGESVsVKKKVLGNDriKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 105 CHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITGESGAGKTENTKK 184
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 185 VIAYFAHVGATSKKEEVKkdtkkgnLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGKLAGADIETYLLEK 264
Cdd:COG5022 172 IMQYLASVTSSSTVEISS-------IEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 265 ARVISQQPAERSYHIFYQLMSGKIAgLKDKLLL**DVHEFHFVSQGK-TGIAGVDDGEELVVTDTAFDVLGFTDEEKENI 343
Cdd:COG5022 245 SRVVHQNKNERNYHIFYQLLAGDPE-ELKKLLLLQNPKDYIYLSQGGcDKIDGIDDAKEFKITLDALKTIGIDEEEQDQI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 344 YKVTAAVMHFGCLKFKQRpREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGRNITQVTASVGALSK 423
Cdd:COG5022 324 FKILAAILHIGNIEFKED-RNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 424 AIFDRLFKWLVKRVNETLDTKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWE 503
Cdd:COG5022 403 ALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWS 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 504 FIDFgLDLQACIELIEK--PMGLLSIMEEESMFPKATDQTFLEKLKTN-HLGKSPNFikpKPPKPNQTEahFAIVHYAGT 580
Cdd:COG5022 483 FIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKF---KKSRFRDNK--FVVKHYAGD 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 581 VPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDhpglgggddkggKGGRKKGSGFQTVSGLYREQLNKLMATLNS 660
Cdd:COG5022 557 VEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDD------------EENIESKGRFPTLGSRFKESLNSLMSTLNS 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 661 TSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILAPNA----VPKGFVDAKNV 736
Cdd:COG5022 625 TQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtgEYTWKEDTKNA 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 737 SEKVIEAIQLDANDFRFGHSKIFFRAGVLGRLEEMRDERLSKIMTMIQAAVRWYICKKHFQKLKEQRVALLVIQRNLRKF 816
Cdd:COG5022 705 VKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLR 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 817 LQLRNWLWWKLYSKVKPLLSAVRVEDELK---AMEEKLKKTEEALAKEEKLRKELEEHNVKVLQEKndlflqleaermgA 893
Cdd:COG5022 785 RLVDYELKWRLFIKLQPLLSLLGSRKEYRsylACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQK-------------F 851
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 894 GDVEERLNKALTQKGD---LESQ--LADLNDRLSHEEDAHASLSQSK---KKLEGEISGLKKDIEDMELAlqkaeqdkat 965
Cdd:COG5022 852 GRSLKAKKRFSLLKKEtiyLQSAqrVELAERQLQELKIDVKSISSLKlvnLELESEIIELKKSLSSDLIE---------- 921
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 966 kdhqirnlndEIQHQDELINKLnkeKKHLQEASQKTSEDLQATE-DKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIE 1044
Cdd:COG5022 922 ----------NLEFKTELIARL---KKLLNNIDLEEGPSIEYVKlPELNKLHEVESKLKETSEEYEDLLKKSTILVREGN 988
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556079866 1045 KNKRKVEG----------DLKLAQEAVADLEKNKKEME--QNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARI 1110
Cdd:COG5022 989 KANSELKNfkkelaelskQYGALQESTKQLKELPVEVAelQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARY 1066
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
93-761 |
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: 828.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRT-EVPPHVFAVSDGAYMDMLANRENQSMLIT 171
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 172 GESGAGKTENTKKVIAYFAHVGATSKKeevKKDTKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGK 251
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSS---KSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 252 LAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGLKDKLLL**DVHEFHF----VSQGKTGIAGVDDGEELVVTD 327
Cdd:cd00124 158 LVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylNSSGCDRIDGVDDAEEFQELL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 328 TAFDVLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREE--QAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFV 405
Cdd:cd00124 238 DALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 406 TQGRNITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQ--HFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFF 483
Cdd:cd00124 318 TKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEstSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 484 NHHMFVLEQEEYKREGIEWEFIDFgLDLQACIELIE-KPMGLLSIMEEESMFPKATDQTFLEKLKTNHlGKSPNFIKPKP 562
Cdd:cd00124 398 NQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAH-GSHPRFFSKKR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 563 PKPNqteaHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDqfkkgsnLLLQaifedhpglgggddkggkggrkkgsgfqt 642
Cdd:cd00124 476 KAKL----EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVD-------LLRS----------------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 643 vSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILA 722
Cdd:cd00124 516 -GSQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILA 594
|
650 660 670
....*....|....*....|....*....|....*....
gi 556079866 723 PNAVPKGFVDAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd00124 595 PGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
93-761 |
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: 809.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITG 172
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 173 ESGAGKTENTKKVIAYFAHVGATSKK-------EEVKKDTKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIH 245
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASKPKgsgavphPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 246 FGPMGKLAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAgLKDKLLL**DVHEFHFVSQGKTGIAGVDDGEELVV 325
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATP-EQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 326 TDTAFDVLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFV 405
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 406 TQGRNITQVTASVGALSKAIFDRLFKWLVKRVNETLD-TKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFN 484
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 485 HHMFVLEQEEYKREGIEWEFIDFGLDLQACIELIEKPMGLLSIMEEESMFPKATDQTFLEKLKTNHlGKSPNFIKPKppk 564
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH-SMHPKFMKTD--- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 565 pNQTEAHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHP---GLGGGDDKGGKGGRKKGSGFQ 641
Cdd:cd14911 476 -FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEivgMAQQALTDTQFGARTRKGMFR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 642 TVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTIL 721
Cdd:cd14911 555 TVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELL 634
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 556079866 722 APNAVPKGFVDAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd14911 635 TPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
93-761 |
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: 782.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITG 172
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 173 ESGAGKTENTKKVIAYFAHVGATSKKEevKKDTKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGKL 252
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGR--KDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 253 AGADIETYLLEKARVISQQPAERSYHIFYQLMSGKiAGLKDKLLL**DVHEFHFVSQGKTGIAGVDDGEELVVTDTAFDV 332
Cdd:cd14920 159 VGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGA-GEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 333 LGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGRNIT 412
Cdd:cd14920 238 MGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 413 QVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKR-QHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVLE 491
Cdd:cd14920 318 QADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 492 QEEYKREGIEWEFIDFGLDLQACIELIEKPM---GLLSIMEEESMFPKATDQTFLEKLkTNHLGKSPNFIKPKPPKpnqT 568
Cdd:cd14920 398 QEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKL-VQEQGSHSKFQKPRQLK---D 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 569 EAHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFED-------HPGLGGGDDKGGKGGRKKGSGFQ 641
Cdd:cd14920 474 KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrivglDQVTGMTETAFGSAYKTKKGMFR 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 642 TVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTIL 721
Cdd:cd14920 554 TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 556079866 722 APNAVPKGFVDAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd14920 634 TPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
93-761 |
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: 736.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITG 172
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 173 ESGAGKTENTKKVIAYFAHVGAT--SKKEEVKKDTKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMG 250
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSfkTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 251 KLAGADIETYLLEKARVISQQPAERSYHIFYQLMSGkiAGLKDKLLL-**DVHEFHFVSQGKTGIAGVDDGEELVVTDTA 329
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTG--AGDKLRSELcLEDYSKYRFLSNGNVTIPGQQDKELFAETMEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 330 FDVLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGR 409
Cdd:cd14932 239 FRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 410 NITQVTASVGALSKAIFDRLFKWLVKRVNETLD-TKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMF 488
Cdd:cd14932 319 TQEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 489 VLEQEEYKREGIEWEFIDFGLDLQACIELIEKPMG---LLSIMEEESMFPKATDQTFLEKLkTNHLGKSPNFIKPKPPKp 565
Cdd:cd14932 399 ILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGppgILALLDEECWFPKATDKSFVEKV-VQEQGNNPKFQKPKKLK- 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 566 nqTEAHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHP------GLGGGDDKGGKGGRKKGSG 639
Cdd:cd14932 477 --DDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDrivgldKVAGMGESLHGAFKTRKGM 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 640 FQTVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYT 719
Cdd:cd14932 555 FRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 634
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 556079866 720 ILAPNAVPKGFVDAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd14932 635 ILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
93-761 |
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: 700.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITG 172
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 173 ESGAGKTENTKKVIAYFAHVGATSKKeevKKDTK-KGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGK 251
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKG---KKDTSiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 252 LAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKiAGLKDKLLL**DVHEFHFVSQGKTGIAGVDDGEELVVTDTAFD 331
Cdd:cd14921 158 IVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGA-KEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 332 VLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGRNI 411
Cdd:cd14921 237 IMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 412 TQVTASVGALSKAIFDRLFKWLVKRVNETLD-TKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVL 490
Cdd:cd14921 317 EQADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFIL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 491 EQEEYKREGIEWEFIDFGLDLQACIELIEKPM---GLLSIMEEESMFPKATDQTFLEKLKTNHlGKSPNFIKPKPPKpNQ 567
Cdd:cd14921 397 EQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKPKQLK-DK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 568 TEahFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFED-------HPGLGGGDDKGGKGGRKKGSGF 640
Cdd:cd14921 475 TE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDvdrivglDQMAKMTESSLPSASKTKKGMF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 641 QTVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTI 720
Cdd:cd14921 553 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 556079866 721 LAPNAVPKGFVDAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd14921 633 LAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
93-761 |
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: 693.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITG 172
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 173 ESGAGKTENTKKVIAYFAHVGAT--SKKEEVKKDTKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMG 250
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASShkTKKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 251 KLAGADIETYLLEKARVISQQPAERSYHIFYQLMSGkIAGLKDKLLL**DVHEFHFVSQGKTGIAGVDDGEELVVTDTAF 330
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTG-AGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 331 DVLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGRN 410
Cdd:cd15896 240 RIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 411 ITQVTASVGALSKAIFDRLFKWLVKRVNETLD-TKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFV 489
Cdd:cd15896 320 QEQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 490 LEQEEYKREGIEWEFIDFGLDLQACIELIEKPM---GLLSIMEEESMFPKATDQTFLEKLKTNHlGKSPNFIKPKPPKpn 566
Cdd:cd15896 400 LEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQ-GTHPKFFKPKKLK-- 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 567 qTEAHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHPG-----LGGGDDKGGKGGRKKGSGFQ 641
Cdd:cd15896 477 -DEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRivgldKVSGMSEMPGAFKTRKGMFR 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 642 TVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTIL 721
Cdd:cd15896 556 TVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 635
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 556079866 722 APNAVPKGFVDAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd15896 636 TPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
93-761 |
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: 689.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITG 172
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 173 ESGAGKTENTKKVIAYFAHVGATSKKeevKKDtkKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGKL 252
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKS---KKD--QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 253 AGADIETYLLEKARVISQQPAERSYHIFYQLMSGkiAGLKDKLLL**D-VHEFHFVSQGKTGIAGVDDGEELVVTDTAFD 331
Cdd:cd14919 156 VGANIETYLLEKSRAIRQAKEERTFHIFYYLLSG--AGEHLKTDLLLEpYNKYRFLSNGHVTIPGQQDKDMFQETMEAMR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 332 VLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGRNI 411
Cdd:cd14919 234 IMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 412 TQVTASVGALSKAIFDRLFKWLVKRVNETLD-TKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVL 490
Cdd:cd14919 314 EQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 491 EQEEYKREGIEWEFIDFGLDLQACIELIEKPMG---LLSIMEEESMFPKATDQTFLEKLKTNHlGKSPNFIKPKPPKpnq 567
Cdd:cd14919 394 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGppgILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLK--- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 568 TEAHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFED-------HPGLGGGDDKGGKGGRKKGSGF 640
Cdd:cd14919 470 DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriiglDQVAGMSETALPGAFKTRKGMF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 641 QTVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTI 720
Cdd:cd14919 550 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 556079866 721 LAPNAVPKGFVDAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd14919 630 LTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
94-761 |
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: 682.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 94 SVLHNLKERYyC--HLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLIT 171
Cdd:cd01380 2 AVLHNLKVRF-CqrNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 172 GESGAGKTENTKKVIAYFAHVGATSKKEEvkkdtkkgNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGK 251
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFATVGGSSSGET--------QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 252 LAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGlKDKLLL**DVHEFHFVSQGKTG-IAGVDDGEELVVTDTAF 330
Cdd:cd01380 153 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLP-ELKELHLGSAEDFFYTNQGGSPvIDGVDDAAEFEETRKAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 331 DVLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGRN 410
Cdd:cd01380 232 TLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 411 ITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQ--KRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMF 488
Cdd:cd01380 312 LQQAIVARDALAKHIYAQLFDWIVDRINKALASPVkeKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 489 VLEQEEYKREGIEWEFIDFgLDLQACIELIEKPMGLLSIMEEESMFPKATDQTFLEKLKTNHLGKSPNFIkpKPPKPNQT 568
Cdd:cd01380 392 KLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNKHF--KKPRFSNT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 569 EahFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNlllqaifedhpglgggddkggkggrkkgsGFQTVSGLYR 648
Cdd:cd01380 469 A--FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKN-----------------------------RKKTVGSQFR 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 649 EQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILAPNAVPK 728
Cdd:cd01380 518 DSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWL 597
|
650 660 670
....*....|....*....|....*....|...
gi 556079866 729 GfVDAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd01380 598 R-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
93-761 |
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: 675.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITG 172
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 173 ESGAGKTENTKKVIAYFAHVGATSKKEevKKDTKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGKL 252
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGR--KEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 253 AGADIETYLLEKARVISQQPAERSYHIFYQLMSGkiAGLKDKLLL**D-VHEFHFVSQGKTGIAGvDDGEELVVTDTAFD 331
Cdd:cd14930 159 VGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG--AGEQLKADLLLEpCSHYRFLTNGPSSSPG-QERELFQETLESLR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 332 VLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGRNI 411
Cdd:cd14930 236 VLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 412 TQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKR-QHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVL 490
Cdd:cd14930 316 EQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 491 EQEEYKREGIEWEFIDFGLDLQACIELIEKPM---GLLSIMEEESMFPKATDQTFLEKLKTNHlGKSPNFIKPKPPKpnq 567
Cdd:cd14930 396 EQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRHLR--- 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 568 TEAHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHPGLGGGDDKGGKGG-----RKKGSGFQT 642
Cdd:cd14930 472 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDgppggRPRRGMFRT 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 643 VSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILA 722
Cdd:cd14930 552 VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 631
|
650 660 670
....*....|....*....|....*....|....*....
gi 556079866 723 PNAVPKGFVDAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd14930 632 PNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
93-761 |
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: 639.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITG 172
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 173 ESGAGKTENTKKVIAYFAHVGAtskkeevkkdtKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGKL 252
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISG-----------QHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 253 AGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAgLKDKLLL**DVHEFHFVSQGKTGIA-GVDDGEELVVTDTAFD 331
Cdd:cd01381 150 EGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSA-EEKKKLELGDASDYYYLTQGNCLTCeGRDDAAEFADIRSAMK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 332 VLGFTDEEKENIYKVTAAVMHFGCLKFKQRPRE--EQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGR 409
Cdd:cd01381 229 VLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 410 NITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQHF---IGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHH 486
Cdd:cd01381 309 SAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRH 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 487 MFVLEQEEYKREGIEWEFIDFgLDLQACIELI-EKPMGLLSIMEEESMFPKATDQTFLEKLKTNHlGKSPNFIKPKppkp 565
Cdd:cd01381 389 IFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKPK---- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 566 NQTEAHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIF-EDHPGLGGGDDKGgkggrkkgsgfQTVS 644
Cdd:cd01381 463 SDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFnEDISMGSETRKKS-----------PTLS 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 645 GLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILAPN 724
Cdd:cd01381 532 SQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPG 611
|
650 660 670
....*....|....*....|....*....|....*..
gi 556079866 725 AVPKGFVDAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd01381 612 IPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
94-761 |
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: 632.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 94 SVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYkgRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITGE 173
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAY--RQKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 174 SGAGKTENTKKVIAYFAHVGATSkkeevkkdtkkGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGKLA 253
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGS-----------SGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKIC 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 254 GADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGlKDKLLL**DVHEFHFVSQGKT-GIAGVDDGEELVVTDTAFDV 332
Cdd:cd01383 149 GAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPA-LREKLNLKSASEYKYLNQSNClTIDGVDDAKKFHELKEALDT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 333 LGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGRNIT 412
Cdd:cd01383 228 VGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 413 QVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQ-HFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVLE 491
Cdd:cd01383 308 QAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTgRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 492 QEEYKREGIEWEFIDFgLDLQACIELIE-KPMGLLSIMEEESMFPKATDQTFLEKLKTnHLGKSPNFIKPKppkpnqtEA 570
Cdd:cd01383 388 QEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKLKQ-HLKSNSCFKGER-------GG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 571 HFAIVHYAGTVPYNLTGWLEKNKDPLN-DCVvdQFKKGSNLLLQAIFEDHPGLGGGDDKGGKGGRKKGSGFQTVSGLYRE 649
Cdd:cd01383 459 AFTIRHYAGEVTYDTSGFLEKNRDLLHsDLI--QLLSSCSCQLPQLFASKMLDASRKALPLTKASGSDSQKQSVATKFKG 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 650 QLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILAPNAVpKG 729
Cdd:cd01383 537 QLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDV-SA 615
|
650 660 670
....*....|....*....|....*....|..
gi 556079866 730 FVDAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd01383 616 SQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
94-761 |
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: 620.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 94 SVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITGE 173
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 174 SGAGKTENTKKVIAYFAHVgaTSKKEEVkkdtkkgnlEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGKLA 253
Cdd:cd14883 82 SGAGKTETTKLILQYLCAV--TNNHSWV---------EQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 254 GADIETYLLEKARVISQQPAERSYHIFYQLMSG-KIAGLKDKLLL**DVHEFHFVSQ-GKTGIAGVDDGEELVVTDTAFD 331
Cdd:cd14883 151 GAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGaKHSKELKEKLKLGEPEDYHYLNQsGCIRIDNINDKKDFDHLRLAMN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 332 VLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAE-ADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGRN 410
Cdd:cd14883 231 VLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 411 ITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVL 490
Cdd:cd14883 311 VQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 491 EQEEYKREGIEWEFIDFGlDLQACIELIEK-PMGLLSIMEEESMFPKATDQTFLEKLKTNHlGKSPNFIKPKPPKPNQTe 569
Cdd:cd14883 391 EQEEYEKEGINWSHIVFT-DNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPDRRRWKTE- 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 570 ahFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIF----EDHPGLGGGDDKGGKGGRKKGSGFQTVSG 645
Cdd:cd14883 468 --FGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFtypdLLALTGLSISLGGDTTSRGTSKGKPTVGD 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 646 LYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILAPNA 725
Cdd:cd14883 546 TFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRA 625
|
650 660 670
....*....|....*....|....*....|....*.
gi 556079866 726 VPKGFVDAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd14883 626 RSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
94-761 |
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: 617.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 94 SVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITGE 173
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 174 SGAGKTENTKKVIAYFAHV--GATSKKEEVKkdtkkgnleDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGK 251
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVsgGSESEVERVK---------DMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 252 LAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGLKDKLLL**DVHEFHFVSQGKTGIAGVDDGEELVVTDTAFD 331
Cdd:cd01378 153 PVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 332 VLGFTDEEKENIYKVTAAVMHFGCLKFKQrprEEQAEADGTEEGER--VAHLLGLNAADLYKNLLKPRIKVGTEFVTQ-- 407
Cdd:cd01378 233 VIGFTEEEQDSIFRILAAILHLGNIQFAE---DEEGNAAISDTSVLdfVAYLLGVDPDQLEKALTHRTIETGGGGRSVye 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 408 -GRNITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQ-HFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNH 485
Cdd:cd01378 310 vPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 486 hmFVL--EQEEYKREGIEWEFIDFgLDLQACIELIE-KPMGLLSIMEEESMFP-KATDQTFLEKLktNHLGKSPNFIKPK 561
Cdd:cd01378 390 --LTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL--NQLFSNHPHFECP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 562 PPKPNQTEAHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHPGLGGGDDKGgkggrkkgsgfq 641
Cdd:cd01378 465 SGHFELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDSKKRPP------------ 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 642 TVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTIL 721
Cdd:cd01378 533 TAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLL 612
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 556079866 722 APNAVPKGFVDAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd01378 613 SPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
93-761 |
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: 596.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFP-IYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLIT 171
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 172 GESGAGKTENTKKVIAYFAHVGAtskkeevKKDTKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGK 251
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGG-------RAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 252 LAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKiAGLKDKLLL**DVHEFHFVSQGKT-GIAGVDDGEELVVTDTAF 330
Cdd:cd01384 154 ISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGA-PPEDREKYKLKDPKQFHYLNQSKCfELDGVDDAEEYRATRRAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 331 DVLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAE-ADGTEEG--ERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQ 407
Cdd:cd01384 233 DVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVpKDEKSEFhlKAAAELLMCDEKALEDALCKRVIVTPDGIITK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 408 GRNITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHM 487
Cdd:cd01384 313 PLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 488 FVLEQEEYKREGIEWEFIDFgLDLQACIELIE-KPMGLLSIMEEESMFPKATDQTFLEKLKTNhLGKSPNFIKPKPPKPN 566
Cdd:cd01384 393 FKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSKPKLSRTD 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 567 qteahFAIVHYAGTVPYNLTGWLEKNKdplnDCVV----DQFKKGSNLLLQAIFEdhpglgggddKGGKGGRKKGSGFQT 642
Cdd:cd01384 471 -----FTIDHYAGDVTYQTDLFLDKNK----DYVVaehqALLNASKCPFVAGLFP----------PLPREGTSSSSKFSS 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 643 VSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILA 722
Cdd:cd01384 532 IGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLA 611
|
650 660 670
....*....|....*....|....*....|....*....
gi 556079866 723 PNaVPKGFVDAKNVSEKVIEAIQLdaNDFRFGHSKIFFR 761
Cdd:cd01384 612 PE-VLKGSDDEKAACKKILEKAGL--KGYQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
93-761 |
4.61e-171 |
|
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: 539.53 E-value: 4.61e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFP-IYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLIT 171
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 172 GESGAGKTENTKKVIAYFAHVGATSKkeevkkdtkkGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGK 251
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSGA----------GPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 252 LAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGlkdklll**dvhefhfVSQGKTGIAGVDDGEELVVTDTAFD 331
Cdd:cd01382 151 VVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPED----------------LREKLLKDPLLDDVGDFIRMDKAMK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 332 VLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGER----VAHLLGLNAADLYKNLLKpRIKVGTEFVTQ 407
Cdd:cd01382 215 KIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGGCNVKPKSEQsleyAAELLGLDQDELRVSLTT-RVMQTTRGGAK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 408 GRNIT------QVTASVGALSKAIFDRLFKWLVKRVNETLDTkQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQ 481
Cdd:cd01382 294 GTVIKvplkveEANNARDALAKAIYSKLFDHIVNRINQCIPF-ETSSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 482 FFNHHMFVLEQEEYKREGIEWEFIDFgLDLQACIELIE-KPMGLLSIMEEESMFPKATDQTFLEKLKTNHlgksPNFIKP 560
Cdd:cd01382 373 FFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKH----KNHFRL 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 561 KPPKPNQTEAH--------FAIVHYAGTVPYNLTGWLEKNKDPLND---CVVDQfkkGSNLLLQAIFEDHPglgggDDKG 629
Cdd:cd01382 448 SIPRKSKLKIHrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHAsleSLICE---SKDKFIRSLFESST-----NNNK 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 630 GKGGRKKGSGFQTVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRM 709
Cdd:cd01382 520 DSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRT 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 556079866 710 IYPDFKQRYTILAPNAVPKgfVDAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd01382 600 SFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
93-761 |
5.22e-170 |
|
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: 536.67 E-value: 5.22e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITG 172
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 173 ESGAGKTENTKKVIAYFAHVGATSkkeevkkdtkkGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGKL 252
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGST-----------NGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 253 AGADIETYLLEKARVISQQPAERSYHIFYQLMSGkiaGLKDKLLL**DVHEFHFVSQGKT-GIAGVDDGEELVVTDTAFD 331
Cdd:cd14872 150 CGASTENYLLEKSRVVYQIKGERNFHIFYQLLAS---PDPASRGGWGSSAAYGYLSLSGCiEVEGVDDVADFEEVVLAME 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 332 VLGFTDEEKENIYKVTAAVMHFGCLKF------KQRPREEQAEADGTEEgerVAHLLGLNAADLYKNLLKPRIKVgtefv 405
Cdd:cd14872 227 QLGFDDADINNVMSLIAAILKLGNIEFasgggkSLVSGSTVANRDVLKE---VATLLGVDAATLEEALTSRLMEI----- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 406 tQGRNIT-------QVTASVGALSKAIFDRLFKWLVKRVNETLD-TKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNE 477
Cdd:cd14872 299 -KGCDPTripltpaQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 478 KLQQFFNHHMFVLEQEEYKREGIEWEFIDFgLDLQACIELIEK-PMGLLSIMEEESMFPKATDQTFLEKLKTNHLGKSpN 556
Cdd:cd14872 378 KLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS-T 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 557 FIkpkPPKPNQTEAHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEdhPGLGGGDDKGGkggrkk 636
Cdd:cd14872 456 FV---YAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFP--PSEGDQKTSKV------ 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 637 gsgfqTVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQ 716
Cdd:cd14872 525 -----TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLK 599
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 556079866 717 RYTILaPNAVPKGF-VDAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd14872 600 RYRFL-VKTIAKRVgPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
93-761 |
6.71e-169 |
|
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: 534.35 E-value: 6.71e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFP-IYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDML----ANRENQS 167
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIqsgvLDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 168 MLITGESGAGKTENTKKVIAYFAHVGATSKKEEVKKDTKK--------GNLEDQVVQTNPVLESFGNAKTVRNDNSSRFG 239
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEAAseaieqtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 240 KFIRIHFGPMGKLAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGLKDKLLL**DVHEFHFVSQgKTGIAGVDD 319
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGE-CSSIPSCDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 320 GEELVVTDTAFDVLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGER-VAHLLGLNAADLYKNLLKPRI 398
Cdd:cd14890 240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTLQSLKlAAELLGVNEDALEKALLTRQL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 399 KVGTEFVTQGRNITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEK 478
Cdd:cd14890 320 FVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 479 LQQFFNHHMFVLEQEEYKREGIEWEFIDFGlDLQACIELIE-----KPmGLLSIMEE-ESMFPKATDQTFLEKLKTNHLG 552
Cdd:cd14890 400 LQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgkvngKP-GIFITLDDcWRFKGEEANKKFVSQLHASFGR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 553 KS------------PNFIKPKPPKpnqtEAHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAifedhp 620
Cdd:cd14890 478 KSgsggtrrgssqhPHFVHPKFDA----DKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSIREV------ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 621 glgggddkggkggrkkgsgfqTVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRI 700
Cdd:cd14890 548 ---------------------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQI 606
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556079866 701 CRKGFPNRMIYPDFKQRYTILAPnavpkgfvDAKNVSEKVIEA---IQLDANDFRFGHSKIFFR 761
Cdd:cd14890 607 RQQGFALREEHDSFFYDFQVLLP--------TAENIEQLVAVLskmLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
93-761 |
3.89e-167 |
|
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: 529.35 E-value: 3.89e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFP-IYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLIT 171
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 172 GESGAGKTENTKKVIAYFAhvgatskkeevkkdTKKGNLED----QVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFG 247
Cdd:cd14903 81 GESGAGKTETTKILMNHLA--------------TIAGGLNDstikKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 248 PMGKLAGADIETYLLEKARVISQQPAERSYHIFYQLM-SGKIAGLKDKLLL**DVHEFhfvSQGKTGIAGVDDGEELVVT 326
Cdd:cd14903 147 KNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLaSPDVEERLFLDSANECAYTG---ANKTIKIEGMSDRKHFART 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 327 DTAFDVLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAE--ADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEF 404
Cdd:cd14903 224 KEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 405 VTQGRNITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFN 484
Cdd:cd14903 304 YTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFT 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 485 HHMFVLEQEEYKREGIEWEFIDFgLDLQACIELIEKPMGLLSIMEEESMFPKATDQTFLEKLKTNHLgKSPNFIkpKPPK 564
Cdd:cd14903 384 QDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHK-DEQDVI--EFPR 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 565 PNQTEahFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIF----EDHPGLGGGDDKGGKGGRKKGSGF 640
Cdd:cd14903 460 TSRTQ--FTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFkekvESPAAASTSLARGARRRRGGALTT 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 641 QTVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTI 720
Cdd:cd14903 538 TTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWL 617
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 556079866 721 LAPNAvPKGFVDAKNVSEKVIEAIQLDA-NDFRFGHSKIFFR 761
Cdd:cd14903 618 FLPEG-RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
93-723 |
8.34e-164 |
|
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: 520.40 E-value: 8.34e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFP-IYTKRVVE--IYKGRRRtevPPHVFAVSDGAYMDMLANRENQSML 169
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLkfIQPSISK---SPHVFSTASSAYQGMCNNKKSQTIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 170 ITGESGAGKTENTKKVIAYFAHVGATSKKeevkkdtKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHF--- 246
Cdd:cd14888 78 ISGESGAGKTESTKYVMKFLACAGSEDIK-------KRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFskl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 247 ------GPMGKLAGADIETYLLEKARVISQQPAERSYHIFYQLMS------------------GKIAGLKDKLLL**DVH 302
Cdd:cd14888 151 kskrmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaareakntglsyeendekLAKGADAKPISIDMSSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 303 EFHFVSQGKT-----GIAGVDDGEELVVTDTAFDVLGFTDEEKENIYKVTAAVMHFGCLKFK-QRPREEQA--EADGTEE 374
Cdd:cd14888 231 EPHLKFRYLTksschELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFEnNEACSEGAvvSASCTDD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 375 GERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGRNITQVTASVGALSKAIFDRLFKWLVKRVNETLD-TKQKRQHFIGV 453
Cdd:cd14888 311 LEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCGV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 454 LDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWEFIDFGlDLQACIELI-EKPMGLLSIMEEES 532
Cdd:cd14888 391 LDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEEC 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 533 MFPKATDQTFLEKLKTNHLG-KSPNFIKPKPpkpnqteAHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLL 611
Cdd:cd14888 470 FVPGGKDQGLCNKLCQKHKGhKRFDVVKTDP-------NSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPF 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 612 LQAIFEdhpglggGDDKGGKGGRKKGSGFQTVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTC 691
Cdd:cd14888 543 ISNLFS-------AYLRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKY 615
|
650 660 670
....*....|....*....|....*....|..
gi 556079866 692 NGVLEGIRICRKGFPNRMIYPDFKQRYTILAP 723
Cdd:cd14888 616 GGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
93-761 |
1.02e-161 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 514.31 E-value: 1.02e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFP-IYTkrVVEIYKGRR----RTEVPPHVFAVSDGAYMDMLANR---- 163
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPlLYD--VPGFDSQRKeeatASSPPPHVFSIAERAYRAMKGVGkgqg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 164 ENQSMLITGESGAGKTENTKKVIAYFAHVGATSKKEEVKKDTKKG--NLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKF 241
Cdd:cd14892 79 TPQSIVVSGESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAheSIEECVLLSNLILEAFGNAKTIRNDNSSRFGKY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 242 IRIHFGPMGKLAGADIETYLLEKARVISQQPAERSYHIFYQLMSGkIAGLKDKLLL**DVHEFHFVSQGKTG-IAGVDDG 320
Cdd:cd14892 159 IQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAG-LDANENAALELTPAESFLFLNQGNCVeVDGVDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 321 EELVVTDTAFDVLGFTDEEKENIYKVTAAVMHFGCLKFKQR--PREEQAEADGTEEGERVAHLLGLNAADLYKNLLKpRI 398
Cdd:cd14892 238 TEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENadDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLVT-QT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 399 KVGTEFVTQGRNITQVTASVG--ALSKAIFDRLFKWLVKRVN----------ETLDTKQKRQHFIGVLDIAGFEIFDHNS 466
Cdd:cd14892 317 TSTARGSVLEIKLTAREAKNAldALCKYLYGELFDWLISRINachkqqtsgvTGGAASPTFSPFIGILDIFGFEIMPTNS 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 467 FEQMCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWEFIDFGlDLQACIELIEK-PMGLLSIMEEESMFP-KATDQTFLE 544
Cdd:cd14892 397 FEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLLT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 545 KLKTNHLGKSPNFIKPKppkpNQTEaHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNlllqaifedhpglgg 624
Cdd:cd14892 476 IYHQTHLDKHPHYAKPR----FECD-EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK--------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 625 gddkggkggrkkgsgfqtvsglYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKG 704
Cdd:cd14892 536 ----------------------FRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREG 593
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556079866 705 FPNRMIYPDFKQRYTILAPNAV--------PKGFVDAKNVSEKVIEAiqLDANDFRFGHSKIFFR 761
Cdd:cd14892 594 FPIRRQFEEFYEKFWPLARNKAgvaaspdaCDATTARKKCEEIVARA--LERENFQLGRTKVFLR 656
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
93-761 |
1.03e-160 |
|
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: 511.22 E-value: 1.03e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITG 172
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 173 ESGAGKTENTKKVIAYFAHVgatskkeevkkdTKKGN--LEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFgPMG 250
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAV------------NQRRNnlVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 251 KLAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGLKDKLLL**DVHEFHFVSQGKTGIAGVDDGEELVVTDTAF 330
Cdd:cd01387 148 VIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 331 DVLGFTDEEKENIYKVTAAVMHFGCLKFKQRPRE---EQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQ 407
Cdd:cd01387 228 QVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRhgqEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 408 GRNITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHM 487
Cdd:cd01387 308 PLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 488 FVLEQEEYKREGIEWEFIDFgLDLQACIELI-EKPMGLLSIMEEESMFPKATDQTFLEKLKTNHlGKSPNFIKPKPPKPn 566
Cdd:cd01387 388 FKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPRMPLP- 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 567 qteaHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHPGLGGGDDKGGKGGRKKGSGFQ--TVS 644
Cdd:cd01387 465 ----EFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDKAPPRLGKGRFVTMKPRtpTVA 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 645 GLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILAPN 724
Cdd:cd01387 541 ARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVAL 620
|
650 660 670
....*....|....*....|....*....|....*..
gi 556079866 725 AVPKGFVDAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd01387 621 KLPRPAPGDMCVSLLSRLCTVTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
94-761 |
1.22e-160 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 510.28 E-value: 1.22e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 94 SVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITGE 173
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 174 SGAGKTENTKKVIAYFAHVGatskkeevKKDTKkgNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGKLA 253
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLG--------KANNR--TLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 254 GADIETYLLEKARVISQQPAERSYHIFYQLMSG----KIAGL--KDKLLL**DVHEFHFVSQGKTGIAGVDDGEELVvtD 327
Cdd:cd01379 152 GARISEYLLEKSRVVHQAIGERNFHIFYYIYAGlaedKKLAKykLPENKPPRYLQNDGLTVQDIVNNSGNREKFEEI--E 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 328 TAFDVLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQ----AEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTE 403
Cdd:cd01379 230 QCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 404 FVTQGRNITQVTASVGALSKAIFDRLFKWLVKRVNETL--DTKQK-RQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQ 480
Cdd:cd01379 310 TIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASdEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 481 QFFNHHMFVLEQEEYKREGIEWEFIDFG-----LDLqacieLIEKPMGLLSIMEEESMFPKATDQTFLEKLKTNHlgKSP 555
Cdd:cd01379 390 YYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI--KSK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 556 NFIKPKppkpnQTEAHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQaifedhpglgggddkggkggrk 635
Cdd:cd01379 463 YYWRPK-----SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR---------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 636 kgsgfQTVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFK 715
Cdd:cd01379 516 -----QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFL 590
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 556079866 716 QRYTILAPNAVPKGFVDAKNVsEKVIEAIQLDanDFRFGHSKIFFR 761
Cdd:cd01379 591 KRYYFLAFKWNEEVVANRENC-RLILERLKLD--NWALGKTKVFLK 633
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
93-761 |
3.20e-160 |
|
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: 511.15 E-value: 3.20e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITG 172
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 173 ESGAGKTENTKKVIayfAHVGATSKKeevkkdTKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGKL 252
Cdd:cd01385 81 ESGSGKTESTNFLL---HHLTALSQK------GYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 253 AGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAgLKDKLLL**DVHEFHFVSQGKT-GIAGVDDGEELVVTDTAFD 331
Cdd:cd01385 152 RGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASE-EERKELHLKQPEDYHYLNQSDCyTLEGEDEKYEFERLKQAME 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 332 VLGFTDEEKENIYKVTAAVMHFGCLKFKQRP--REEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGR 409
Cdd:cd01385 231 MVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyhRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 410 NITQVTASVGALSKAIFDRLFKWLVKRVNETL----DTKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNH 485
Cdd:cd01385 311 KLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 486 HMFVLEQEEYKREGIEWEFIDFgLDLQACIELIE-KPMGLLSIMEEESMFPKATDQTFLEKLKTNHlgKSPNFIKpKPPK 564
Cdd:cd01385 391 HIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAKFKQQH--KDNKYYE-KPQV 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 565 pnqTEAHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHP------------------------ 620
Cdd:cd01385 467 ---MEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDPvavfrwavlrafframaafreagr 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 621 ----------GLGGGDDKGGKGGRKKGSGFQTVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLT 690
Cdd:cd01385 544 rraqrtaghsLTLHDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLR 623
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556079866 691 CNGVLEGIRICRKGFPNRMIYPDFKQRYTILapnaVPKGFVDAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd01385 624 YTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
93-759 |
6.00e-160 |
|
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: 509.33 E-value: 6.00e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIY------KGRRRTEVPPHVFAVSDGAYMDMLANRE-- 164
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 165 --NQSMLITGESGAGKTENTKKVIAYFAHVgaTSKKEEVKKDTKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFI 242
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASV--SSATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 243 RIHFGPMGKLAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKiAGLKDKLLL**DVHEFHFV--SQGKTGIAGVDDG 320
Cdd:cd14901 159 RLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGA-SSDELHALGLTHVEEYKYLnsSQCYDRRDGVDDS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 321 EELVVTDTAFDVLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGERVA-HLLGLNAADLYKNLLKPRIK 399
Cdd:cd14901 238 VQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLANVRAAcDLLGLDMDVLEKTLCTREIR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 400 VGTEFVTQGRNITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQK--RQHFIGVLDIAGFEIFDHNSFEQMCINFTNE 477
Cdd:cd14901 318 AGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINFANE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 478 KLQQFFNHHMFVLEQEEYKREGIEWEFIDFGlDLQACIELIE-KPMGLLSIMEEESMFPKATDQTFLEKLkTNHLGKSPN 556
Cdd:cd14901 398 KLQQLFGKFVFEMEQDEYVAEAIPWTFVEYP-NNDACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKY-YDLLAKHAS 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 557 FikpKPPKPNQTEAHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAifedhpglgggddkggkggrkk 636
Cdd:cd14901 476 F---SVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS---------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 637 gsgfqTVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQ 716
Cdd:cd14901 531 -----TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVH 605
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 556079866 717 RYTILAPN-----AVPKGFVDAKNVSEKVIEAIQLDANDFRFGHSKIF 759
Cdd:cd14901 606 TYSCLAPDgasdtWKVNELAERLMSQLQHSELNIEHLPPFQVGKTKVF 653
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
93-761 |
4.71e-156 |
|
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: 498.17 E-value: 4.71e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFP-IYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLIT 171
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 172 GESGAGKTENTKKVIAYFAHVGATSKkeEVKKDTKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGK 251
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSL--ELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 252 LAGADIETYLLEKARVISQQPAERSYHIFYQLMSGkiAGLKDKLLL**DVHE-FHFVSQ-GKTGIAGVDDGEELVVTDTA 329
Cdd:cd14873 159 IQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAG--LEHEEREEFYLSTPEnYHYLNQsGCVEDKTISDQESFREVITA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 330 FDVLGFTDEEKENIYKVTAAVMHFGCLKFKQrprEEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGR 409
Cdd:cd14873 237 MEVMQFSKEEVREVSRLLAGILHLGNIEFIT---AGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 410 NITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRqHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFV 489
Cdd:cd14873 314 NVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDF-KSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 490 LEQEEYKREGIEWEFIDFgLDLQACIELIEKPMGLLSIMEEESMFPKATDQTFLEKLKTNHlGKSPNFIKPKppkpnQTE 569
Cdd:cd14873 393 LEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH-ANNHFYVKPR-----VAV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 570 AHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEdhpgLGGGDDKGGKGGRKKGSGFQTVSGLYRE 649
Cdd:cd14873 466 NNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFE----HVSSRNNQDTLKCGSKHRRPTVSSQFKD 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 650 QLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILAPNAVPKg 729
Cdd:cd14873 542 SLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALP- 620
|
650 660 670
....*....|....*....|....*....|..
gi 556079866 730 fVDAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd14873 621 -EDVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
93-761 |
3.18e-151 |
|
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: 483.81 E-value: 3.18e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRR-RTEVPPHVFAVSDGAYMDMLANRENQSMLIT 171
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 172 GESGAGKTENTKKVIAYFAHVgatSKKEEvkkdtkkGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGK 251
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKL---SPSDD-------SDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 252 LAGADIETYLLEKARVISQQPAERSYHIFYQLMSGkiAGLKDKLLL**DVHEFHFVSQGKTGIAGV-DDGEELVVTDTAF 330
Cdd:cd14897 151 LLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAG--MSRDRLLYYFLEDPDCHRILRDDNRNRPVfNDSEELEYYRQMF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 331 DVL-------GFTDEEKENIYKVTAAVMHFGCLKFkqrprEEQAEADG-----TEEGERVAHLLGLNAADLYKNLLKPRI 398
Cdd:cd14897 229 HDLtnimkliGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGvtvadEYPLHAVAKLLGIDEVELTEALISNVN 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 399 KVGTEFVTQGRNITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQHF-----IGVLDIAGFEIFDHNSFEQMCIN 473
Cdd:cd14897 304 TIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQLCIN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 474 FTNEKLQQFFNHHMFVLEQEEYKREGIEWEFIDFGlDLQACIELI-EKPMGLLSIMEEESMFPKATDQTFLEKLkTNHLG 552
Cdd:cd14897 384 LSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKL-NKYCG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 553 KSPNFIkpkPPKPNQTEahFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHpglgggddkggkg 632
Cdd:cd14897 462 ESPRYV---ASPGNRVA--FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSY------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 633 grkkgsgfqtvsglYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYP 712
Cdd:cd14897 524 --------------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYE 589
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 556079866 713 DFKQRYTILAPNAvPKGFVDAKNVSEKVIEAiqLDANDFRFGHSKIFFR 761
Cdd:cd14897 590 DFVKRYKEICDFS-NKVRSDDLGKCQKILKT--AGIKGYQFGKTKVFLK 635
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
94-722 |
2.51e-145 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 467.09 E-value: 2.51e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 94 SVLHNLKERYYCHLIYTYSGLFCVAINPYKRFP-IYTKRVVEIY-----------KGRRRTEVPPHVFAVSDGAYMDM-- 159
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 160 --LANRENQSMLITGESGAGKTENTKKVIAYFAHVGATSKKEEVKKDTKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSR 237
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 238 FGKFIRIHFGPMGKLAGADIETYLLEKARVISQQPAERSYHIFYQLMSGkiaglkdkllL**DVHEFHFVSQgktgiagv 317
Cdd:cd14900 162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIG----------ASEAARKRDMYRR-------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 318 ddgeelvVTDtAFDVLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEG-------ERVAHLLGLNAADLY 390
Cdd:cd14900 224 -------VMD-AMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLLSVDATKLE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 391 KNLLKPRIKVGTEFVTQGRNITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQ-----HFIGVLDIAGFEIFDHN 465
Cdd:cd14900 296 KALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMDDSSKshgglHFIGILDIFGFEVFPKN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 466 SFEQMCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWEFIDFGlDLQACIELI-EKPMGLLSIMEEESMFPKATDQTFLE 544
Cdd:cd14900 376 SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTLAS 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 545 KLkTNHLGKSPNFikpKPPKPNQTEAHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGsnlllqaifedhpglgg 624
Cdd:cd14900 455 KL-YRACGSHPRF---SASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVYG----------------- 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 625 gddkggkggrkkgsgfqtvsGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKG 704
Cdd:cd14900 514 --------------------LQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAG 573
|
650
....*....|....*...
gi 556079866 705 FPNRMIYPDFKQRYTILA 722
Cdd:cd14900 574 FPIRLLHDEFVARYFSLA 591
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
95-761 |
1.53e-136 |
|
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: 443.19 E-value: 1.53e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 95 VLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLAN----RENQSMLI 170
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLGRlargPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 171 TGESGAGKTENTKKVIAYFAhvgatskkEEVKKDTKkgnLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPmG 250
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIM--------ELCRGNSQ---LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFRN-G 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 251 KLAGADIETYLLEKARVISQQPAERSYHIFYQLMSG------KIAGLKDKLLL**DVHEF---HFVSQGKTGIAgvddge 321
Cdd:cd14889 151 HVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGisaedrENYGLLDPGKYRYLNNGAgckREVQYWKKKYD------ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 322 ELVvtdTAFDVLGFTDEEKENIYKVTAAVMHFGCLKFKQrpreEQAEADGTEEGER-----VAHLLGLNAADLYKNLLKP 396
Cdd:cd14889 225 EVC---NAMDMVGFTEQEEVDMFTILAGILSLGNITFEM----DDDEALKVENDSNgwlkaAAGQFGVSEEDLLKTLTCT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 397 RIKVGTEFVTQGRNITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQ---HFIGVLDIAGFEIFDHNSFEQMCIN 473
Cdd:cd14889 298 VTFTRGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSvelREIGILDIFGFENFAVNRFEQACIN 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 474 FTNEKLQQFFNHHMFVLEQEEYKREGIEWEFIDFgLDLQACIEL-IEKPMGLLSIMEEESMFPKATDQTFLEKLKTnHLG 552
Cdd:cd14889 378 LANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKLNI-HFK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 553 KSPNFIKPKPPKPNqteahFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHPGLGGGDDKGGKG 632
Cdd:cd14889 456 GNSYYGKSRSKSPK-----FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKL 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 633 GRKKGSGF-----QTVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPN 707
Cdd:cd14889 531 PQAGSDNFnstrkQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSW 610
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 556079866 708 RMIYPDFKQRYTILAPNAVPKGfvdAKNVSEKVIEAIQLdaNDFRFGHSKIFFR 761
Cdd:cd14889 611 RPSFAEFAERYKILLCEPALPG---TKQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
93-761 |
2.19e-136 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 442.56 E-value: 2.19e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERyyCHLI----YTYSGLFCVAINPYKRFPiytKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRE---N 165
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 166 QSMLITGESGAGKTENTKKVIAYF---AHVGATSKKEEVKKDTKKG-----NLEDQVVQTNPVLESFGNAKTVRNDNSSR 237
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLttrAVGGKKASGQDIEQSSKKRklsvtSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 238 FGKFIRIHFGPMG-KLAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKiAGLKDKLLL**DVHEFHFVSQ-GKTGIA 315
Cdd:cd14891 156 FGKFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGA-SAELLKELLLLSPEDFIYLNQsGCVSDD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 316 GVDDGEELVVTDTAFDVLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREE-QAEADGTEEGERVAH---LLGLNAADLYK 391
Cdd:cd14891 235 NIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEgEAEIASESDKEALATaaeLLGVDEEALEK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 392 NLLKPRIKVGTEFVTQGRNITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQHFIGVLDIAGFEIFD-HNSFEQM 470
Cdd:cd14891 315 VITQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 471 CINFTNEKLQQFFNHHMFVLEQEEYKREGIEWEFIDFGlDLQACIELI-EKPMGLLSIMEEESMFPKATDQTFLEKLKTN 549
Cdd:cd14891 395 LINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKT 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 550 HlGKSPNFIkpkPPKPNQTEAHFAIVHYAGTVPYNLTGWLEKNkdplNDCVVDQFkkgSNLLLQaifedhpglgggddkg 629
Cdd:cd14891 474 H-KRHPCFP---RPHPKDMREMFIVKHYAGTVSYTIGSFIDKN----NDIIPEDF---EDLLAS---------------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 630 gkggrkkgsgfqtvSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRM 709
Cdd:cd14891 527 --------------SAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRV 592
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 556079866 710 IYPDFKQRYTILAPNAVPKGFVDA-KNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd14891 593 TYAELVDVYKPVLPPSVTRLFAENdRTLTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
93-761 |
1.02e-134 |
|
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276869 Cd Length: 653 Bit Score: 437.84 E-value: 1.02e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFP-IYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLIT 171
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 172 GESGAGKTENTKKVIAYFAHVGATSKKEEVkkdtkkgnleDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGK 251
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKDKTI----------AKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 252 LAGADIETYLLEKARVISQQPAERSYHIFYQLMSGkIAGLKDKLLL**DVHEFHFV--SQGKTGIAGVDDGEELVVTDTA 329
Cdd:cd14904 151 LIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAG-LSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKLFASTQKS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 330 FDVLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGtEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGR 409
Cdd:cd14904 230 LSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNG-SQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 410 NITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKR-QHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMF 488
Cdd:cd14904 309 APVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRiKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 489 VLEQEEYKREGIEWEFIDFGlDLQACIELIEKPMGLLSIMEEESMFPKATDQTFLEKLKTNH--LGKSPNFikpKPPKPN 566
Cdd:cd14904 389 KTVEEEYIREGLQWDHIEYQ-DNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESI---DFPKVK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 567 QTEahFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHPGLGGGDDKGGKGGRKKGsgfQTVSGL 646
Cdd:cd14904 465 RTQ--FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEAPSETKEGKSGKGTKAP---KSLGSQ 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 647 YREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILAPNAV 726
Cdd:cd14904 540 FKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSM 619
|
650 660 670
....*....|....*....|....*....|....*.
gi 556079866 727 PKGfvDAKNVSEKVIEAI-QLDANDFRFGHSKIFFR 761
Cdd:cd14904 620 HSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
93-761 |
1.92e-134 |
|
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: 437.54 E-value: 1.92e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFP-IYTKRVVEIYKGR--------RRTEVPPHVFAVSDGAYMDMLANR 163
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 164 ENQSMLITGESGAGKTENTKKVIAYF-----------AHVGATSKKEEVKKDTKkgNLEDQVVQTNPVLESFGNAKTVRN 232
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLtqlsqqeqnseEVLTLTSSIRATSKSTK--SIEQKILSCNPILEAFGNAKTVRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 233 DNSSRFGKFIRIHFG-PMGKLAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGLKDKLLL**DVHEFHFVSQGK 311
Cdd:cd14907 159 DNSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSGDRYDYLKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 312 TGIAGVD--DGEELV--VTDtAFDVLGFTDEEKENIYKVTAAVMHFGCLKFKQRP--REEQAEADGTEEGERVAHLLGLN 385
Cdd:cd14907 239 SNCYEVDtiNDEKLFkeVQQ-SFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGID 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 386 AADLYKNLLKPRIKVGTEFVTQGRNITQVTASVGALSKAIFDRLFKWLVKRVNETL--------DTKQKRQHFIGVLDIA 457
Cdd:cd14907 318 EEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 458 GFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWEF--IDFgLDLQACIELIEK-PMGLLSIMEEESMF 534
Cdd:cd14907 398 GFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 535 PKATDQTFLEKLKTNHLGKSPNFIKPKPPKPNqteahFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQA 614
Cdd:cd14907 477 ATGTDEKLLNKIKKQHKNNSKLIFPNKINKDT-----FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISS 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 615 IFEDhpgLGGGDDKGGKGGRKKGSGFQTVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGV 694
Cdd:cd14907 552 IFSG---EDGSQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGV 628
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556079866 695 LEGIRICRKGFPNRMIYPDFKQRYTILAPNAVpkgfvdaknvsekvieaiqldandfrFGHSKIFFR 761
Cdd:cd14907 629 LESIRVRKQGYPYRKSYEDFYKQYSLLKKNVL--------------------------FGKTKIFMK 669
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
93-761 |
8.32e-133 |
|
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: 433.57 E-value: 8.32e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYK--GRRRTE-------VPPHVFAVSDGAYMDMLAN- 162
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 163 RENQSMLITGESGAGKTENTKKVIAYFAHVGatSKKEEVKKDTK---KGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFG 239
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLG--NGEEGAPNEGEelgKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 240 KFIRIHFGPMGKLAGADIETYLLEKARVISQQPAERSYHIFYQLMSG-------KIAGLKDKLLL**DVHEFHFVSQGKT 312
Cdd:cd14908 159 KFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGgdeeeheKYEFHDGITGGLQLPNEFHYTGQGGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 313 -GIAGVDDGEELVVTDTAFDVLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGE---RVAHLLGLNAAD 388
Cdd:cd14908 239 pDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKclaRVAKLLGVDVDK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 389 LYKNLLKPRIKVGTEFVTQGRNITQVTASVGALSKAIFDRLFKWLVKRVNETL--DTKQKRQHFIGVLDIAGFEIFDHNS 466
Cdd:cd14908 319 LLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSSVGVLDIFGFECFAHNS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 467 FEQMCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWEFIDFGlDLQACIELIE-KPMGLLSIMEEESMFP-KATDQTFLE 544
Cdd:cd14908 399 FEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYAS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 545 KLKTNHLGKSPNFI----KPKPPKPNQTEAHFAIVHYAGTVPYNL-TGWLEKNKDPLNDCVVDQFKKGSNlllqaifedh 619
Cdd:cd14908 478 RLYETYLPEKNQTHsentRFEATSIQKTKLIFAVRHFAGQVQYTVeTTFCEKNKDEIPLTADSLFESGQQ---------- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 620 pglgggddkggkggrkkgsgfqtvsglYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIR 699
Cdd:cd14908 548 ---------------------------FKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVR 600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 700 ICRKGFPNRMIYPDFKQRYTILAPnAVPK--------------------GFVDAKNV-SEKVIEAIQLDANDFRFGHSKI 758
Cdd:cd14908 601 VARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlswsmerldpqklcvkkmCKDLVKGVlSPAMVSMKNIPEDTMQLGKSKV 679
|
...
gi 556079866 759 FFR 761
Cdd:cd14908 680 FMR 682
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
93-723 |
2.10e-132 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 433.55 E-value: 2.10e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFP-IYTKRVVEIYK--------GRRRTEVPPHVFAVSDGAYMDMLAN- 162
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKPe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 163 RENQSMLITGESGAGKTENTKKVIAYFAHVGATSKKEEVKKDTKKgNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFI 242
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAV-EIGKRILQTNPILESFGNAQTIRNDNSSRFGKFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 243 RIHFGPMGKLAGADIETYLLEKARVISQQPAERSYHIFYQLMSG----KIAGLKDKLLL**DVHEFHFVSQGKTGIAGVD 318
Cdd:cd14902 160 KIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGadktLLDLLGLQKGGKYELLNSYGPSFARKRAVADK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 319 DGEELVVTDTAFDVLGFTDEEKENIYKVTAAVMHFGCLKFK---QRPREEQAEADGTEEGERVAHLLGLNAADLYKNLLK 395
Cdd:cd14902 240 YAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTaenGQEDATAVTAASRFHLAKCAELMGVDVDKLETLLSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 396 PRIKVGTEFVTQGRNITQVTASVGALSKAIFDRLFKWLVKRVNETLD-------TKQKRQHF--IGVLDIAGFEIFDHNS 466
Cdd:cd14902 320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsISDEDEELatIGILDIFGFESLNRNG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 467 FEQMCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWEFIDFGlDLQACIELIE-KPMGLLSIMEEESMFPKATDQTFLEK 545
Cdd:cd14902 400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGSNQALSTK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 546 LKTNHLGkspnfikpkppkpnqtEAHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHPGLGGG 625
Cdd:cd14902 479 FYRYHGG----------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENRDSPG 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 626 DDKGGKGGRKKGSGFQ-TVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKG 704
Cdd:cd14902 543 ADNGAAGRRRYSMLRApSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHG 622
|
650
....*....|....*....
gi 556079866 705 FPNRMIYPDFKQRYTILAP 723
Cdd:cd14902 623 YSVRLAHASFIELFSGFKC 641
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
839-1731 |
4.56e-131 |
|
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: 441.54 E-value: 4.56e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 839 RVEDELKAMEEKLKKTEEALAKEEKLRKELEEHNVKVLQEKNDLFLQLEAERMGAGDVEERLNKALTQKGDLESQLADLN 918
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 919 DRLSHEEDAHASLSQSKKKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLNDEIQHQDELINKLNKEKKHLQEAS 998
Cdd:pfam01576 82 SRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 999 QKTSEDLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKRKVEGDLKLAQEAVADLEKNKKEMEQNLQRK 1078
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1079 EKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLAREIEELSERLEESGGATSSQIEL 1158
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1159 NKRREAELSKLRRDLEESNLQHEQAMSNLRKKHNDTVAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDHSNKAQA 1238
Cdd:pfam01576 322 RSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1239 NAEKQVKQLEVQLADAQFKVDEMNRTLNDLDGGKKKLAVENSELQRQLEESESQVAQLNKIKASLATQLEEAKRMADEEA 1318
Cdd:pfam01576 402 DSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEET 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1319 RERAAILGKYRNLEHDLDNLRESVEEEQEAKADFQRQLSKANAEAQLWRSKYESEGLArLEELEEAKRKLHGKLQEAEEA 1398
Cdd:pfam01576 482 RQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGT-LEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1399 MEQLNAKCSGLEKTKSHLQGELEDMSIEVDKANALASSLEKRQKSFDKVIAEWKAKVDDLAAELDASQKECRNYSTEVFK 1478
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1479 LRAAYEESQEHYESVKRENKNLQDEVKDLMDQLGEGGRSVHELEKSRKRLEMEKEELQAALEEAEAALEQEENKVLRAQL 1558
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1559 ELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRLKKKLESDINELEIALDHANKANAEAQKNL 1638
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1639 KKYQQNVKDLQGALEEEQRARDEAREQYASAERRCNAMHGELEESRQLLASSKNsHLRHIEQmEGEEL--------LMQK 1710
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASER-ARRQAQQ-ERDELadeiasgaSGKS 878
|
890 900
....*....|....*....|.
gi 556079866 1711 KLRTEVIRLEDALVQVRKEYE 1731
Cdd:pfam01576 879 ALQDEKRRLEARIAQLEEELE 899
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
42-817 |
1.51e-128 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 425.98 E-value: 1.51e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 42 ILGNISSTKGDMVTVDCP-GGERVFKKDQL----QQVNPPKFEkceDMSSLTYLNDASVLHNLKERYYCHLIYTYSGLFC 116
Cdd:PTZ00014 57 VLPGSTGEKLTLKQIDPPtNSTFEVKPEHAfnanSQIDPMTYG---DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 117 VAINPYKRFPIYTKRVVEIYK-GRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITGESGAGKTENTKKVIAYFAhvgaT 195
Cdd:PTZ00014 134 VAINPFKDLGNTTNDWIRRYRdAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFA----S 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 196 SKKEEVKkdtkkGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGKLAGADIETYLLEKARVISQQPAER 275
Cdd:PTZ00014 210 SKSGNMD-----LKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDER 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 276 SYHIFYQLMSGkIAGLKDKLLL**DVHEFHFVSQGKTGIAGVDDGEELVVTDTAFDVLGFTDEEKENIYKVTAAVMHFGC 355
Cdd:PTZ00014 285 SYHIFYQLLKG-ANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGN 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 356 LKFKqrPREEQAEADG---TEEGERV----AHLLGLNAADLYKNLLKPRIKVGTEFVTQGRNITQVTASVGALSKAIFDR 428
Cdd:PTZ00014 364 VEIE--GKEEGGLTDAaaiSDESLEVfneaCELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEK 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 429 LFKWLVKRVNETLDTKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWEFIDFG 508
Cdd:PTZ00014 442 LFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYT 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 509 LDLQACIELIEKPMGLLSIMEEESMFPKATDQTFLEKLKTNhLGKSPNFikpKPPKPNQTEaHFAIVHYAGTVPYNLTGW 588
Cdd:PTZ00014 522 SNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTN-LKNNPKY---KPAKVDSNK-NFVIKHTIGDIQYCASGF 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 589 LEKNKDPLNDCVVDQFKKGSNLLLQAIFEDhpglgggddkgGKGGRKKGSGFQTVSGLYREQLNKLMATLNSTSPHFVRC 668
Cdd:PTZ00014 597 LFKNKDVLRPELVEVVKASPNPLVRDLFEG-----------VEVEKGKLAKGQLIGSQFLNQLDSLMSLINSTEPHFIRC 665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 669 IIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILAPNAVPKGFVDAKNVSEKVIEAIQLDA 748
Cdd:PTZ00014 666 IKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPK 745
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556079866 749 NDFRFGHSKIFFRAGVLGRLEEMRDERLSKIMTMIQAAVRWYICKKHFQKLKEQRVALLVIQRNLRKFL 817
Cdd:PTZ00014 746 DSYAIGKTMVFLKKDAAKELTQIQREKLAAWEPLVSVLEALILKIKKKRKVRKNIKSLVRIQAHLRRHL 814
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
94-761 |
4.78e-119 |
|
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: 394.70 E-value: 4.78e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 94 SVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPiytkRVVEIYKGRRR----TEVPPHVFAVSDGAYMDML-------AN 162
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP----GLYDLHKYREEmpgwTALPPHVFSIAEGAYRSLRrrlhepgAS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 163 RENQSMLITGESGAGKTENTKKVIAYFAHVgATSKKEEVKKDTKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFI 242
Cdd:cd14895 78 KKNQTILVSGESGAGKTETTKFIMNYLAES-SKHTTATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 243 RIHFGPMG-----KLAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGLKDKLL-L**DVHEFHFVSQGKTGIA- 315
Cdd:cd14895 157 RMFFEGHEldtslRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQlELLSAQEFQYISGGQCYQRn 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 316 -GVDDGEELVVTDTAFDVLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGT------------------EEGE 376
Cdd:cd14895 237 dGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAasapcrlasaspssltvqQHLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 377 RVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGRNITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQH------- 449
Cdd:cd14895 317 IVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALNpnkaank 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 450 ----FIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWEFIDFGLDlQACIELIE-KPMGL 524
Cdd:cd14895 397 dttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLEqRPSGI 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 525 LSIMEEESMFPKATDQTFLEKLkTNHLGKSPNFikpKPPKPNQTEAHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQF 604
Cdd:cd14895 476 FSLLDEECVVPKGSDAGFARKL-YQRLQEHSNF---SASRTDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 605 KKGSNLLLQAIFEDHPGLGGGDDKGGKGGRKKGSGFQTVSGL---YREQLNKLMATLNSTSPHFVRCIIPNETKSPGVID 681
Cdd:cd14895 552 GKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSSVGIgsqFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFD 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 682 SHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILapnavpkgfVDAKNVSE----KVIEAIQLDANDfrFGHSK 757
Cdd:cd14895 632 MAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLL---------VAAKNASDatasALIETLKVDHAE--LGKTR 700
|
....
gi 556079866 758 IFFR 761
Cdd:cd14895 701 VFLR 704
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
93-722 |
3.19e-116 |
|
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: 384.52 E-value: 3.19e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITG 172
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 173 ESGAGKTENTKKVIAYFAHVGATSKKEEVKkdtkkgnledQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFgPMGKL 252
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQTEDRLR----------QPEDVLPILESFGHAKTILNANASRFGQVLRLHL-QHGVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 253 AGADIETYLLEKARVISQQPAERSYHIFYQLMSGkIAGLKDKLLL**DVHEFHFVSQGKT-GIAGVDDGEELVVTDTAFD 331
Cdd:cd14896 150 VGASVSHYLLETSRVVFQAQAERSFHVFYELLAG-LDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFEGLLKALQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 332 VLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGE--RVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGR 409
Cdd:cd14896 229 GLGLCAEELTAIWAVLAAILQLGNICFSSSERESQEVAAVSSWAEihTAARLLQVPPERLEGAVTHRVTETPYGRVSRPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 410 NITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQHF--IGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHM 487
Cdd:cd14896 309 PVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 488 FVLEQEEYKREGIEWEFIDfGLDLQACIELI-EKPMGLLSIMEEESMFPKATDQTFLEKLKTNHlGKSPNFIKPKPPKPN 566
Cdd:cd14896 389 LAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQLPLPV 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 567 qteahFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHPGLGGGDDKGGkggrkkgsgfqTVSGL 646
Cdd:cd14896 467 -----FTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP-----------TLASR 530
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556079866 647 YREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILA 722
Cdd:cd14896 531 FQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALG 606
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
93-759 |
1.10e-115 |
|
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: 382.80 E-value: 1.10e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRR-TEVPPHVFAVSDGAYMDMLANRENQSMLIT 171
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDlTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 172 GESGAGKTENTKKVIAYFAHvgatskkeevkkdTKKGNLeDQVVQT-----NPVLESFGNAKTVRNDNSSRFGKFIRIHF 246
Cdd:cd14876 81 GESGAGKTEATKQIMRYFAS-------------AKSGNM-DLRIQTaimaaNPVLEAFGNAKTIRNNNSSRFGRFMQLDV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 247 GPMGKLAGADIETYLLEKARVISQQPAERSYHIFYQLMSGkIAGLKDKLLL**DVHEFHFVSQGKTGIAGVDDGEELVVT 326
Cdd:cd14876 147 ASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKG-ADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFEEV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 327 DTAFDVLGFTDEEKENIYKVTAAVMHFGCLKFKQRPR---EEQAEADGTEEG--ERVAHLLGLNAADLYKNLLKPRIKVG 401
Cdd:cd14876 226 LESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEqgvDDAAAISNESLEvfKEACSLLFLDPEALKRELTVKVTKAG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 402 TEFVTQGRNITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQ 481
Cdd:cd14876 306 GQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 482 FFNHHMFVLEQEEYKREGIEWEFIDFGLDLQACIELIEKPMGLLSIMEEESMFPKATDQTFLEKLKTNhLGKSPnfiKPK 561
Cdd:cd14876 386 NFIDIVFERESKLYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSK-LKSNG---KFK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 562 PPKPNQtEAHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHPGLGGGDDKGgkggrkkgsgfQ 641
Cdd:cd14876 462 PAKVDS-NINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKGKIAKG-----------S 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 642 TVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTIL 721
Cdd:cd14876 530 LIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFL 609
|
650 660 670
....*....|....*....|....*....|....*...
gi 556079866 722 APNAVPKGFVDAKNVSEKVIEAIQLDANDFRFGHSKIF 759
Cdd:cd14876 610 DLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
93-745 |
7.97e-115 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 382.79 E-value: 7.97e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFP-IYTKRVVEIYKGRRR-TEVPPHVFAVSDGAYMDMLANRENQSMLI 170
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 171 TGESGAGKTENTKKVIAYFAHVGATSKKEEVKKDTKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHF-GPM 249
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFrSSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 250 GKLAGADIETYLLEKARvISQQP--AERSYHIFYQLMSGKIAGLKDKLLL**DVHEFHFVSQGKTGIAGV---------- 317
Cdd:cd14906 161 GKIDGASIETYLLEKSR-ISHRPdnINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFksqssnknsn 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 318 -----DDGEELVVTDTAFDVLGFTDEEKENIYKVTAAVMHFGCLKFKQ---RPREEQAEADGTEEGERVAHLLGLNAADL 389
Cdd:cd14906 240 hnnktESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEdsdFSKYAYQKDKVTASLESVSKLLGYIESVF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 390 YKNLLKPRIKVGTEFVTQGR--NITQVTASVGALSKAIFDRLFKWLVKRVNETLD-----------TKQKRQHFIGVLDI 456
Cdd:cd14906 320 KQALLNRNLKAGGRGSVYCRpmEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNqntqsndlaggSNKKNNLFIGVLDI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 457 AGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWEFIDFgLDLQACIELIE-KPMGLLSIMEEESMFP 535
Cdd:cd14906 400 FGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMP 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 536 KATDQTFLEKLKTNHLGkspnfiKPKPPKPNQTEAHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAI 615
Cdd:cd14906 479 KGSEQSLLEKYNKQYHN------TNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 616 FEdhpglggGDDKGGKGGRKKGSGFQTVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVL 695
Cdd:cd14906 553 FQ-------QQITSTTNTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVL 625
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 556079866 696 EGIRICRKGFPNRMIYPDFKQRYTILAPNAVPKGFVDAKNVSEKVIEAIQ 745
Cdd:cd14906 626 NTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIQ 675
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
93-761 |
1.81e-113 |
|
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: 377.23 E-value: 1.81e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERY-YCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTE-VPPHVFAVSDGAYMDM-LANRENQSML 169
Cdd:cd14875 1 ATLLHCIKERFeKLHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRlLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 170 ITGESGAGKTENTKKVIAY-----FAHVGATSKKEEVKKdtkkgnLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRI 244
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYlgqlsYMHSSNTSQRSIADK------IDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 245 HFGPM-GKLAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGLKDKLLL**DVHEFHFVSQGKT----GIAG--V 317
Cdd:cd14875 155 YFDPTsGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGNTfvrrGVDGktL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 318 DDGEELVVTDTAFDVLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGErVAHLLGLNAADLYKNLLkpr 397
Cdd:cd14875 235 DDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFLT-ACRLLQLDPAKLRECFL--- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 398 IKVGTEFVTQGRNITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQ--KRQHFIGVLDIAGFEIFDHNSFEQMCINFT 475
Cdd:cd14875 311 VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGdcSGCKYIGLLDIFGFENFTRNSFEQLCINYA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 476 NEKLQQFFNHHMFVLEQEEYKREGIEWEFIDFGlDLQACIELIE-KPMGLLSIMEEESMFPKATDQTFLEKLKTNHLGKS 554
Cdd:cd14875 391 NESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 555 PNFIKPKPPKPNQteahFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHPGLGGGDdkggkggr 634
Cdd:cd14875 470 PYFVLPKSTIPNQ----FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLARRK-------- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 635 kkgsgfQTVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDF 714
Cdd:cd14875 538 ------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQF 611
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 556079866 715 KQRYTILAPNAVPKGFvDAKNVSEKVIEAIQL-------DANDFRFGHSKIFFR 761
Cdd:cd14875 612 CRYFYLIMPRSTASLF-KQEKYSEAAKDFLAYyqrlygwAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
93-718 |
2.82e-111 |
|
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: 372.51 E-value: 2.82e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFP-IYTKRVVEIYK-------GRRRTEV---PPHVFAVSDGAYMDMLA 161
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhnsqfGDRVTSTdprEPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 162 NRENQSMLITGESGAGKTENTKKVIAYFA-------HVGATSKKEEVKKDTKKGNLEDQVVQTNPVLESFGNAKTVRNDN 234
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAvhcgtgnNNLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 235 SSRFGKFIRIHF-GPMGKLAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGLKDKLLL**DV----HEFHFVSQ 309
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADNNCVSKEQKQVLALsggpQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 310 GKTGIA--GVDDGEELVVTDTAFDVLGFTDEEKENIYKVTAAVMHFGCLKFKQRP--REEQAEADGT----------EEG 375
Cdd:cd14899 241 SLCSKRrdGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPhkGDDTVFADEArvmssttgafDHF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 376 ERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGRNITQVTASVGALSKAIFDRLFKWLVKRVNETL-------------- 441
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 442 -DTKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWEFIDFGlDLQACIELIE- 519
Cdd:cd14899 401 vDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEh 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 520 KPMGLLSIMEEESMFPKATDQTFLEK--LKTNHLGKSPNFikpKPPKPNQTEAHFAIVHYAGTVPYNLTGWLEKNKDPLN 597
Cdd:cd14899 480 RPIGIFSLTDQECVFPQGTDRALVAKyyLEFEKKNSHPHF---RSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFC 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 598 DCVVDQFKKGSNLLLQAI-----FEDHPGLGGGDDKGGKGGRKKGSGFQTVS--GLYREQLNKLMATLNSTSPHFVRCII 670
Cdd:cd14899 557 ESAAQLLAGSSNPLIQALaagsnDEDANGDSELDGFGGRTRRRAKSAIAAVSvgTQFKIQLNELLSTVRATTPRYVRCIK 636
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 556079866 671 PNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRY 718
Cdd:cd14899 637 PNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
93-723 |
5.82e-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: 366.87 E-value: 5.82e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFP-IYTKRVVEIYKGRRRTE-VPPHVFAVSDGAYMDMLANRE--NQSM 168
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQPQkLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 169 LITGESGAGKTENTKKVIAYFAHVGATSKKEEVKKDTKKgnLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGP 248
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAER--IEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 249 MGKLAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGLKDKLLL**DVhEFHFVSQGKTGIagvdDGEELVVTDT 328
Cdd:cd14880 159 AQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGA-AFSWLPNPERNL----EEDCFEVTRE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 329 AFDVLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQA--EADGTEEGERV-AHLLGLNAADLYKNLLKPRIKVGTEFV 405
Cdd:cd14880 234 AMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqPMDDTKESVRTsALLLKLPEDHLLETLQIRTIRAGKQQQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 406 TQGRNITQVTASV--GALSKAIFDRLFKWLVKRVNETLDTKQKR-QHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQF 482
Cdd:cd14880 314 VFKKPCSRAECDTrrDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 483 FNHHMFVLEQEEYKREGIEWEFIDFGlDLQACIELIE-KPMGLLSIMEEESMFPKATD----QTFLEKLKTNHLGKSPNF 557
Cdd:cd14880 394 FVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIEgSPISICSLINEECRLNRPSSaaqlQTRIESALAGNPCLGHNK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 558 IKPKPpkpnqteaHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHPGLGGGDDKGGKGGRKKG 637
Cdd:cd14880 473 LSREP--------SFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQSRAPVL 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 638 sgfqTVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQR 717
Cdd:cd14880 545 ----TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVER 620
|
....*.
gi 556079866 718 YTILAP 723
Cdd:cd14880 621 YKLLRR 626
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
93-761 |
4.46e-107 |
|
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: 358.04 E-value: 4.46e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFP-IYTKRVVEIYKGRRRT-----EVPPHVFAVSDGAYMDMLANRENQ 166
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 167 SMLITGESGAGKTENTKKVIAYFAHvGATSKKEEVKKdtkkgnledQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHF 246
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAY-GHSTSSTDVQS---------LILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 247 GPMGKLAGADIETYLLEKARVISQQPAERSYHIFYQLMSGkIAGLKDKLLL**DVHEFHFVSQGKT-GIAGVDDGEELVV 325
Cdd:cd14886 151 GPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKG-LSPEEKKSLGFKSLESYNFLNASKCyDAPGIDDQKEFAP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 326 TDTAFDVLgFTDEEKENIYKVTAAVMHFGCLKFKQRPR---EEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGT 402
Cdd:cd14886 230 VRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 403 EFVTQGRNITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQF 482
Cdd:cd14886 309 ETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 483 FNHHMFVLEQEEYKREGIEWEFIDFGlDLQACIELIEKP-MGLLSIMEEESMFPKATDQTFLEKLKTnHLgKSPNFIkpk 561
Cdd:cd14886 389 FINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSCKS-KI-KNNSFI--- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 562 PPKPNQTEahFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHPGLGGGDDKggkggrkkgsgfQ 641
Cdd:cd14886 463 PGKGSQCN--FTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNMKG------------K 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 642 TVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTIL 721
Cdd:cd14886 529 FLGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKIL 608
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 556079866 722 A--PNAVPKGFVDAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd14886 609 IshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
93-722 |
7.70e-97 |
|
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: 328.31 E-value: 7.70e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIY---KGRRRTEVPPHVFAVSDGAYMDMLANRENQSML 169
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 170 ITGESGAGKTENTKKVIAYFAhvgatskkeeVKKDTKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPM 249
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLT----------CRASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCER 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 250 GK-LAGADIETYLLEKARVISQQPAERSYHIFYQLMSGkIAGLKDKLLL**DVHEFHFVSQGKTG----IAGVDDGEELV 324
Cdd:cd14878 151 KKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDG-LSAEEKYGLHLNNLCAHRYLNQTMREdvstAERSLNREKLA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 325 VTDTAFDVLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEF 404
Cdd:cd14878 230 VLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 405 VTQGRNITQVTASVGALSKAIFDRLFKWLVKRVNETL----DTKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQ 480
Cdd:cd14878 310 IIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 481 QFFNHHMFVLEQEEYKREGIEWEFIdFGLDLQACIE--LIEKPMGLLSIMEEESM--------FPKATdQTFLEKLKTNH 550
Cdd:cd14878 390 HYINEVLFLQEQTECVQEGVTMETA-YSPGNQTGVLdfFFQKPSGFLSLLDEESQmiwsvepnLPKKL-QSLLESSNTNA 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 551 LGKSPNFIKPKPPKPNQTEAhFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEdhpglgggddkgg 630
Cdd:cd14878 468 VYSPMKDGNGNVALKDQGTA-FTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ------------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 631 kggrkkgSGFQTVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMI 710
Cdd:cd14878 534 -------SKLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLS 606
|
650
....*....|..
gi 556079866 711 YPDFKQRYTILA 722
Cdd:cd14878 607 FSDFLSRYKPLA 618
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
93-761 |
1.47e-95 |
|
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: 325.80 E-value: 1.47e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITG 172
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 173 ESGAGKTENTKKVIAYFAHV-GATSKKEEVKKdtkkgnledqVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGK 251
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAaGSVGGVLSVEK----------LNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 252 LAGADIETYLLEKARVISQQPAERSYHIFYQLMSGkiaglkdklLL**DVHEFHF---VSQGKTGIAGVDDGEE------ 322
Cdd:cd01386 151 LASASIQTLLLERSRVARRPEGESNFNVFYYLLAG---------ADAALRTELHLnqlAESNSFGIVPLQKPEDkqkaaa 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 323 -LVVTDTAFDVLGFTDEEKENIYKVTAAVMHFGC---LKFKQRPREEQAEadgTEEGERVAHLLGLNAADL----YKNLL 394
Cdd:cd01386 222 aFSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFAR---PEWAQRAAYLLGCTLEELssaiFKHHL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 395 KPRIKVGTEFVTQ---------GRNITQVTAsVGALSKAIFDRLFKWLVKRVNETLDTKQKRQHFIGVLDIAGFEIFDHN 465
Cdd:cd01386 299 SGGPQQSTTSSGQesparsssgGPKLTGVEA-LEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 466 ------SFEQMCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWEFIDFGLDLQACIELIEK---------------PMGL 524
Cdd:cd01386 378 gsqrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQapqqalvrsdlrdedRRGL 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 525 LSIMEEESMFPKATDQTFLEKLKTnHLGKSPNFIKPKPPKPNQTEAHFAIVHYAGT--VPYNLTGWLEKNKD---PLNDC 599
Cdd:cd01386 458 LWLLDEEALYPGSSDDTFLERLFS-HYGDKEGGKGHSLLRRSEGPLQFVLGHLLGTnpVEYDVSGWLKAAKEnpsAQNAT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 600 VVDQ-------FKKGSNLLLQAIFedhpglgggddkggkggrkkgsgfqtvsglyreQLNKLMATLNSTSPHFVRCIIPN 672
Cdd:cd01386 537 QLLQesqketaAVKRKSPCLQIKF---------------------------------QVDALIDTLRRTGLHFVHCLLPQ 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 673 ------------ETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILAPNAVPKGF-----VDAKN 735
Cdd:cd01386 584 hnagkderstssPAAGDELLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERK 663
|
730 740
....*....|....*....|....*.
gi 556079866 736 VSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd01386 664 AVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
90-760 |
4.45e-93 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 317.18 E-value: 4.45e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 90 LNDASVLHNLKERYYCHLIYTY---SGLfcVAINPYKRFPIYTKRVVEIYKGRRRTE-------VPPHVFAVSDGAYMDM 159
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGSEYYDTtsgskepLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 160 LANRENQSMLITGESGAGKTENTKKVIAYFAHVGATSKKEevkkdTKkgnLEDQVVQTNPVLESFGNAKTVRNDNSSRFG 239
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKKG-----TK---LSSQISAAEFVLDSFGNAKTLTNPNASRFG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 240 KFIRIHFGPMGKLAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGLKDKLLL**DVHEFHFVSQGK---TGIAG 316
Cdd:cd14879 151 RYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYGChplPLGPG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 317 VDDGEELVVTDTAFDVLGFTDEEKENIYKVTAAVMHFGCLKFKQRP--REEQAEADGTEEGERVAHLLGLNAADL----- 389
Cdd:cd14879 231 SDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHegGEESAVVKNTDVLDIVAAFLGVSPEDLetslt 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 390 YKNLLkprikVGTEFVTQGRNITQVTASVGALSKAIFDRLFKWLVKRVNETL-DTKQKRQHFIGVLDIAGFEIFD---HN 465
Cdd:cd14879 311 YKTKL-----VRKELCTVFLDPEGAAAQRDELARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQNRSstgGN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 466 SFEQMCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWEFIDFgLDLQACIELI-EKPMGLLSIMEEE-SMFPKATDQTFL 543
Cdd:cd14879 386 SLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQtRRMPKKTDEQML 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 544 EKLKtNHLGKSPNFIKPKPPKPNQTEAHFAIVHYAGTVPYNLTGWLEKNKDPLN-DCVvdqfkkgsNLLLQAIFEdhpgl 622
Cdd:cd14879 465 EALR-KRFGNHSSFIAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSpDFV--------NLLRGATQL----- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 623 gggddkggkggrkkgsgfqtvsglyREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICR 702
Cdd:cd14879 531 -------------------------NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLR 585
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 556079866 703 KGFPNRMIYPDFKQRYTILAPNAvpkgfvDAKNVSEKVIEAIQLDANDFRFGHSKIFF 760
Cdd:cd14879 586 VEYVVSLEHAEFCERYKSTLRGS------AAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
94-725 |
1.63e-92 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 313.37 E-value: 1.63e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 94 SVLHNLKERYYCHLIYTYSGLFCVAINPYKRfpIYTKRVVEIYKgRRRTEVPPHVFAVSDGAYMDMLANrENQSMLITGE 173
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLVH-GNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 174 SGAGKTENTKKVIAYFAHVGATSKKeevkkdtkkgnLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGpmGKLA 253
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTTS-----------IEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKIT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 254 GADIETYLLEKARVISQQPAERSYHIFYQLMSGKiaglkdKLLL**DVHEFHFVSQGKTGIagVDDGEELVVTDTAFDVL 333
Cdd:cd14898 145 GAKFETYLLEKSRVTHHEKGERNFHIFYQFCASK------RLNIKNDFIDTSSTAGNKESI--VQLSEKYKMTCSAMKSL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 334 GFTDeeKENIYKVTAAVMHFGCLKFKQrprEEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQGRNITQ 413
Cdd:cd14898 217 GIAN--FKSIEDCLLGILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 414 VTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQhfIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVLEQE 493
Cdd:cd14898 292 ARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 494 EYKREGIEWEFIDFgLDLQACIELIEKPMGLLSIMEEESMFPKATDQTFLEKLKTNHLGkspnFIKPKppkpnqTEAHFA 573
Cdd:cd14898 370 MYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIKKYLNG----FINTK------ARDKIK 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 574 IVHYAGTVPYNLTGWLEKNKDplndcvvdqfkkGSNLLlqaIFEDhpglgggddkggkGGRKKGSGFQTVSGLYREQLNK 653
Cdd:cd14898 439 VSHYAGDVEYDLRDFLDKNRE------------KGQLL---IFKN-------------LLINDEGSKEDLVKYFKDSMNK 490
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556079866 654 LMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILAPNA 725
Cdd:cd14898 491 LLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
93-761 |
1.09e-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: 303.88 E-value: 1.09e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERY--------YCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRE 164
Cdd:cd14887 1 PNLLENLYQRYnkayinkeNRNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 165 NQSMLITGESGAGKTENTKKVIAYFAHVgatskkEEVKKDTKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRI 244
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAV------SDRRHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 245 HFGPMGKLAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAglkdklll**dvhefhfvSQGKTGIAGVDDGE--E 322
Cdd:cd14887 155 HFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVA------------------AATQKSSAGEGDPEstD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 323 LVVTDTAFDVLGFTDEEKENIYKVTAAVMHFGCLKF--KQRPRE-------------EQAEADGTEEGE----------- 376
Cdd:cd14887 217 LRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFttDQEPETskkrkltsvsvgcEETAADRSHSSEvkclssglkvt 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 377 --------RVAHLLGLNAADLYKNLLkpRIKVGTEFVTQGR---NITQVTASVGALSKAIFDRLFKWLVKRVNETL---- 441
Cdd:cd14887 297 easrkhlkTVARLLGLPPGVEGEEML--RLALVSRSVRETRsffDLDGAAAARDAACKNLYSRAFDAVVARINAGLqrsa 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 442 ---------DTK-QKRQHFIGVLDIAGFEIFDH---NSFEQMCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWEFI--D 506
Cdd:cd14887 375 kpsesdsdeDTPsTTGTQTIGILDLFGFEDLRNhskNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsA 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 507 FGLDLQACIELIEKP------------------------MGLLSIMEEE-SMFPKATDQTFLEKLKTNHLGKS-PNFIKP 560
Cdd:cd14887 455 FPFSFPLASTLTSSPsstspfsptpsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKNiINSAKY 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 561 KPPKPNQTEAH--FAIVHYAGTVPYNLTGWLEKNKDPLNDcVVDQFKKGSNLLLQAIFEDhpglgggddkGGKGGRKKGS 638
Cdd:cd14887 535 KNITPALSRENleFTVSHFACDVTYDARDFCRANREATSD-ELERLFLACSTYTRLVGSK----------KNSGVRAISS 603
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 639 GFQTVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRY 718
Cdd:cd14887 604 RRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRY 683
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 556079866 719 TILAPNAVpKGFVDAKNVSEKVIEAIQLDANDFRFGHSKIFFR 761
Cdd:cd14887 684 ETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
93-761 |
5.61e-86 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 296.16 E-value: 5.61e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRvveiYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITG 172
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 173 ESGAGKTENTKKVIAYFAhvgatskkEEVKKDTkkgNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGKL 252
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL--------SGVKEDN---EISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 253 AGADIETYLLEKARVISQQPAERSYHIFYQLMSGkIAGLKDKLLL**DVHEFHFVSQGKTGIAGVDDGEELVVTDTAFDV 332
Cdd:cd14937 146 VSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNG-MSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISFDK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 333 LGFTDeEKENIYKVTAAVMHFGCLKFKQ-----RPREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGTEFVTQ 407
Cdd:cd14937 225 MNMHD-MKDDLFLTLSGLLLLGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 408 GRNITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHM 487
Cdd:cd14937 304 PLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 488 FVLEQEEYKREGIEWEFIDFGLDlQACIELIEKPMGLLSIMEEESMFPKATDQTFLeKLKTNHLGKSPNFikpKPPKPNQ 567
Cdd:cd14937 384 YEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESIV-SVYTNKFSKHEKY---ASTKKDI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 568 TEaHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHPGLGGGDDKggkggrkkgsgfQTVSGLY 647
Cdd:cd14937 459 NK-NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRK------------NLITFKY 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 648 REQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRIcRKGFPNRMIYPDFKQRYTILAPNAVP 727
Cdd:cd14937 526 LKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSK 604
|
650 660 670
....*....|....*....|....*....|....*.
gi 556079866 728 KGFVDAKnvsEKVIEAIQ--LDANDFRFGHSKIFFR 761
Cdd:cd14937 605 DSSLTDK---EKVSMILQntVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
92-795 |
1.72e-76 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 268.14 E-value: 1.72e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 92 DAsVLHNLKERYYCHLIYTYSGLFCVAINPYKrfpiytkrvveiYKGRRRTEVPPHvfAVSDGAYMDML---ANREN--- 165
Cdd:cd14881 1 DA-VMKCLQARFYAKEFFTNVGPILLSVNPYR------------DVGNPLTLTSTR--SSPLAPQLLKVvqeAVRQQset 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 166 ---QSMLITGESGAGKTENTKKVI-AYFAHVGATSKKEEVKkdtkkgnledQVVQTNPVLESFGNAKTVRNDNSSRFGKF 241
Cdd:cd14881 66 gypQAIILSGTSGSGKTYASMLLLrQLFDVAGGGPETDAFK----------HLAAAFTVLRSLGSAKTATNSESSRIGHF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 242 IRIHFGPmGKLAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGLKDKLLL*-*DVHEFHFVSQGKTGIAGVDDG 320
Cdd:cd14881 136 IEVQVTD-GALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgYSPANLRYLSHGDTRQNEAEDA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 321 EELVVTDTAFDVLG--FTDeekenIYKVTAAVMHFGCLKFKQrPREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRI 398
Cdd:cd14881 215 ARFQAWKACLGILGipFLD-----VVRVLAAVLLLGNVQFID-GGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTH 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 399 KVGTEFVTQGRNITQVTASVGALSKAIFDRLFKWLVKRVNE------TLDTKqKRQHFIGVLDIAGFEIFDHNSFEQMCI 472
Cdd:cd14881 289 NARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANSlkrlgsTLGTH-ATDGFIGILDMFGFEDPKPSQLEHLCI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 473 NFTNEKLQQFFNHHMFVLEQEEYKREGIEWEF-IDFgLDLQACIELIEK-PMGLLSIMEEESMfPKATDQTFLEKLKTNH 550
Cdd:cd14881 368 NLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQH 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 551 LGkSPNFIKPKPPKPNQteahFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSnllLQAIFEDHpglgggddkgg 630
Cdd:cd14881 446 RQ-NPRLFEAKPQDDRM----FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN---CNFGFATH----------- 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 631 kggrkkGSGFQTvsglyreQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMI 710
Cdd:cd14881 507 ------TQDFHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMR 573
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 711 YPDFKQRYTILAPNAVPKGFVDAKNVSEKVIeaiqldaNDFrfghskiffragvlgrLEEMRDERLSkimtmiQAAVRWY 790
Cdd:cd14881 574 FKAFNARYRLLAPFRLLRRVEEKALEDCALI-------LQF----------------LEAQPPSKLS------SVSTSWA 624
|
....*
gi 556079866 791 ICKKH 795
Cdd:cd14881 625 LGKRH 629
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
93-761 |
2.00e-73 |
|
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: 259.03 E-value: 2.00e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYkgrrrtevppHVFAVSDGAYMDMLANRENQSMLI-T 171
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNAESIVfG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 172 GESGAGKTENTKKVIAYFahvgatSKKEEVKKDTKKGNledqVVQTnpVLESFGNAKTVRNDNSSRFGKFIRIHFgPMGK 251
Cdd:cd14874 71 GESGSGKSYNAFQVFKYL------TSQPKSKVTTKHSS----AIES--VFKSFGCAKTLKNDEATRFGCSIDLLY-KRNV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 252 LAGADIE-TYLLEKARVISQQPAERSYHIFYQLMSGkIAGLKDKLLL**DVHEFHFVSQGKTGIAGVDDGEELVVTDTAF 330
Cdd:cd14874 138 LTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHG-LNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLEDAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 331 DVLGFTDEEKENIYKVTAAVMHFGCLKFKQR--PREEQ--AEADGTEEGERVAHLLGLNAaDLYKNLLKPRIKVGTEFvt 406
Cdd:cd14874 217 HVLGFSDDHCISIYKIISTILHIGNIYFRTKrnPNVEQdvVEIGNMSEVKWVAFLLEVDF-DQLVNFLLPKSEDGTTI-- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 407 qgrNITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQkRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHH 486
Cdd:cd14874 294 ---DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPL-HTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKH 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 487 MFVLEQEEYKREGIEWEF-IDFGLDLQACIELI-EKPMGLLSIMEEESMFPKATDQTFLEKLKTNHLGKSpNFIKPKppk 564
Cdd:cd14874 370 SFHDQLVDYAKDGISVDYkVPNSIENGKTVELLfKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRS-SYGKAR--- 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 565 pNQTEAHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDHpglgggddkggkgGRKKGSGFQTVS 644
Cdd:cd14874 446 -NKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESY-------------SSNTSDMIVSQA 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 645 GLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILAPN 724
Cdd:cd14874 512 QFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLPG 591
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 556079866 725 AVPKgfvdAKNVSEKVIEAIQLDA----NDFRFGHSKIFFR 761
Cdd:cd14874 592 DIAM----CQNEKEIIQDILQGQGvkyeNDFKIGTEYVFLR 628
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
93-709 |
2.79e-73 |
|
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: 260.22 E-value: 2.79e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 93 ASVLHNLKERYYCHLIYTYSGLFCVAINPYKRFP-IYTKRVVEIYKGRRRTE-------VPPHVFAVSDGAYMDMLANRE 164
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 165 NQSMLITGESGAGKTENTKKVIAYFAHVgatskkeevKKDTKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRI 244
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI---------QTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 245 HF---------GPMGKLAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGLKDKLLL**DVHEFHF----VSQGK 311
Cdd:cd14884 152 IFeeventqknMFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLlnpdESHQK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 312 TGIAG--------VDDGEELVVTDTA-----FDVLGFT--DEEKEN-IYKVTAAVMHFGCLKFKQrpreeqaeadgteeg 375
Cdd:cd14884 232 RSVKGtlrlgsdsLDPSEEEKAKDEKnfvalLHGLHYIkyDERQINeFFDIIAGILHLGNRAYKA--------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 376 erVAHLLGLNAADLyKNLLKPR-IKVGTEFVTQGRNITQVTASVGALSKAIFDRLFKWLVKRVNET-LDTKQKRQ----- 448
Cdd:cd14884 297 --AAECLQIEEEDL-ENVIKYKnIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNvLKCKEKDEsdned 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 449 ------HFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVLEQEEYKREGIEW--EFIDFGLDLQACIELIEK 520
Cdd:cd14884 374 iysineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICcsDVAPSYSDTLIFIAKIFR 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 521 pmGLLSIMEEESMFPKATDQTFLEKLKTN----HLGK--SPNFIKPK-----PPKPNQTEAHFAIVHYAGTVPYNLTGWL 589
Cdd:cd14884 454 --RLDDITKLKNQGQKKTDDHFFRYLLNNerqqQLEGkvSYGFVLNHdadgtAKKQNIKKNIFFIRHYAGLVTYRINNWI 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 590 EKNKDPLNDCVVDQFKKGSNLLLQaifedhpglgggddkgGKGGRKKGSGFQTVSGLYREQLNKLMATLNSTSPHFVRCI 669
Cdd:cd14884 532 DKNSDKIETSIETLISCSSNRFLR----------------EANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCF 595
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 556079866 670 IPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRM 709
Cdd:cd14884 596 LPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKI 635
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
94-761 |
4.25e-66 |
|
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: 238.84 E-value: 4.25e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 94 SVLHNLKERYYCHLIYTYSGLFCVAINPYKRFP-IYTKRVVEIYKGRRrtEVPPHVFAVSDGAYMDMLANRENQSMLITG 172
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYNQRR--GLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 173 ESGAGKTENTKKVIAYFAHVGATSKKEevkkdtkkgnLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGKL 252
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTDLSRSKY----------LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 253 AGADIETYLLEKARVISQQPAERSYHIFYQLMSGkIAGLKDKLLL**DVHEFHFVSQGKT-GIAGVDDGEELVVTDTAFD 331
Cdd:cd14905 150 QGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKG-ITDEEKAAYQLGDINSYHYLNQGGSiSVESIDDNRVFDRLKMSFV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 332 VLGFTDEEKENIYKVTAAVMHFGCLKFKQrpREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRikvgtefvtqGRNI 411
Cdd:cd14905 229 FFDFPSEKIDLIFKTLSFIIILGNVTFFQ--KNGKTEVKDRTLIESLSHNITFDSTKLENILISDR----------SMPV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 412 TQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQkRQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVLE 491
Cdd:cd14905 297 NEAVENRDSLARSLYSALFHWIIDFLNSKLKPTQ-YSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 492 QEEYKREGIEWEFIDFGLDLQACIELIEKpmgLLSIMEEESMFPKATDQTFLEKLKtNHLGKSPNFIKpkppKPNQteah 571
Cdd:cd14905 376 QREYQTERIPWMTPISFKDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKLQ-NFLSRHHLFGK----KPNK---- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 572 FAIVHYAGTVPYNLTGWLEKNKdplndcvvDQFKKGSNLLLQAIFEDHPGLGGGDDKGGKGGRKKGSGFQTVSGLYREQL 651
Cdd:cd14905 444 FGIEHYFGQFYYDVRGFIIKNR--------DEILQRTNVLHKNSITKYLFSRDGVFNINATVAELNQMFDAKNTAKKSPL 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 652 N--KLMATLNSTSP-----------------------------------------------HFVRCIIPNETKSPGVIDS 682
Cdd:cd14905 516 SivKVLLSCGSNNPnnvnnpnnnsgggggggnsgggsgsggstyttysstnkainnsncdfHFIRCIKPNSKKTHLTFDV 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 683 HLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTILAPNAvpKGFvdaKNVSEKVIEA-IQLDA---NDFRFGHSKI 758
Cdd:cd14905 596 KSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQNQ--RNF---QNLFEKLKENdINIDSilpPPIQVGNTKI 670
|
...
gi 556079866 759 FFR 761
Cdd:cd14905 671 FLR 673
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
94-722 |
5.77e-61 |
|
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: 222.69 E-value: 5.77e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 94 SVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITGE 173
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 174 SGAGKTENTKKVIAYFAHVGatskkeevkkdtkKGNLED--QVVQTNPVLESFGNAKTVRNDNSSRFGKFIRIHFGPMGK 251
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLG-------------DGNRGAtgRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 252 LAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKIAGLKDKLLL**DVHEFHF----VSQGKTGIAGV-DDGEELVVT 326
Cdd:cd14882 149 MSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNRLKEYNLKAGRNYRYlripPEVPPSKLKYRrDDPEGNVER 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 327 ----DTAFDVLGFTDEEKENIYKVTAAVMHFGCLKFKQrpREEQAEADGTEEGERVAHLLGLNAADLYKNLLKPRIKVGT 402
Cdd:cd14882 229 ykefEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 403 EFVTQGRNITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQK---RQHFIGVLDIAGFEIFDHNSFEQMCINFTNEKL 479
Cdd:cd14882 307 SAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPRAvfgDKYSISIHDMFGFECFHRNRLEQLMVNTLNEQM 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 480 QQFFNHHMFVLEQEEYKREGIEWEFIDFGLDLQACIELIEKPMGLLSIMEEESMfpKATDQTF-LEKLKTNHlgkSPnFI 558
Cdd:cd14882 387 QYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDDASR--SCQDQNYiMDRIKEKH---SQ-FV 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 559 KPkppkpnQTEAHFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIFEDhpglgggddkggkggrKKGS 638
Cdd:cd14882 461 KK------HSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN----------------SQVR 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 639 GFQTVSGLYR----EQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDF 714
Cdd:cd14882 519 NMRTLAATFRatslELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEF 598
|
....*...
gi 556079866 715 KQRYTILA 722
Cdd:cd14882 599 LRRYQFLA 606
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
96-718 |
2.85e-53 |
|
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: 201.74 E-value: 2.85e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 96 LHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIY-KGRRRT---------EVPPHVFAVSDGAYMDMLANREN 165
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYnKSREQTplyekdtvnDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 166 QSMLITGESGAGKTENTKKVIAYFAHVGATSkkeEVKKDTKKGN-----LEDQVVQTNPVLESFGNAKTVRNDNSSRFGK 240
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDET---EPRPDSEGASgvlhpIGQQILHAFTILEAFGNAATRQNRNSSRFAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 241 FIRIHFGPMGKLAGADIETYLLEKARVISQQPAERSYHIFYQLMSG--KIAGLKDKLLL**DVHEFHFVSQGKTGIAGVD 318
Cdd:cd14893 161 MISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGvqHDPTLRDSLEMNKCVNEFVMLKQADPLATNFA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 319 -DGEELVVTDTAFDVLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGER---------------VAHLL 382
Cdd:cd14893 241 lDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGANSTTVSdaqscalkdpaqillAAKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 383 GLNAADLyKNLLKPR---IKVGTEFVTQGRNIT--QVTASVGALSKAIFDRLFKWLVKRVNETL----DTKQKRQHFIG- 452
Cdd:cd14893 321 EVEPVVL-DNYFRTRqffSKDGNKTVSSLKVVTvhQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNIVINs 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 453 ----VLDIAGFEIFD--HNSFEQMCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWE-------FIDFGLDLQACIELIE 519
Cdd:cd14893 400 qgvhVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAINFSFLEDESQQVEnrltvnsNVDITSEQEKCLQLFE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 520 -KPMGLLSIMEEESMFPKATDQTFLEKL-----KTNHLGKsPN----FIKPKPPKPNQTEAHFAIVHYAGTVPYNLTGWL 589
Cdd:cd14893 480 dKPFGIFDLLTENCKVRLPNDEDFVNKLfsgneAVGGLSR-PNmgadTTNEYLAPSKDWRLLFIVQHHCGKVTYNGKGLS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 590 EKNKDPLNDCVVDQFKKGSNLLLQAI--FEDHPGLGGGDDKGGKGGRKKGSGFQTVSGLYRE--------------QLNK 653
Cdd:cd14893 559 SKNMLSISSTCAAIMQSSKNAVLHAVgaAQMAAASSEKAAKQTEERGSTSSKFRKSASSAREsknitdsaatdvynQADA 638
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556079866 654 LMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRY 718
Cdd:cd14893 639 LLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY 703
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
115-244 |
9.46e-51 |
|
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: 177.54 E-value: 9.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 115 FCVAINPYKRFPIYTKRVV-EIYKGRRRTEVPPHVFAVSDGAYMDMLANRENQSMLITGESGAGKTENTKKVIAYFAHVG 193
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 556079866 194 ATSKKE-----EVKKDTKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSRFGKFIRI 244
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 ... |
94-759 |
4.54e-46 |
|
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: 179.26 E-value: 4.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 94 SVLHNLKERYYCHLIYTYSGLFCVAINPYKRFPIYTKRVVEIYKGRRRTE---VPPHVFAVSDGAYMDMLanRENQSMLI 170
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEdlsLNEYHVVHNALKNLNEL--KRNQSIII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 171 TGESGAGKTENTKKVIAYFAHVGATSKKEEVKKD-------------TKKGNLEDQVVQTNPVLESFGNAKTVRNDNSSR 237
Cdd:cd14938 80 SGESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNdqeednihneentDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 238 FGKFIRIHFGPmGKLAGADIETYLLEKARVISQQPAERSYHIFYQLMSGKiAGLKDKLLL**DVHEFHFVSQGKTGIAGV 317
Cdd:cd14938 160 FSKFCTIHIEN-EEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGS-SDKFKKMYFLKNIENYSMLNNEKGFEKFS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 318 DDGEELVVTDTAFDVLGFTDEEKENIYKVTAAVMHFGCLKFKQRPREEQAEADGTEEGERVAHLLGLNAAD--------- 388
Cdd:cd14938 238 DYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVKAFRKKSLLMGKNQCGQNINYETILSELEnsediglde 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 389 ------LYKNLLKPRIKVGTEFVT-----------QGRNITQVTASVGALSKAIFDRLFKWLVKRVNETLDTKQKRQ--- 448
Cdd:cd14938 318 nvknllLACKLLSFDIETFVKYFTtnyifndsiliKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNINint 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 449 HFIGVLDIAGFEIFDHNSFEQMCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWEFIDFGLD-LQACIELIEKPMGLLSI 527
Cdd:cd14938 398 NYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDnEPLYNLLVGPTEGSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 528 MEEESMFPKATDQTFLEKLKTNHLGKSPNFIKPKPPKPNQTEahFAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKG 607
Cdd:cd14938 478 LLENVSTKTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT--FVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 608 SNLLLQA------------IFEDHPGLGGGDDKGGKGGRKKGSGFQTVSgLYREQLNKLMATLNSTSPHFVRCIIPNETK 675
Cdd:cd14938 556 ENEYMRQfcmfynydnsgnIVEEKRRYSIQSALKLFKRRYDTKNQMAVS-LLRNNLTELEKLQETTFCHFIVCMKPNESK 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 676 SP-GVIDSHLVMHQLTCNGVLEGIRICRKGFPNRMIYPDFKQRYTIlaPNAvpkgfvDAKNVSEKVIEAIQLDANDFRFG 754
Cdd:cd14938 635 RElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDI--KNE------DLKEKVEALIKSYQISNYEWMIG 706
|
....*
gi 556079866 755 HSKIF 759
Cdd:cd14938 707 NNMIF 711
|
|
| RING-HC_dBre1-like |
cd16705 |
RING finger, HC subclass, found in Drosophila melanogaster Bre1 (dBre1) and similar proteins; ... |
2155-2223 |
2.65e-44 |
|
RING finger, HC subclass, found in Drosophila melanogaster Bre1 (dBre1) and similar proteins; dBre1 is the functional homolog of yeast Bre1, an E3 ubiquitin ligase required for the monoubiquitination of histone H2B and, indirectly, for H3K4 methylation. dBre1 acts as a nuclear component required for the expression of Notch target genes in Drosophila development. dBre1 contains a C3HC4-type RING-HC finger at its C-terminus.
Pssm-ID: 438365 [Multi-domain] Cd Length: 69 Bit Score: 155.12 E-value: 2.65e-44
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556079866 2155 DEVLMEEIKEYKEQLTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYETRQRKCPKCNAPFGTNDYHRLYL 2223
Cdd:cd16705 1 DEVLMEEIREYKEQLTCPSCKVKRKDAVLTKCFHVFCLDCLRTRYETRQRKCPKCNAAFGANDYHRLYL 69
|
|
| RING-HC_RNF20 |
cd16814 |
RING finger, HC subclass, found in RING finger protein 20 (RNF20); RNF20, also known as BRE1A ... |
2150-2223 |
1.25e-36 |
|
RING finger, HC subclass, found in RING finger protein 20 (RNF20); RNF20, also known as BRE1A or BRE1, is an E3 ubiquitin-protein ligase that forms a heterodimeric complex together with BRE1B, also known as RNF40, to facilitate the K120 monoubiquitination of histone H2B (H2Bub1), a DNA damage-induced histone modification that is crucial for recruitment of the chromatin remodeler SNF2h to DNA double-strand break (DSB) damage sites. It regulates the cell cycle and differentiation of neural precursor cells (NPCs), and links histone H2B ubiquitylation with inflammation and inflammation-associated cancer. Moreover, RNF20 promotes the polyubiquitination and proteasome-dependent degradation of transcription factor activator protein 2alpha (AP-2alpha), a negative regulator of adipogenesis by repressing the transcription of CCAAT/enhancer binding protein (C/EBPalpha) gene. Furthermore, RNF20 functions as an additional chromatin regulator that is necessary for mixed-lineage leukemia (MLL)-fusion-mediated leukemogenesis. It also inhibits TFIIS-facilitated transcriptional elongation to suppress pro-oncogenic gene expression. TFIIS is a factor capable of relieving stalled RNA polymerase II. RNF20 contains a C3HC4-type RING-HC finger at its C-terminus.
Pssm-ID: 438463 [Multi-domain] Cd Length: 75 Bit Score: 133.24 E-value: 1.25e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556079866 2150 LATNTDEVLMEEIKEYKEQLTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYETRQRKCPKCNAPFGTNDYHRLYL 2223
Cdd:cd16814 1 LVPNCDEILMEEIKDYKARLTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKCNAAFGANDFHRIYI 74
|
|
| RING-HC_RNF20-like |
cd16704 |
RING finger, HC subclass, found in RING finger protein RNF20, RNF40, and similar proteins; ... |
2159-2223 |
5.21e-36 |
|
RING finger, HC subclass, found in RING finger protein RNF20, RNF40, and similar proteins; RNF20, also known as BRE1A, and RNF40, also known as BRE1B, are E3 ubiquitin-protein ligases that work together to form a heterodimeric complex that facilitate the K120 monoubiquitination of histone H2B (H2Bub1), a DNA damage-induced histone modification that is crucial for recruitment of the chromatin remodeler SNF2h to DNA double-strand break (DSB) damage sites. RNF20 regulates the cell cycle and differentiation of neural precursor cells (NPCs) and links histone H2B ubiquitylation with inflammation and inflammation-associated cancer. RNF40, also known as 95 kDa retinoblastoma-associated protein (RBP95), was identified as a novel leucine zipper retinoblastoma protein (pRb)-associated protein that may function as a regulation factor in RNA polymerase II-mediated transcription and/or transcriptional processing. All subfamily members contain a C3HC4-type RING-HC finger at its C-terminus.
Pssm-ID: 438364 [Multi-domain] Cd Length: 65 Bit Score: 131.03 E-value: 5.21e-36
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556079866 2159 MEEIKEYKEQLTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYETRQRKCPKCNAPFGTNDYHRLYL 2223
Cdd:cd16704 1 LEEIKEYKARLTCPCCNTRKKDAVLTKCFHVFCFECLKTRYETRQRKCPKCNAAFGANDFHRIYI 65
|
|
| RING-HC_RNF40 |
cd16815 |
RING finger, HC subclass, found in RING finger protein 40 (RNF40); RNF40, also known as BRE1B ... |
2146-2223 |
2.67e-34 |
|
RING finger, HC subclass, found in RING finger protein 40 (RNF40); RNF40, also known as BRE1B or 95 kDa retinoblastoma-associated protein (RBP95), was identified as a novel leucine zipper retinoblastoma protein (pRb)-associated protein that may function as a regulation factor in RNA polymerase II-mediated transcription and/or transcriptional processing. RNF40 also functions as an E3 ubiquitin-protein ligase that forms a heterodimeric complex with BRE1B, also known as RNF40, to facilitate the K120 monoubiquitination of histone H2B (H2Bub1), a DNA damage-induced histone modification that is crucial for recruitment of the chromatin remodeler SNF2h to DNA double-strand break (DSB) damage sites. It cooperates with SUPT16H to induce dynamic changes in chromatin structure during DSB repair. RNF40 contains a C3HC4-type RING-HC finger at the C-terminus.
Pssm-ID: 438464 [Multi-domain] Cd Length: 78 Bit Score: 126.68 E-value: 2.67e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556079866 2146 KKFELATNTDEVLMEEIKEYKEQLTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYETRQRKCPKCNAPFGTNDYHRLYL 2223
Cdd:cd16815 1 KKVEVYADADEILQEEIKEYKARLTCPCCNTRKKDAVLTKCFHVFCFECVKTRYESRQRKCPKCNAAFGAHDFHRIYI 78
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
905-1723 |
8.67e-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: 133.26 E-value: 8.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 905 TQKGDLESQLADLNDRLSHEEDAHASLSQSKKKLEGEISG------LKKDIEDMELALQKAEqdkatkdhqIRNLNDEIQ 978
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKaerykeLKAELRELELALLVLR---------LEELREELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 979 HQDELINKLNKEKKHLQEASQKTSEDLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKRKVEGDLKLAQ 1058
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1059 EAVADLEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLArei 1138
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN--- 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1139 eelserleesggatsSQIELNKRREAELSKLRRDLEESNLQHEQAMSNLRKKhndtvaEMSEQIDQLNKHKAKVEKERAT 1218
Cdd:TIGR02168 400 ---------------NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK------ELQAELEELEEELEELQEELER 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1219 MSAEVSDLQSLLdhsnkaqANAEKQVKQLEVQLADAQFKVDEMNRTLNDLDG-GKKKLAVENSelQRQLEESESQVAQLN 1297
Cdd:TIGR02168 459 LEEALEELREEL-------EEAEQALDAAERELAQLQARLDSLERLQENLEGfSEGVKALLKN--QSGLSGILGVLSELI 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1298 KIKASLATQLEEA--KRMAD-----------------EEARERAAILGKYRNLEHDLDNLRESVEEEQEAKADFQRQLSK 1358
Cdd:TIGR02168 530 SVDEGYEAAIEAAlgGRLQAvvvenlnaakkaiaflkQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVK 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1359 ANAEAQLWRSkYESEGLARLEELEEA---KRKLHG----------------------------------KLQEAEEAMEQ 1401
Cdd:TIGR02168 610 FDPKLRKALS-YLLGGVLVVDDLDNAlelAKKLRPgyrivtldgdlvrpggvitggsaktnssilerrrEIEELEEKIEE 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1402 LNAKCSGLEKTKSHLQGELEDMSIEVDKANALASSLEKRQKSFDKVIAEWKAKVDDLAAELDASQKECRNYSTEVFKLRA 1481
Cdd:TIGR02168 689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1482 AYEESQEHYESVKRENKNLQDEVKDLMDQLGEGGRSVHELEKSRKRLEmekeelqaaleeaeaaleqeenkvlRAQLELS 1561
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN-------------------------EEAANLR 823
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1562 QVRQEIDRRIQEKEEEFENTRKNHQRALDSMqASLEAEAKGKAEALRlkkKLESDINELEIALDHANKANAEAQKNLKKY 1641
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDI-ESLAAEIEELEELIE---ELESELEALLNERASLEEALALLRSELEEL 899
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1642 QQNVKDLQGALEEEQRARDEAREQYASAERRCNAMHGELEESRQLLASSKNSHLRHIEQMEGEELLMQKKLRTEVIRLED 1721
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
..
gi 556079866 1722 AL 1723
Cdd:TIGR02168 980 KI 981
|
|
| RING-HC_Bre1-like |
cd16499 |
RING finger, HC subclass, found in yeast Bre1 and its homologs from eukaryotes; Bre1 is an E3 ... |
2163-2221 |
1.02e-27 |
|
RING finger, HC subclass, found in yeast Bre1 and its homologs from eukaryotes; Bre1 is an E3 ubiquitin-protein ligase that catalyzes monoubiquitination of histone H2B in concert with the E2 ubiquitin-conjugating enzyme, Rad6. The Rad6-Bre1-mediated histone H2B ubiquitylation modulates the formation of double-strand breaks (DSBs) during meiosis in yeast. it is also required, indirectly, for the methylation of histone 3 on lysine 4 (H3K4) and 79. RNF20, also known as BRE1A and RNF40, also known as BRE1B, are the mammalian homologs of Bre1. They work together to form a heterodimeric Bre1 complex that facilitate the K120 monoubiquitination of histone H2B (H2Bub1), a DNA damage-induced histone modification that is crucial for recruitment of the chromatin remodeler SNF2h to DNA double-strand break (DSB) damage sites. Moreover, the Bre1 complex acts as a tumor suppressor, augmenting expression of select tumor suppressor genes and suppressing select oncogenes. Deficiency in the mammalian histone H2B ubiquitin ligase Bre1 leads to replication stress and chromosomal instability. All subfamily members contain a C3HC4-type RING-HC finger at its C-terminus.
Pssm-ID: 438162 [Multi-domain] Cd Length: 59 Bit Score: 107.26 E-value: 1.02e-27
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 556079866 2163 KEYKEQLTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYETRQRKCPKCNAPFGTNDYHRL 2221
Cdd:cd16499 1 KDLRELLKCSVCNDRFKDVIITKCGHVFCNECVQKRLETRQRKCPGCGKAFGANDVQRI 59
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
839-1620 |
9.55e-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: 116.69 E-value: 9.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 839 RVEDELKAMEEKL-------KKTEEALAKEEKLRKELEEHNVKVLQEKNDlflQLEAERMGAGDVEERLNKALTQKGDLE 911
Cdd:TIGR02168 190 RLEDILNELERQLkslerqaEKAERYKELKAELRELELALLVLRLEELRE---ELEELQEELKEAEEELEELTAELQELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 912 SQLADLndrlsheEDAHASLSQSKKKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLNDEIQHQDELINKLNKEK 991
Cdd:TIGR02168 267 EKLEEL-------RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 992 KHLQEASQKTSEDLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKRKVEGDLKLAQEAVADLEKNKKEM 1071
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1072 EQNL-----QRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADL-AREIEELSERL 1145
Cdd:TIGR02168 420 QQEIeellkKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLqARLDSLERLQE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1146 EESG-GATSSQIELNKRREAELSKLRRDLEESNLQHEQAMSN-LRKKHNDTVAEMSEQIDQLNKHKAKVEKERATMSAEV 1223
Cdd:TIGR02168 500 NLEGfSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAaLGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLD 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1224 SDLQSLLDHSNKAQANAEKQVKQLEVQLADAQfkvDEMNRTLNDLDGGkkkLAVENS-----ELQRQLEESESQVAQ--- 1295
Cdd:TIGR02168 580 SIKGTEIQGNDREILKNIEGFLGVAKDLVKFD---PKLRKALSYLLGG---VLVVDDldnalELAKKLRPGYRIVTLdgd 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1296 -------LNKIKASLATQLEEAKRMADEEARERAAILGKYRNLEHDLDNLRESVEEEQEAKADFQRQLSKANAEAQLWRS 1368
Cdd:TIGR02168 654 lvrpggvITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRK 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1369 KYESEGlARLEELEEAKRKLHGKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEVDKANALASSLEKRQKSFDKVI 1448
Cdd:TIGR02168 734 DLARLE-AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1449 AEWKAKVDDLAAELDASQKECRNYSTEVFKLRAAYEESQEHYESVKRENKNLQDEVKDLMDQLGEGGRSVHELEKSRKRL 1528
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1529 EMEKEELQAALEEAEAALEQEENKVLRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDsMQASLEAEAKGKAEALR 1608
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE-EAEALENKIEDDEEEAR 971
|
810
....*....|...
gi 556079866 1609 LK-KKLESDINEL 1620
Cdd:TIGR02168 972 RRlKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
999-1723 |
4.81e-25 |
|
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: 114.39 E-value: 4.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 999 QKTSEDLQATEDKVNHLNKVKAKLEQTLDELEDslEREKKAR-GDIEKNKRKVEGDLKLAQeaVADLEKNKKEMEQNLQR 1077
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLERLRR--EREKAERyQALLKEKREYEGYELLKE--KEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1078 KEKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEEleaeRQARAKAEKqradlareieelserleesgGATSSQIE 1157
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE----EQLRVKEKI--------------------GELEAEIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1158 LNKRREAELSKLRRDLEESNLQHEQAMSNLRKKHndtvAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDHSNKAQ 1237
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERLAKLEAEIDKLLAEI----EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1238 ANAEKQVKQLEVQLADAQFKVDEMNRTLNDLDGGKKKLAVENSELQRQLEESESQVAQLNKIKASLATQLEEAKRMADEE 1317
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1318 ARERAAILGKYRNLEHDLDnlreSVEEEQEAKadfQRQLSKANAEAQLWRSkYESEGLARLEELEEAKRKLHGKLQE--- 1394
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYD----RVEKELSKL---QRELAEAEAQARASEE-RVRGGRAVEEVLKASIQGVHGTVAQlgs 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1395 ---------------------------AEEAMEQLNAKCSG------LEKTKSH-------------------------- 1415
Cdd:TIGR02169 533 vgeryataievaagnrlnnvvveddavAKEAIELLKRRKAGratflpLNKMRDErrdlsilsedgvigfavdlvefdpky 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1416 -------------------------------LQGELEDMSIEVDKANALASSLEKRQKSFDKVIAEWKAKVDDLAAELDA 1464
Cdd:TIGR02169 613 epafkyvfgdtlvvedieaarrlmgkyrmvtLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSS 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1465 SQKECRNYSTEVFKLRAAYEESQEHYESVKRENKNLQDEVKDLMDQLGEGGRSVHELEKSRKRLEMEKEELQAALEEAEA 1544
Cdd:TIGR02169 693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1545 aleqeenKVLRAQLELSQVRQEIDR-RIQEKEEEFENTRKNHQR---ALDSMQASLEAEAKGKAEALRLKKKLESDINEL 1620
Cdd:TIGR02169 773 -------DLHKLEEALNDLEARLSHsRIPEIQAELSKLEEEVSRieaRLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1621 EI-------ALDHANKANAEAQKNLKKYQQNVKDLQGALEEEQRARDEAREQYASAERRCNAMHGELEESRQLL------ 1687
Cdd:TIGR02169 846 KEqiksiekEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLselkak 925
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 556079866 1688 ASSKNSHLRHIEQMEGE------ELLMQKKLRTEVIRLEDAL 1723
Cdd:TIGR02169 926 LEALEEELSEIEDPKGEdeeipeEELSLEDVQAELQRVEEEI 967
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
214-702 |
9.35e-22 |
|
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: 103.28 E-value: 9.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 214 VVQTNPVLESFGNAKTVRNDNSSRFGKF--IRIHFGPMG---KLAGADIETYLLEKARVISQQPAER------SYHIFYQ 282
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERGRESgdqnelNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 283 LmsgkIAGLKDKLLL**DVHEFH---------------------FVSQGKTGIAGVDDGEELVvtdTAFDVLGFTDEEKE 341
Cdd:cd14894 329 M----VAGVNAFPFMRLLAKELHldgidcsaltylgrsdhklagFVSKEDTWKKDVERWQQVI---DGLDELNVSPDEQK 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 342 NIYKVTAAVMHFGCLKFKQRPREEQAEADGT---EEGERVAHLLGLNAADLYKNLLKPRiKVGTEFVTQGRNIT----QV 414
Cdd:cd14894 402 TIFKVLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTK-SVSLQSTSETFEVTlekgQV 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 415 TASVGALSKAIFDRLFKWLVKRVNET-----LDTKQKRQH------------FIGVLDIAGFEIFDHNSFEQMCINFTNE 477
Cdd:cd14894 481 NHVRDTLARLLYQLAFNYVVFVMNEAtkmsaLSTDGNKHQmdsnasapeavsLLKIVDVFGFEDLTHNSLDQLCINYLSE 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 478 KLqqfFNHHMFVLEQEEYKREGIewefidFGLDLQACIELI-EKPMGLLSIMEEESMFPKATDQTFLEKLKTNHLgkspn 556
Cdd:cd14894 561 KL---YAREEQVIAVAYSSRPHL------TARDSEKDVLFIyEHPLGVFASLEELTILHQSENMNAQQEEKRNKL----- 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 557 FIK----------PKPPKP-NQTEAH---------FAIVHYAGTVPYNLTGWLEKNKDPLNDCVVDQFKKGSNLLLQAIF 616
Cdd:cd14894 627 FVRniydrnssrlPEPPRVlSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRML 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 617 EDHPGLGGGDDKGGKGGRKKGSGF---QTVSGLYREQLNKLMATLNSTSPHFVRCIIPNETKSPGVIDSHLVMHQLTCNG 693
Cdd:cd14894 707 NESSQLGWSPNTNRSMLGSAESRLsgtKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQR 786
|
....*....
gi 556079866 694 VLEGIRICR 702
Cdd:cd14894 787 LIRQMEICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
841-1592 |
9.69e-22 |
|
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: 103.60 E-value: 9.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 841 EDELKAMEEKL--KKTEEALAKEEKLRKELEEHNVKVLQEKNDLFLQLEAERMGAGD-----VEERLNKALTQKGDLESQ 913
Cdd:TIGR02168 259 TAELQELEEKLeeLRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLErqleeLEAQLEELESKLDELAEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 914 LADLNDRLSHEEDAHASLSQSKKKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLNDEIQHQDELINKLNKEKKH 993
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 994 LQE-----ASQKTSEDLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKRKVEGDLKLAQEAVADLE--- 1065
Cdd:TIGR02168 419 LQQeieelLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLErlq 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1066 -------KNKKEMEQNLQRKEKEMASLAAKLE----DEQALVAKLQKQikeLQARIEELEEELEAERQARAKAEKQRADL 1134
Cdd:TIGR02168 499 enlegfsEGVKALLKNQSGLSGILGVLSELISvdegYEAAIEAALGGR---LQAVVVENLNAAKKAIAFLKQNELGRVTF 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1135 AREIEELSERLEESGGATSSQIELNKRREAELSKLRRDLE---ESNLQH-------EQAMsNLRKKHNDTVAEMSEQIDQ 1204
Cdd:TIGR02168 576 LPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalSYLLGGvlvvddlDNAL-ELAKKLRPGYRIVTLDGDL 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1205 LNKHKA-------------KVEKERATMSAEVSDLQSLLDHSNKAQANAEKQVKQLEVQLADAQFKVDEMNRTLNDLDGG 1271
Cdd:TIGR02168 655 VRPGGVitggsaktnssilERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1272 KKKLAVENSELQRQLEESESQVAQLNKIKASLATQLEEAKRMADEEARERAailgkyrNLEHDLDNLRESVEEEQEAKAD 1351
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE-------ELEAQIEQLKEELKALREALDE 807
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1352 FQRQLSKANAEAQLWRSKYESEgLARLEELEEAKRKLHGKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEVDKAN 1431
Cdd:TIGR02168 808 LRAELTLLNEEAANLRERLESL-ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1432 ALASSLEKRQKSFDKVIAEWKAKVDDLAAELDASQKECRNYSTEVFKLRA---------------AYEESQEHYESVKRE 1496
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVridnlqerlseeyslTLEEAEALENKIEDD 966
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1497 NKNLQDEVKDLMDQLGEGGR----SVHELEKSRKRLEmekeelqaaleeaeaALEQEENKVLRAQLELSQVRQEIDRRIQ 1572
Cdd:TIGR02168 967 EEEARRRLKRLENKIKELGPvnlaAIEEYEELKERYD---------------FLTAQKEDLTEAKETLEEAIEEIDREAR 1031
|
810 820
....*....|....*....|.
gi 556079866 1573 EK-EEEFENTRKNHQRALDSM 1592
Cdd:TIGR02168 1032 ERfKDTFDQVNENFQRVFPKL 1052
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
936-1509 |
1.09e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.09 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 936 KKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLNDEIQHQDELINKLNKEKKHLQEASQKTSEDLQATEDKVNHL 1015
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1016 NKVKAKLEQTLDELEDSLEREKKARGDIEKNKRKVEGDLKLAQEAVADLEKNKKEMEQNLQRKEKEMASLAAKLEDEQAL 1095
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1096 VAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLAREIEELSERLEesggATSSQIELNKRREAELSKLRRDLEE 1175
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE----EAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1176 SNLQHEQAMSNLRKKHNDTVAEMSEQIDQLNKH--------KAKVEKERATMSAEVSDLQSLLDHSNKAQANAEKQVKQL 1247
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYegflegvkAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQN 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1248 EVQLADAQFKvdEMNRTLNDLDGGKKKLAVENSELQRQLEESESQVAQLNKIKASLATQLEEAKRMADEEARERAAILGK 1327
Cdd:COG1196 551 IVVEDDEVAA--AAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLV 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1328 YRNLEHDLDNLRESVEEEQEAKADfQRQLSKANAEAQLWRSKYESEGLARLEELEEAKRKLHGKLQEAEEAMEQLNAKCS 1407
Cdd:COG1196 629 AARLEAALRRAVTLAGRLREVTLE-GEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1408 GLEKTKSHLQGELEDMSIEVDKANALASSLEKRQKSFDKVIAEWKAKVDDLAAELDASQKECRNYSTEVFKL-----RA- 1481
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnlLAi 787
|
570 580
....*....|....*....|....*....
gi 556079866 1482 -AYEESQEHYESVKRENKNLQDEVKDLMD 1509
Cdd:COG1196 788 eEYEELEERYDFLSEQREDLEEARETLEE 816
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
989-1654 |
1.42e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 102.71 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 989 KEKKHlqEASQKtsedLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKARgDIEKNKRKVEGDLKL-----AQEAVAD 1063
Cdd:COG1196 171 KERKE--EAERK----LEATEENLERLEDILGELERQLEPLERQAEKAERYR-ELKEELKELEAELLLlklreLEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1064 LEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLAREIEELSE 1143
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1144 RLEESGGATSSQIELNKRREAELSKLRRDLEESNLQHEQAMSNLRKKHNDtVAEMSEQIDQLNKHKAKVEKERATMSAEV 1223
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE-LAEAEEELEELAEELLEALRAAAELAAQL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1224 SDLQSLLDHSNKAQANAEKQVKQLEVQLADAQFKVDEMNRTLndldggkKKLAVENSELQRQLEESESQVAQLNKIKASL 1303
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL-------EEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1304 ATQLEEAKRMADEEARERAAILGKYRNLEHDLDNLRESVEEEQeakadfQRQLSKANAEAQLWRSKYESEGLARLEELee 1383
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG------LRGLAGAVAVLIGVEAAYEAALEAALAAA-- 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1384 AKRKLHGKLQEAEEAMEQLNAKCSG------LEKTKSHLQGELEDMSIEVDKANALASSLEKRQKSFDKVIAEWKAKVDD 1457
Cdd:COG1196 548 LQNIVVEDDEVAAAAIEYLKAAKAGratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1458 LAAELDASQKECRNYSTEVFKLRAAYEESQEHYESVKRENKNLQDEVKDLMDQLGEGGRSVHELEKSRKRLEMEKEELQA 1537
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1538 ALEEAEAALEQEENKVLRAQLELSQVRQEIDRRIQEKEEEFENtrknhqrALDSMQASLEAEAKGKAEALRLKKKLES-- 1615
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE-------EALEELPEPPDLEELERELERLEREIEAlg 780
|
650 660 670
....*....|....*....|....*....|....*....
gi 556079866 1616 DINELeiALDHAnkanAEAQKNLKKYQQNVKDLQGALEE 1654
Cdd:COG1196 781 PVNLL--AIEEY----EELEERYDFLSEQREDLEEARET 813
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1019-1672 |
7.54e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.40 E-value: 7.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1019 KAKLEQTLDELEDSLEREKKARGDIEKNKRKvegdlkLAQEAvadlEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAK 1098
Cdd:COG1196 174 KEEAERKLEATEENLERLEDILGELERQLEP------LERQA----EKAERYRELKEELKELEAELLLLKLRELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1099 LQKQIKELQARIEELEEELeaeRQARAKAEKQRADLAREIEELSERLEESGGATSSQIELNKRREAELSKLRRDLEESnl 1178
Cdd:COG1196 244 LEAELEELEAELEELEAEL---AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL-- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1179 qheqamsnlrkkhndtvAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDHSNKAQANAEKQVKQLEVQLADAQFKV 1258
Cdd:COG1196 319 -----------------EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1259 DEMNRTLNDLDGGKKKLAVENSELQRQLEESESQVAQLNKIKASLATQLEEAKRMADEEARERAAILGKYRNLEHDLDNL 1338
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1339 RESVEEEQEAKADFQRQLSKANAEAQlwrskyesEGLARLEELEEAKRKLHGKLQEAEEAmeQLNAKCSGLEKTKSHLQG 1418
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELA--------EAAARLLLLLEAEADYEGFLEGVKAA--LLLAGLRGLAGAVAVLIG 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1419 --ELEDMSIEVDKANALASSLEKRQKSFDKVIAEWKAKVDDLAAELDASQKEcrnySTEVFKLRAAYEESQEHYESVKRE 1496
Cdd:COG1196 532 veAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIR----ARAALAAALARGAIGAAVDLVASD 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1497 NKNLQDEVKDLMDQLGEGGRSVHELEKSRKRLEMEKEELQAALEEAEAALEQEENKVLRAQLELSQVRQEIDRRIQEKEE 1576
Cdd:COG1196 608 LREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1577 EfentrknhQRALDSMQASLEAEAKGKAEALRLKKKLESDINELEIALDHANKANAEAQKNLKKYQQNVKDLQGALEEEQ 1656
Cdd:COG1196 688 L--------AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP 759
|
650
....*....|....*.
gi 556079866 1657 RARDEAREQYASAERR 1672
Cdd:COG1196 760 PDLEELERELERLERE 775
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1160-1741 |
3.08e-20 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 98.59 E-value: 3.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1160 KRREAELSKLRRDLEESNLQHEQAMSNLRKKHndtvaemsEQIDQLNKHKAKVEKERA-------TMSAEVSDLQSLLDH 1232
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELE--------EKLEELRLEVSELEEEIEelqkelyALANEISRLEQQKQI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1233 SNKAQANAEKQVKQLEVQLADAQFKVDEMNRTLNDLDGGKKKLAVENSELQRQLEESESQVAQLNKIKASLATQLEEAKR 1312
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1313 MADEEARERAAILGKYRNLEHDLDNLRESVEEEQEAKADFQRQLSKANAE---AQLWRSKYESEGL--------ARLEEL 1381
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKelqAELEELEEELEELqeelerleEALEEL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1382 EEAKRKLHGKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEVDKANAL---------------------------- 1433
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgilgvlselisvdegyeaaieaalggr 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1434 ---------------------------------------------------------ASSLEKRQKSFDKVIAEWKAK-- 1454
Cdd:TIGR02168 547 lqavvvenlnaakkaiaflkqnelgrvtflpldsikgteiqgndreilkniegflgvAKDLVKFDPKLRKALSYLLGGvl 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1455 -VDDLAAELD-------------------------------------ASQKECRNYSTEVFKLRAAYEESQEHYESVKRE 1496
Cdd:TIGR02168 627 vVDDLDNALElakklrpgyrivtldgdlvrpggvitggsaktnssilERRREIEELEEKIEELEEKIAELEKALAELRKE 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1497 NKNLQDEVKDLMDQLGEGGRSVHELEKSRKRLEMEKEELQAALEEAEAALEQEENKVLRAQLELSQVRQEIDRRIQEKE- 1575
Cdd:TIGR02168 707 LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEe 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1576 -----EEFENTRKNHQRALDSMQASLEAEAKGKAEALRLKKKLESDINELEIALDHANKANAEAQKNLKKYQQNVKDLQG 1650
Cdd:TIGR02168 787 leaqiEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE 866
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1651 ALEEEQRARDEAREQYASAERRCNamhgELEESRQLLASSKNSHLRHIEQMEGEELLMQKKLRTEVIRLEDALVQVRKEY 1730
Cdd:TIGR02168 867 LIEELESELEALLNERASLEEALA----LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
730
....*....|.
gi 556079866 1731 EMLRIEFEQNL 1741
Cdd:TIGR02168 943 ERLSEEYSLTL 953
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
837-1516 |
5.38e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 98.29 E-value: 5.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 837 AVRVEDELKAME----EKLKKTEEAlakeEKLRKELEEHNVKVLQEKNDLFLQLEAERMGAgdVEERLNKALTQKGDLES 912
Cdd:PTZ00121 1175 AKKAEAARKAEEvrkaEELRKAEDA----RKAEAARKAEEERKAEEARKAEDAKKAEAVKK--AEEAKKDAEEAKKAEEE 1248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 913 QLADLNDRLSHEEDAHASLSQSKKKLEGeisglKKDIEDMELALQKAEQDKATKDHQIRNLnDEIQHQDELINKLNKEKK 992
Cdd:PTZ00121 1249 RNNEEIRKFEEARMAHFARRQAAIKAEE-----ARKADELKKAEEKKKADEAKKAEEKKKA-DEAKKKAEEAKKADEAKK 1322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 993 HLQEASQKTSEDLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKRKVEGDLKLAQEAVADLEKNKKEME 1072
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE 1402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1073 QNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARieeleeeleAERQARAKAEKQRADLAREIEELSERLEESGGAT 1152
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKK---------AEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1153 SSQIELNKRREAElsKLRRDLEESNLQHEQAmsnlRKKhndtvAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDH 1232
Cdd:PTZ00121 1474 EAKKKAEEAKKAD--EAKKKAEEAKKKADEA----KKA-----AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA 1542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1233 SNKAQANAEKQVKqlEVQLADAQFKVDEMNRTLNDLDGGKKKLAVENSELQRQLEESESQVAQLNKIKASLATQLEEAKR 1312
Cdd:PTZ00121 1543 EEKKKADELKKAE--ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI 1620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1313 MADE---EARERAAILGKYRNLEHDLDNLRESVEEEQEAKADFQRQLSKANAEaqlwrsKYESEGLARLEELEEAKRKLH 1389
Cdd:PTZ00121 1621 KAEElkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED------KKKAEEAKKAEEDEKKAAEAL 1694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1390 GKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEVDKANALASSlEKRQKSFDKVIAEWKAKVDDLAAELDASQKEC 1469
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE-DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEI 1773
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 556079866 1470 RNYSTEVFKlraayEESQEHYESVKRENKNLQDEVKDLMDQLGEGGR 1516
Cdd:PTZ00121 1774 RKEKEAVIE-----EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGK 1815
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
974-1739 |
5.75e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 98.29 E-value: 5.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 974 NDEIQHQDELINkLNKEKKHLQEASQKTS----EDLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKRK 1049
Cdd:PTZ00121 1038 NDDVLKEKDIID-EDIDGNHEGKAEAKAHvgqdEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARK 1116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1050 VEGDLKLAQEAVADLEKNKKE----MEQNLQRKEKEMASLAAKLEDEQalvaKLQKQIKELQARIEELEEELEAERQA-- 1123
Cdd:PTZ00121 1117 AEEAKKKAEDARKAEEARKAEdarkAEEARKAEDAKRVEIARKAEDAR----KAEEARKAEDAKKAEAARKAEEVRKAee 1192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1124 -RAKAEKQRADLAREIEELSERLEESGGATSSQIELNKR--------REAELSKLRRDLEESNLQHEQAMSNLRKKHNDT 1194
Cdd:PTZ00121 1193 lRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKaeeakkdaEEAKKAEEERNNEEIRKFEEARMAHFARRQAAI 1272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1195 VAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLldhsnKAQANAEKQVKQLEVQLADAQFKVDEMnrtlndldggKKK 1274
Cdd:PTZ00121 1273 KAEEARKADELKKAEEKKKADEAKKAEEKKKADEA-----KKKAEEAKKADEAKKKAEEAKKKADAA----------KKK 1337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1275 lavenSELQRQLEESESQVAQLNKIKASLATQLEEAKRMADEEARERAAILGKYRNLEHDLDNLRESVEEEQEaKADFQR 1354
Cdd:PTZ00121 1338 -----AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKK-KADELK 1411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1355 QLSKANAEAQLWRSKYESEGLArleelEEAKRKlhgklqeAEEAMEQLNAKCSGLEKTKSHlqgeledmsievdkaNALA 1434
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKA-----DEAKKK-------AEEAKKADEAKKKAEEAKKAE---------------EAKK 1464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1435 SSLEKRQKSFDKVIAEWKAKVDDLAAELDASQKECRnystevfKLRAAYEESQEHYESVKRENKNLQDEVKDlmdqlGEG 1514
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAD-------EAKKAAEAKKKADEAKKAEEAKKADEAKK-----AEE 1532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1515 GRSVHELEKSRKRLEMEKEELQAALEEAEAALEQEENKVLRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQA 1594
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA 1612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1595 SLEAEAKGKAEALRLKKKLESDINELEIALDHANKANAEAQKNLKKYQQNVKDLQGALEEEQRARDEAREQYASAERRCN 1674
Cdd:PTZ00121 1613 KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556079866 1675 AMHGELEESRQL--LASSKNSHLRHIEQMEGEEllMQKKLRTEVIRLEDAlvQVRKEYEMLRIEFEQ 1739
Cdd:PTZ00121 1693 ALKKEAEEAKKAeeLKKKEAEEKKKAEELKKAE--EENKIKAEEAKKEAE--EDKKKAEEAKKDEEE 1755
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
936-1654 |
7.08e-20 |
|
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: 97.01 E-value: 7.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 936 KKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLNDEI----QHQDELINKLNKEKKHLQeasqKTSEDLQATEDK 1011
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIkileQQIKDLNDKLKKNKDKIN----KLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1012 VNHLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKRKVEGDLKLAQEAVADLEKNKKEMEQNLQRKEKEMASLAAKLED 1091
Cdd:TIGR04523 112 IKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1092 EQALVAKLQKQIKELQARIeeleeeleaerqarakaekqradlareieelserleesggatssqiELNKRREAELSklrr 1171
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKKI----------------------------------------------QKNKSLESQIS---- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1172 DLEESNLQHEQAMSNLRKKHNDTVAEMSEQIDQLNKHKAKVEKERATMSaevsDLQSLLDHSNKAQANAEKQVKQLEVQL 1251
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS----EKQKELEQNNKKIKELEKQLNQLKSEI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1252 ADAQfkvdemNRTLNDLDggkKKLAVENSELQRQLEESESQVAQLNKIKASLATQLEeakrmadeeareraailgkyrNL 1331
Cdd:TIGR04523 298 SDLN------NQKEQDWN---KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS---------------------QL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1332 EHDLDNLRESVEEEQEAKADFQRQLSKANAEAQlwrSKYESeglarLEELEEAKRKLHGKLQEAEEAMEQLNAKCSGLEK 1411
Cdd:TIGR04523 348 KKELTNSESENSEKQRELEEKQNEIEKLKKENQ---SYKQE-----IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQ 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1412 TKSHLQGELEDMSIEVDKANALASSLEKRQKSFDKVIAEWKAKVDDLAAELDASQKECRNYSTEVFKLRAAYEESQEHYE 1491
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELK 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1492 SVKRENKNLQDEVKDLMDQLGEGGRSVHELEKSRKRLEMEkeelqaaleeaeaaLEQEENKVLRAQLELSqvRQEIDRRI 1571
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESK--------------ISDLEDELNKDDFELK--KENLEKEI 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1572 QEKEEEFENTrKNHQRALDSMQASLEAEAKGKAEAlrlKKKLESDINELEIALDHANKANAEAQKNLKKYQQNVKDLQGA 1651
Cdd:TIGR04523 564 DEKNKEIEEL-KQTQKSLKKKQEEKQELIDQKEKE---KKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSK 639
|
...
gi 556079866 1652 LEE 1654
Cdd:TIGR04523 640 KNK 642
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
764-1578 |
1.46e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 96.29 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 764 VLGRLEEMRdERLSKIMTMIQaavrwyICKKHFQKLKEQRVALLVIQRNLRKFLQLRNWLwwKLYSKVKPLLSAVRVEDE 843
Cdd:TIGR02169 175 ALEELEEVE-ENIERLDLIID------EKRQQLERLRREREKAERYQALLKEKREYEGYE--LLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 844 LKAMEEKLKKTEEALAKeeklrkeleehNVKVLQEKNDLFLQLEAERMGAGdvEERLNKALTQKGDLESQLADLNDRLSH 923
Cdd:TIGR02169 246 LASLEEELEKLTEEISE-----------LEKRLEEIEQLLEELNKKIKDLG--EEEQLRVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 924 EEDAHASLSQSKKKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLNDEIqhqDELINKLNKEKKHLQEASQKTS- 1002
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL---EDLRAELEEVDKEFAETRDELKd 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1003 --EDLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKRKVEGDLKLAQEAVADLEKNKKEMEQNLQRKEK 1080
Cdd:TIGR02169 390 yrEKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1081 EMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQR-------ADLAREIEELSERLEESGGA-- 1151
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgtvAQLGSVGERYATAIEVAAGNrl 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1152 ----------TSSQIELNKRREA------ELSKLRRDLEESNLQHE---------------QAMSNLRKKHNDTVaeMSE 1200
Cdd:TIGR02169 550 nnvvveddavAKEAIELLKRRKAgratflPLNKMRDERRDLSILSEdgvigfavdlvefdpKYEPAFKYVFGDTL--VVE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1201 QIDQLNKHKAKVEkeRATMSAEVSDLQSLLDHSNKAQANAEKQVKQLEVQLADAQFKVDEMNRTLNDL-------DGGKK 1273
Cdd:TIGR02169 628 DIEAARRLMGKYR--MVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLqselrriENRLD 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1274 KLAVENSELQRQLEESESQVAQLNKIKASLATQLEEAKRMADEEARERAAILGKYRNLEHDLDNLRESVEEEQEAKADFQ 1353
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1354 RQLS-----KANAEAQLWRsKYESEGLARLEELEEAKRKLHGKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEVD 1428
Cdd:TIGR02169 786 ARLShsripEIQAELSKLE-EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1429 KANALASSLEKRQKSFDKVIAEWKAKVDDLAAELDASQKECRNYSTEVFKLRAAYEESQEHYESVKRENKNLQDEVKDLM 1508
Cdd:TIGR02169 865 ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556079866 1509 DQLGEGgRSVHELEKSRKRLEME-------KEELQAALEEAEAALEQEENKVLRAQLELSQVRQEIDRRIQEKEEEF 1578
Cdd:TIGR02169 945 EIPEEE-LSLEDVQAELQRVEEEiralepvNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVF 1020
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
840-1602 |
3.93e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 95.13 E-value: 3.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 840 VEDELKAMEEKLKKT-EEALAKEEKLRKELEEHNVKVLQEKNDLFLQLEAermgagdVEERLNKALTQKGDLESQLADLN 918
Cdd:TIGR02169 192 IIDEKRQQLERLRRErEKAERYQALLKEKREYEGYELLKEKEALERQKEA-------IERQLASLEEELEKLTEEISELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 919 DRLSHEEDAHASLS-QSKKKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLNDEIQHQDELINKLNKEKKHLQEA 997
Cdd:TIGR02169 265 KRLEEIEQLLEELNkKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 998 SQKTSEDLQATEDKVNHLNKVKAKLEQTLDELEDSL----EREKKARGDIEKNKRKVE---GDLKLAQEAVADLEKNKKE 1070
Cdd:TIGR02169 345 IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFaetrDELKDYREKLEKLKREINelkRELDRLQEELQRLSEELAD 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1071 MEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRAD----LAREIEELSERLE 1146
Cdd:TIGR02169 425 LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKlqreLAEAEAQARASEE 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1147 ESGGATSSQIELNKRREA---ELSKLRRDLEESNLQHEQAMSNLRKK---HNDTVAEmsEQIDQLNKHKA---------- 1210
Cdd:TIGR02169 505 RVRGGRAVEEVLKASIQGvhgTVAQLGSVGERYATAIEVAAGNRLNNvvvEDDAVAK--EAIELLKRRKAgratflplnk 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1211 ----KVEKERATMSAEVSDLQSLLDHSNKAQaNAEKQVKQLEVQLADAQFKVDEMNR-TLNDLDG----------GKKKL 1275
Cdd:TIGR02169 583 mrdeRRDLSILSEDGVIGFAVDLVEFDPKYE-PAFKYVFGDTLVVEDIEAARRLMGKyRMVTLEGelfeksgamtGGSRA 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1276 AVENSELQRQLEESESQVAQ----LNKIKASLATQLEEAKRMADEEARERAAILGKYRNLEHDLDNL---RESVEEEQEA 1348
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRErlegLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLeqeEEKLKERLEE 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1349 KADFQRQLSKANAEAQLWRSKYEseglARLEELEEAKRKLHGKLQE-----AEEAMEQLNAKCSGLEKTKSHLQGELEDM 1423
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELE----ARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRIEARLREI 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1424 SIEVDKANALASSLEKRQKSFDKVIAEWKAKVDDLAAELDASQKECRNYSTEVFKLRAAYEESQEHYESVKRENKNLQDE 1503
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1504 VKDLMDQLGEGGRSVHELEKSRKRLEmEKEELQAALEEAEAALEQEENKVLRAQLELSQV---RQEIDRRIQEKE----- 1575
Cdd:TIGR02169 898 LRELERKIEELEAQIEKKRKRLSELK-AKLEALEEELSEIEDPKGEDEEIPEEELSLEDVqaeLQRVEEEIRALEpvnml 976
|
810 820
....*....|....*....|....*....
gi 556079866 1576 --EEFENTRKNhQRALDSMQASLEAEAKG 1602
Cdd:TIGR02169 977 aiQEYEEVLKR-LDELKEKRAKLEEERKA 1004
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
834-1682 |
5.81e-19 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 94.65 E-value: 5.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 834 LLSAVRVEDELKAMEEKLKKTEEALAKEEKL--RKELEEHNVKVLQEKNDLFLQLEAERMGAGDVEERLnKALTQKGDLE 911
Cdd:pfam02463 158 IEEEAAGSRLKRKKKEALKKLIEETENLAELiiDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYL-LYLDYLKLNE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 912 SQLADLNDRLSHEEDAHASLSQSKKKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLNDEIQHQDELINKLNKEK 991
Cdd:pfam02463 237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 992 KHLQEASQKTSEDLQATEDKVNHLNKVKakleqtldeleDSLEREKKARGDIEKNKRKVEGDLKLAQEAVADLEKNKKEM 1071
Cdd:pfam02463 317 KESEKEKKKAEKELKKEKEEIEELEKEL-----------KELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESER 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1072 EQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLAREIEELSERLEESGGA 1151
Cdd:pfam02463 386 LSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1152 TSSQIELNKRREAELSKLRRDLEESNLQHEQAMSNLRKKHNDTVAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQslld 1231
Cdd:pfam02463 466 ELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENY---- 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1232 hSNKAQANAEKQVKQLEVQLADAQFKVDEMNRTLNDLDGGKKKLAVENSELQRQLEesESQVAQLNKIKASLATQLEEAK 1311
Cdd:pfam02463 542 -KVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV--LEIDPILNLAQLDKATLEADED 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1312 RMADEEARERAAILGKYRNLEHDLDNLRESVEEEQEAKADFQRQLSKANAEAQLWRSKYESEGLARLEELEEAKRKL-HG 1390
Cdd:pfam02463 619 DKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILrRQ 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1391 KLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSI--------EVDKANALASSLEKRQKSFDKVIAEWKAKVDDLAAEL 1462
Cdd:pfam02463 699 LEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKineelkllKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAE 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1463 DASQKECRNYSTEVFKLRAAYEESQEHYESVKRENKNLQDEvkDLMDQLGEGGRSVHELEKSRKRLEMEKEELQAALEEA 1542
Cdd:pfam02463 779 EREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEE--EQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEEL 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1543 EAALEQEENKVLRAQLELSQVR---QEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRLKKKLESDINE 1619
Cdd:pfam02463 857 ERLEEEITKEELLQELLLKEEEleeQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEE 936
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556079866 1620 LEIALDHANKANAEAQKNLKKYQQNVKDLQGALEEEQRARDEAREQYASAERRCNAMHGELEE 1682
Cdd:pfam02463 937 PEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKER 999
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
913-1749 |
1.27e-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: 93.26 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 913 QLADLNDRLSHEEDAHaslsqSKKKLEgeisgLKKDIEDMELALQKAEQDK-ATKDHQIRnlndEIQHQDELINKLNKEK 991
Cdd:pfam15921 86 QVKDLQRRLNESNELH-----EKQKFY-----LRQSVIDLQTKLQEMQMERdAMADIRRR----ESQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 992 KHLQEASQKTSEDLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKARGdieknKRKVEGDlklaQEAVADLEKNKKEM 1071
Cdd:pfam15921 152 HELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASG-----KKIYEHD----SMSTMHFRSLGSAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1072 EQNLQRKEKEMASLAAKL---EDE-QALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLAReieelserleE 1147
Cdd:pfam15921 223 SKILRELDTEISYLKGRIfpvEDQlEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSAR----------S 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1148 SGGATSSQIEL--NKRREAELSKLRR--DLEESNLQHEQAMSNLRKKHNDTVAEMSEQIDQLNKHKAKVEKERATMSAEV 1223
Cdd:pfam15921 293 QANSIQSQLEIiqEQARNQNSMYMRQlsDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQES 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1224 SD----LQSLLD--HSNKAQANAEK-QVKQLEVQLADAQFKVDEMNRTLND-------LDGGKKKLAVE-NSELQRQLEE 1288
Cdd:pfam15921 373 GNlddqLQKLLAdlHKREKELSLEKeQNKRLWDRDTGNSITIDHLRRELDDrnmevqrLEALLKAMKSEcQGQMERQMAA 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1289 SESQVAQLNKIkASLATQLEEAKRMADEEARERAAILGKYRNLEHDLDNLRESVEEEqeakadfQRQLSKANAEAQLWRS 1368
Cdd:pfam15921 453 IQGKNESLEKV-SSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK-------ERAIEATNAEITKLRS 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1369 KYEseglARLEELEEAKRKlHGKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEVDKANALASSLEKRQKSFDKVI 1448
Cdd:pfam15921 525 RVD----LKLQELQHLKNE-GDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEI 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1449 AEWKAKVDDLAAELDASQKECRNYSTEVfklraayeesqehyesvkrenKNLQDEVKDLMDQLGEGGRSVHELEKSRKRL 1528
Cdd:pfam15921 600 NDRRLELQEFKILKDKKDAKIRELEARV---------------------SDLELEKVKLVNAGSERLRAVKDIKQERDQL 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1529 emekeelqaaleeaeaaleqeENKVLRAQLELSQVRQE---IDRRIQEKEEEFENTRKNHQRALDSMQASLEaeakgkae 1605
Cdd:pfam15921 659 ---------------------LNEVKTSRNELNSLSEDyevLKRNFRNKSEEMETTTNKLKMQLKSAQSELE-------- 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1606 alrlkkKLESDINELEIALDHANKANAEAQKNLKKYQQNVKDLQGALEEEQRARDEAREQYASAERRCNAMHGELEEsrq 1685
Cdd:pfam15921 710 ------QTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELST--- 780
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556079866 1686 lLASSKNSHLRHIEQMEGEELLMQKKLRTEVIRLEDALVQV--------RKEYEMLRIEFEQNLAATEQTGP 1749
Cdd:pfam15921 781 -VATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFaecqdiiqRQEQESVRLKLQHTLDVKELQGP 851
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
843-1402 |
1.67e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 92.69 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 843 ELKAMEEKLKKTEEALAKEEKLRKELEEHNVKVLQEKNDLFLQLEAERMGAGDVEERLNKALTQKGDLESQLADLNDRLS 922
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 923 HEEDAHASLSQSKKKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLND-------EIQHQDELINKLNKEKKHLQ 995
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEalleaeaELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 996 EASQKTSEDLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKARgdieknkrkvegdlklaqeavADLEKNKKEMEQNL 1075
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE---------------------EEEEEALEEAAEEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1076 QRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLAREIEELSERLEESGGATSSQ 1155
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIG 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1156 IELNKRR--EAELSKLRRDLEESNLQHEQAMSNLRKKHNDTVAEmseqIDQLNKHKAKVEKERATMSAEVSDLQSLLDHS 1233
Cdd:COG1196 532 VEAAYEAalEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT----FLPLDKIRARAALAAALARGAIGAAVDLVASD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1234 NKAQANAEKQVKQLEVQLADAQFKVDEMNRTLNDLDGGKKKLAVENSELQRQLEESESQVAQLNKIKASLATQLEEAKRM 1313
Cdd:COG1196 608 LREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1314 ADEEARERAAILGKYRNLEHDLDNLRESVEEEQEAKADFQRQLS--KANAEAQLWRSKYESEGLARLEELEEAKR-KLHG 1390
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEaeREELLEELLEEEELLEEEALEELPEPPDLeELER 767
|
570
....*....|..
gi 556079866 1391 KLQEAEEAMEQL 1402
Cdd:COG1196 768 ELERLEREIEAL 779
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
897-1507 |
9.19e-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: 90.08 E-value: 9.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 897 EERLNKALTQKGDLESQLADLNDRLSHEEDAHASLS-------QSKKKLEGEISGLKKDIEDMELALQKAEQDKATKDHQ 969
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNnkyndlkKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 970 IRNLNDEIQHQDEL---INKLNKEKKHLQEASQKTSEDLQateDKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIEKN 1046
Cdd:TIGR04523 203 LSNLKKKIQKNKSLesqISELKKQNNQLKDNIEKKQQEIN---EKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1047 KRKVEGDLKLAQEAVADLEKNKKEMEQN--------LQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELE 1118
Cdd:TIGR04523 280 NKKIKELEKQLNQLKSEISDLNNQKEQDwnkelkseLKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENS 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1119 AERQARAKAEKQRADLAREIEELSERLEESGGATS---SQIELNKRREAELSKLRRDLEESNLQHEQAMSNLRKKHNDTV 1195
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINdleSKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNN 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1196 AEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDHSNKAQANAEKQVKQLevqladaqfkvDEMNRTLNDLDGGKKKL 1275
Cdd:TIGR04523 440 SEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEL-----------KSKEKELKKLNEEKKEL 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1276 AVENSELQRQLEESESQVAQLNKIKASLATQLEEAKRMADEEARERaailgKYRNLEHDLDNLRESVEEEQEAkadfQRQ 1355
Cdd:TIGR04523 509 EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFEL-----KKENLEKEIDEKNKEIEELKQT----QKS 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1356 LSKANAEAQLWRSKYESEGLA---RLEELEEAKRKLHGKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEVDKANA 1432
Cdd:TIGR04523 580 LKKKQEEKQELIDQKEKEKKDlikEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556079866 1433 LASSLEKRQKSFDKVIAEWKAKVDDLAAELDASQKEcrnYSTEVFKLRaAYEESQEHYESVKRENKNLQDEVKDL 1507
Cdd:TIGR04523 660 KWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKK---YITRMIRIK-DLPKLEEKYKEIEKELKKLDEFSKEL 730
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1280-1744 |
1.26e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.00 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1280 SELQRQLEESESQVAqlnkiKASLATQLEEakrmaDEEARERAAILGKYRNLEHDLDNLRESVEEEQEAKADFQRQLSKA 1359
Cdd:COG1196 196 GELERQLEPLERQAE-----KAERYRELKE-----ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1360 NAEaqlwrskyeseglarLEELEEAKRKLHGKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEVDKANALASSLEK 1439
Cdd:COG1196 266 EAE---------------LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1440 RQKSFDKVIAEWKAKVDDLAAELDASQKECRNYSTEVFKLRAAYEESQEHYESVKRENKNLQDEVKDLMDQLGEGGRSVH 1519
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1520 ELEKSRKRLEMEKEELQAALEeaeaaleqeenKVLRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAE 1599
Cdd:COG1196 411 ALLERLERLEEELEELEEALA-----------ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1600 AKGKAEALRLKKKLESDINELEIALDHANKANAEAQKNLKKYQQNVKDLQGALEEEQRARDEAREQYASAERRCNAMhGE 1679
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDD-EV 558
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556079866 1680 LEESRQLLASSKNSHL--RHIEQMEGEELLMQKKLRTEVIRLEDALVQVRKEYEMLRIEFEQNLAAT 1744
Cdd:COG1196 559 AAAAIEYLKAAKAGRAtfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR 625
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
875-1462 |
8.09e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 87.40 E-value: 8.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 875 VLQEKNDLFLQLEA--ERMGAGDVEERLNkaltqkgDLESQLADLNDRLSH----EEDAHASLSQSKKKLEG------EI 942
Cdd:PRK02224 181 VLSDQRGSLDQLKAqiEEKEEKDLHERLN-------GLESELAELDEEIERyeeqREQARETRDEADEVLEEheerreEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 943 SGLKKDIEDMELALQKAEQDKATkdhqirnLNDEIQHQDELINKLNKEKKHLQEASQKTSEDLQATEDKVNHLNKVKAKL 1022
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREE-------LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEEL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1023 EQTLDEledslerekkARGDIEKNKRKVEGdlklAQEAVADLEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQ 1102
Cdd:PRK02224 327 RDRLEE----------CRVAAQAHNEEAES----LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1103 IKELQARIEELEEeleaerqARAKAEKQRADLAreieelserlEESGGATSSQIELnkrrEAELSKLRRDLEESN-LQHE 1181
Cdd:PRK02224 393 IEELRERFGDAPV-------DLGNAEDFLEELR----------EERDELREREAEL----EATLRTARERVEEAEaLLEA 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1182 -------QAMSNlrKKHNDTVAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDHSNKAQANAEKqVKQLEVQLADA 1254
Cdd:PRK02224 452 gkcpecgQPVEG--SPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEER-REDLEELIAER 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1255 QFKVDEMNRTLNDLDGGKKKLAVEN-------SELQRQLEESESQVAQLNKIKASLATQLEEAKRMADeeareraaILGK 1327
Cdd:PRK02224 529 RETIEEKRERAEELRERAAELEAEAeekreaaAEAEEEAEEAREEVAELNSKLAELKERIESLERIRT--------LLAA 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1328 YRNLEHDLDNLRESVEEEQEAKADFQRQLSKANAEAQLWRSKYESeglARLEELEEAKRKLHGKLQEAEEAMEQLNAKCS 1407
Cdd:PRK02224 601 IADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDE---ARIEEAREDKERAEEYLEQVEEKLDELREERD 677
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 556079866 1408 GLEKTKSHLQGELEDMSIEVDKANALASSLEKRQKSFDKViAEWKAKVDDLAAEL 1462
Cdd:PRK02224 678 DLQAEIGAVENELEELEELRERREALENRVEALEALYDEA-EELESMYGDLRAEL 731
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
949-1532 |
1.20e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 86.66 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 949 IEDMELALQKAEQDKATKDHQIRNLNDEIQHQDELINKLNKEKKHLQEASQKTSEDLQATEDKVNHLNKVKAKLEqTLDE 1028
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-ELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1029 LEDSLEREKKARGDIEKNKRKVEGDLKLAQEAVADLEKNKKEMEQNLQRKEkemaslaaKLEDEQALVAKLQKQIKELQA 1108
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK--------ELKEKAEEYIKLSEFYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1109 RIEELEEELEAERQARAKAEKQRADLAREieelserleesggatSSQIELNKRREAELSKLRRDLEESNLQHEQAMSNLr 1188
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGIEERIKELEEK---------------EERLEELKKKLKELEKRLEELEERHELYEEAKAKK- 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1189 kkhndtvaemseqiDQLNKHKAKVEKEratmsaEVSDLQSLLDHSNKAQANAEKQVKQLEVQLADAQFKVDEMNRTLNDL 1268
Cdd:PRK03918 372 --------------EELERLKKRLTGL------TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1269 DGGKKKLAVENSELQRQLEES--ESQVAQLNKIKASLATqLEEAKRMADEEARERAAILG------KYRNLEHDLDNLRE 1340
Cdd:PRK03918 432 KKAKGKCPVCGRELTEEHRKEllEEYTAELKRIEKELKE-IEEKERKLRKELRELEKVLKkeseliKLKELAEQLKELEE 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1341 SVE----EEQEAKADFQRQLSKANAEAQLWRSKYESEgLARLEELEEAKRKLHGKLQEAEEAMEQLNAKCSGLE-KTKSH 1415
Cdd:PRK03918 511 KLKkynlEELEKKAEEYEKLKEKLIKLKGEIKSLKKE-LEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEE 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1416 LQGELEDMSIEVDKANALASSlEKRQKSFDKVIAEWKAKVDDLAAELDASQKECRNYSTEVFKLRAAYeeSQEHYESVKR 1495
Cdd:PRK03918 590 LEERLKELEPFYNEYLELKDA-EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY--SEEEYEELRE 666
|
570 580 590
....*....|....*....|....*....|....*..
gi 556079866 1496 ENKNLQDEVKDLMDQLGEGGRSVHELEKSRKRLEMEK 1532
Cdd:PRK03918 667 EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
848-1531 |
1.26e-16 |
|
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: 86.77 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 848 EEKLKKTEEALAKEEKLRKELEEHNVKVLQEKNDLFLQLEAERMGAGDVEERLNKALTQKGDLESQLADLNDRLSHEEDA 927
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 928 HASLSQSKKKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLNDEIQHQDELINKLNKEKKHLQEASQKTSEDLQA 1007
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEE 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1008 TEDKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKRKVEGDLKLAQEAVADLEKNKKEMEQNLQRKEKEMASLAA 1087
Cdd:pfam01576 564 KAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLAR 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1088 KLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQR----ADLAREIEELSERLEESGGATSSQIELNKRRE 1163
Cdd:pfam01576 644 ALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKraleQQVEEMKTQLEELEDELQATEDAKLRLEVNMQ 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1164 AELSKLRRDLEESNLQHEQAMSNLRKKhndtVAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDHSNKAQANAEKQ 1243
Cdd:pfam01576 724 ALKAQFERDLQARDEQGEEKRRQLVKQ----VRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQ 799
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1244 VKQLEVQLADAQfkvdemnRTLNDLDGGKKKLAVENSELQRQLEESESQVAQLNKIKASLATQLEEAKRMADEEARE--- 1320
Cdd:pfam01576 800 LKKLQAQMKDLQ-------RELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEias 872
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1321 ----RAAILGKYRNLEHDLDNLRESVEEEQ---EAKADFQR----QLSKANAEAQLWRSKYESEGLARlEELEEAKRKLH 1389
Cdd:pfam01576 873 gasgKSALQDEKRRLEARIAQLEEELEEEQsntELLNDRLRkstlQVEQLTTELAAERSTSQKSESAR-QQLERQNKELK 951
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1390 GKLQEAEEAME-QLNAKCSGLEKTKSHLQGELEDMSIEVDKANALASSLEKRQKsfdkviaEWKAKVDDlaaeldasqke 1468
Cdd:pfam01576 952 AKLQEMEGTVKsKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLK-------EVLLQVED----------- 1013
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556079866 1469 crnystevfklraayeeSQEHYESVKRENKNLQDEVKDLMDQLGEGGRSVHELEKSRKRLEME 1531
Cdd:pfam01576 1014 -----------------ERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRE 1059
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1281-2072 |
4.48e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 85.11 E-value: 4.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1281 ELQRQLEESESQVAQLNKIKASLATQLEEAKRMAdEEARERAAILGKYRNLEH-----DLDNLRESVEEEQEAKADFQRQ 1355
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNELERQLKSLERQA-EKAERYKELKAELRELELallvlRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1356 LSKANAEAQlwrsKYESEglarLEELEEAKRKLHGKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEVDKANALAS 1435
Cdd:TIGR02168 255 LEELTAELQ----ELEEK----LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1436 SLEKRQKSFDKVIAEWKAKVDDLAAELDASQKECRNYSTEVFKLRAAYEESQEHYESVKRENKNLQDEVKDLMDQLGEGG 1515
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1516 RSVHELEKSRKRLEMEKEELQAALEEAEAALEQEENKVLRAQLELSQVRQE--------IDRRIQEKEEEFENTRKNHQR 1587
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELErleealeeLREELEEAEQALDAAERELAQ 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1588 ------ALDSMQASLEAEAKGKAEAL-----------RLKKKLESDiNELEIALDHANKANaeAQKNLKKYQQNVKDLQG 1650
Cdd:TIGR02168 487 lqarldSLERLQENLEGFSEGVKALLknqsglsgilgVLSELISVD-EGYEAAIEAALGGR--LQAVVVENLNAAKKAIA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1651 ALEEEQRARDEAREQYASAERRCNAMHGELEESRQLLASSKNShlrHIEQMEGEELLMQKKLRTEVI--RLEDALVQVRK 1728
Cdd:TIGR02168 564 FLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKD---LVKFDPKLRKALSYLLGGVLVvdDLDNALELAKK 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1729 EYEMLRI-----------------EFEQNLAATEQTGPInREMRHLITSLQSHNRQLKGEVSRYKRKLREAAAEAARLKQ 1791
Cdd:TIGR02168 641 LRPGYRIvtldgdlvrpggvitggSAKTNSSILERRREI-EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1792 TLEMSNVAVSSTTVPSSASSTSSDNGSSRGEEgapvscpqpgQGGREEGGTPSASSQRREEEAREEEPIPEREKGKSDLD 1871
Cdd:TIGR02168 720 ELEELSRQISALRKDLARLEAEVEQLEERIAQ----------LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1872 IIRDLKAQLKKSQEAQRELKLLLDMYKGapkEQRDKVQLMAAEKKARAEVEEHRQQLKKLAEHERKERRKLADEdaMKKI 1951
Cdd:TIGR02168 790 QIEQLKEELKALREALDELRAELTLLNE---EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE--IEEL 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1952 RGLEETVASLHKSLTAQKQEVWE--EALLSEMEVTGQAFEDMQEQNLRLIQQLREKDDanfKLMSERIKSNQIHKLLQEE 2029
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEalALLRSELEELSEELRELESKRSELRRELEELRE---KLAQLELRLEGLEVRIDNL 941
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 556079866 2030 KAMLSEQGATLQAQVEAQnqvVRKLEEKERLLQNSLSTLEKEL 2072
Cdd:TIGR02168 942 QERLSEEYSLTLEEAEAL---ENKIEDDEEEARRRLKRLENKI 981
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1163-1526 |
1.58e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 83.19 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1163 EAELSKLRRDLEESNLQHEQAMSnlrkkhndTVAEMSEQIDQLNKHKAKVEKERATMS----AEVSDLQSLLDHSNKAQA 1238
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDL--------IIDEKRQQLERLRREREKAERYQALLKekreYEGYELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1239 NAEKQVKQLEVQLADAQFKVDEMNRTLNDLDggkKKLAVENSELQRQLEESESQV-AQLNKIKASLAT---QLEEAKRMA 1314
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIE---QLLEELNKKIKDLGEEEQLRVkEKIGELEAEIASlerSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1315 DEEARERAAILGKYRNLEHDLDNLRESVEEEQEAKADFQRQLSKANAEAQLWRSkyeseglaRLEELEEAKRKLHGKLQE 1394
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA--------ELEEVDKEFAETRDELKD 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1395 AEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEVDKANALASSLEKRQKSFDKVIAEWKAKVDDLAAELDASQKECRNYST 1474
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 556079866 1475 EVFKLRAAYEESQEHYESVKRENKNLQDEVKDLMDQLGEGGRSVHELEKSRK 1526
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
837-1499 |
2.09e-15 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 82.38 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 837 AVRVEDELKAMEEKLKKTEEALAKEEKLrkeleehnVKVLQEKNDlflqleaermgagDVEERLNKALTQKGDLESQLAD 916
Cdd:TIGR04523 28 ANKQDTEEKQLEKKLKTIKNELKNKEKE--------LKNLDKNLN-------------KDEEKINNSNNKIKILEQQIKD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 917 LNDRLSHEEDAHASLSQSKKKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLNDEIQHQDELINKLN-------K 989
Cdd:TIGR04523 87 LNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNnkyndlkK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 990 EKKHLQEASQKTSEDLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKRKVEgdlklaqeavaDLEKNKK 1069
Cdd:TIGR04523 167 QKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNN-----------QLKDNIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1070 EMEQNLQRKEKEMASLAAKLEDeqaLVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLAreieelserleesg 1149
Cdd:TIGR04523 236 KKQQEINEKTTEISNTQTQLNQ---LKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIS-------------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1150 gatssqiELNKRREAELSK-LRRDLEESNLQHEQAMSNLRkKHNDTVAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQS 1228
Cdd:TIGR04523 299 -------DLNNQKEQDWNKeLKSELKNQEKKLEEIQNQIS-QNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQN 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1229 LLDHSNKAQANAEKQVKQLEVQLADAQFKVDEMNRTLNDLDGGKKKLAVENSELQRQLE-------ESESQVAQLNKIKA 1301
Cdd:TIGR04523 371 EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIErlketiiKNNSEIKDLTNQDS 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1302 SLATQLEEAKRMADEEARERAAILGKYRNLEHDLDNL-RESVEEEQEAKA--DFQRQLSKANAEAQlwrsKYESEGLARL 1378
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKqKELKSKEKELKKlnEEKKELEEKVKDLT----KKISSLKEKI 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1379 EELEEAKRKLHGKLQEAEEAMEQL--NAKCSGLEKTKSHLQGELEDMSIEVD-------KANALASSLEKRQKSFDKVIA 1449
Cdd:TIGR04523 527 EKLESEKKEKESKISDLEDELNKDdfELKKENLEKEIDEKNKEIEELKQTQKslkkkqeEKQELIDQKEKEKKDLIKEIE 606
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 556079866 1450 EWKAKVDDLAAELDASQKECRNYSTEVFKLRAAYEESQEHYESVKRENKN 1499
Cdd:TIGR04523 607 EKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKE 656
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
934-1740 |
3.81e-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: 3.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 934 SKKKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLNDEIQHQDELINKLNKEKKHLQEASQKTSEDLQATEDKVN 1013
Cdd:pfam02463 175 LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1014 HLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKRKVEGDLKLAQEAVADLEKNKKEMEQNLQRKEKEMASLAAKLEDEQ 1093
Cdd:pfam02463 255 SSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1094 ALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLAREIEELSERLeesgGATSSQIELNKRREAELSKLRRDL 1173
Cdd:pfam02463 335 EEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERL----SSAAKLKEEELELKSEEEKEAQLL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1174 EESNLQHEQAMSNLRKKHNDTVAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDHSNKAQANAEKQVKQLEVQLAD 1253
Cdd:pfam02463 411 LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLL 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1254 AQFKVDEMNRTLNDLDGGKKKlaveNSELQRQLEESESQVAQLNKIKASLATQLEEAKRMA------DEEARERAAILGK 1327
Cdd:pfam02463 491 SRQKLEERSQKESKARSGLKV----LLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTavivevSATADEVEERQKL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1328 YRNLEHDLDNLRESVEEEQEAKADFQRQLSKANAEAQLWRSKYESEGLARLEELEEAKRKLHGKLQEAEEAMEQLNAKCS 1407
Cdd:pfam02463 567 VRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKES 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1408 GLEKTKSHLQGELE----DMSIEVDKANALASSLEKRQKSFDKVIAEWKAKVDDLAAELDASQKECRNYSTEVFKL---- 1479
Cdd:pfam02463 647 GLRKGVSLEEGLAEksevKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELladr 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1480 -RAAYEESQEHYESVKRENK-NLQDEVKDLMDQLGEGGRSVHELEKSRKRLEMEKEELQAALEEAEAALEQEENKVLRAQ 1557
Cdd:pfam02463 727 vQEAQDKINEELKLLKQKIDeEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRAL 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1558 LELSQVRQEIDRRIQEKEEEFENTR-----KNHQRALDSMQASLEAEAKGKAEALRLKKKLESDINELEialDHANKANA 1632
Cdd:pfam02463 807 EEELKEEAELLEEEQLLIEQEEKIKeeeleELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLK---EEELEEQK 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1633 EAQKNLKKYQQNVKDLQGALEEEQRARDEAREQYASAERRCNAMHGELEESRQLLASSKNSHLRHIEQMEGEELLMQKKL 1712
Cdd:pfam02463 884 LKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNK 963
|
810 820
....*....|....*....|....*...
gi 556079866 1713 RTEVIRLEDALVQVRKEYEMLRIEFEQN 1740
Cdd:pfam02463 964 RLLLAKEELGKVNLMAIEEFEEKEERYN 991
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
837-1409 |
4.48e-15 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 81.76 E-value: 4.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 837 AVRVEDELKAMEEKLKKTEEALAKEEKLRKELEEHNVKVLQEKNDLFLQLEAERMGAGDVEERLNKaltqkgdLESQLAD 916
Cdd:pfam01576 456 NIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLST-------LQAQLSD 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 917 LNDRLSHEEDAHASLSQSKKKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLNDEIQHQDELINKLNKEKKHLQ- 995
Cdd:pfam01576 529 MKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDq 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 996 ---------------------EASQKT------SEDLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKR 1048
Cdd:pfam01576 609 mlaeekaisaryaeerdraeaEAREKEtralslARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKR 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1049 KVEGDLKLAQEAVADLEKNKKEMEQNLQRKEKEMASLAAKLE------DEQALVAK--LQKQIKELQARIEELeeeleae 1120
Cdd:pfam01576 689 ALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFErdlqarDEQGEEKRrqLVKQVRELEAELEDE------- 761
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1121 RQARAKAEKQRADLAREIEELSERLEESGGATSSQIELNKRREAELSKLRRDLEESNLQHEQAMSNLR---KKHNDTVAE 1197
Cdd:pfam01576 762 RKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKeseKKLKNLEAE 841
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1198 ---MSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDHSNKAQANAEKQVKQLEVQLADAQFKVDEMN------------ 1262
Cdd:pfam01576 842 llqLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNdrlrkstlqveq 921
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1263 ---------RTLNDLDGGKKKLAVENSELQRQLEESESQVAQLNKIK-ASLATQLEEAKRMADEEARERAAILGKYRNLE 1332
Cdd:pfam01576 922 lttelaaerSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSiAALEAKIAQLEEQLEQESRERQAANKLVRRTE 1001
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1333 HDLDNLRESVEEEQEAKADFQRQLSKANAEA-QLWRskyeseglaRLEELEE-------AKRKLHGKLQEAEEAMEQLNA 1404
Cdd:pfam01576 1002 KKLKEVLLQVEDERRHADQYKDQAEKGNSRMkQLKR---------QLEEAEEeasranaARRKLQRELDDATESNESMNR 1072
|
....*
gi 556079866 1405 KCSGL 1409
Cdd:pfam01576 1073 EVSTL 1077
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
906-1127 |
6.60e-14 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 75.96 E-value: 6.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 906 QKGDLESQLADLNDRLSHEEDAHASLSQSKKKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLNDEIQHQDELIN 985
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 986 KLNKEKKHLQEASQKTSE----DLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKRKVEGDLKLAQEAV 1061
Cdd:COG4942 101 AQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556079866 1062 ADLEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKA 1127
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
982-1715 |
2.05e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 76.16 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 982 ELINKLNKEKKHLQEASQKTSEDLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKRKVegdlKLAQEAV 1061
Cdd:TIGR00618 191 SLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQ----QLLKQLR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1062 ADLEK-NKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLAREIEE 1140
Cdd:TIGR00618 267 ARIEElRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1141 LSerleesggaTSSQIELNKRREAELSKLRRdlEESNLQHEQAMSNLRKKHNDTVAEMSEQIdqLNKHKAKVEKERATMS 1220
Cdd:TIGR00618 347 LQ---------TLHSQEIHIRDAHEVATSIR--EISCQQHTLTQHIHTLQQQKTTLTQKLQS--LCKELDILQREQATID 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1221 AEVSDLQSLLDHSNKAQANAEKQVKQLEVQLADAQFKVDEmnrtlndldggKKKLAVENSELQRQLEESESQVAQLNKIk 1300
Cdd:TIGR00618 414 TRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQC-----------EKLEKIHLQESAQSLKEREQQLQTKEQI- 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1301 aslatQLEEAKRMADEEAReraailgkyrnlehdldnlresVEEEQEAKADFQRQLSKANAEAQLwrsKYESEGLARLEE 1380
Cdd:TIGR00618 482 -----HLQETRKKAVVLAR----------------------LLELQEEPCPLCGSCIHPNPARQD---IDNPGPLTRRMQ 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1381 LEEAKrklHGKLQEAEEAME-QLNAKCSGLEKTKSHLQGELEDMSIEVDKANALASSLEKRQKSFDKVIAEWKAKVDDLA 1459
Cdd:TIGR00618 532 RGEQT---YAQLETSEEDVYhQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAED 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1460 AELDASQKECRNYSTEVFKLRAAYEESQEHYESVKRENKNLQDEVKDLMDQLGEGGRSVHELEKsrkrlemekeeLQAAL 1539
Cdd:TIGR00618 609 MLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPK-----------ELLAS 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1540 EEAEAALEQEENKVLRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALrlkkklesdiNE 1619
Cdd:TIGR00618 678 RQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSL----------KE 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1620 LEIALDHANKANAEAQKNlkKYQQNVKDLQGALEEEQRARDEAREQYasaerrcnamhgELEESRQLLASSKNSHLRHIE 1699
Cdd:TIGR00618 748 LMHQARTVLKARTEAHFN--NNEEVTAALQTGAELSHLAAEIQFFNR------------LREEDTHLLKTLEAEIGQEIP 813
|
730
....*....|....*.
gi 556079866 1700 QMEGEELLMQKKLRTE 1715
Cdd:TIGR00618 814 SDEDILNLQCETLVQE 829
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
907-1281 |
2.10e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 76.26 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 907 KGDLESQLADLNDRLSHEEDAHASLSQSKKKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLNDEIQHQDELINK 986
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 987 LNKEKKHLQEASQKTSEDLQATEDKVNH------------LNKVKAKLEQTLDELEDSLERE-------KKARGDIEKNK 1047
Cdd:TIGR02169 763 LEARIEELEEDLHKLEEALNDLEARLSHsripeiqaelskLEEEVSRIEARLREIEQKLNRLtlekeylEKEIQELQEQR 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1048 RKVEGDLKLAQEAVADLEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIeeleeeleaeRQARAKA 1127
Cdd:TIGR02169 843 IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI----------EELEAQI 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1128 EKQRADLAREIEELSERLEESggatsSQIELNKRREAELSKLR---RDLEESNLQHEQAMSNLRKKHNDTVAEMSEQIDQ 1204
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEEEL-----SEIEDPKGEDEEIPEEElslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKR 987
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556079866 1205 LNKHKAKvekeRATMSAEVSDLQSLLDhsnkaqaNAEKQVKQLEVQLADAqfKVDEMNRTLNDLDGGKKKLAVENSE 1281
Cdd:TIGR02169 988 LDELKEK----RAKLEEERKAILERIE-------EYEKKKREVFMEAFEA--INENFNEIFAELSGGTGELILENPD 1051
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1026-1606 |
5.06e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 74.72 E-value: 5.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1026 LDELEDSLEREKKARGDIEKNKRKVEGDLKlaqeAVADLEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKE 1105
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFIK----RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1106 LQA---RIEELEEELEAERQARAKAEKQRADLAREIEELSERLEESGGATSSQIELNKRREA--ELSKLRRDLEESNLQH 1180
Cdd:PRK03918 233 LEElkeEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1181 EQAMSNLRKKhndtVAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLldhsnKAQANAEKQVKQLEVQLadAQFKVDE 1260
Cdd:PRK03918 313 EKRLSRLEEE----INGIEERIKELEEKEERLEELKKKLKELEKRLEEL-----EERHELYEEAKAKKEEL--ERLKKRL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1261 MNRTLNDLDGGKKKLAVENSELQRQLEESESQVAQLNKIKASLATQLEEAK----------RMADEEARERaaILGKYRn 1330
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgRELTEEHRKE--LLEEYT- 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1331 leHDLDNLRESVEEEQEAKADFQRQLSKanAEAQLWRSKYESEGLARLEELEEAKRKLHG----KLQEAEEAMEQLNAKC 1406
Cdd:PRK03918 459 --AELKRIEKELKEIEEKERKLRKELRE--LEKVLKKESELIKLKELAEQLKELEEKLKKynleELEKKAEEYEKLKEKL 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1407 SGLEKTKSHLQGELEDMSIEVDKANALASSLEKRQKSFDKVIAEWKAKVDDLAAELDASQKECRNYSTEVFKLRAAYEEs 1486
Cdd:PRK03918 535 IKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKE- 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1487 qehYESVKRENKNLQDEVKDLMDQLGEGGRSVHELEKSRKRLEMEKEELQAALEEAEAALEQEENKVLRAQLE-LSQVRQ 1565
Cdd:PRK03918 614 ---LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEeLEKRRE 690
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 556079866 1566 EIDRRIQEKEEEFENTRK------NHQRALDSMQASLEAEAKGKAEA 1606
Cdd:PRK03918 691 EIKKTLEKLKEELEEREKakkeleKLEKALERVEELREKVKKYKALL 737
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1026-1686 |
5.23e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 74.69 E-value: 5.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1026 LDELEDSLEREKKAR---GDIEKNKRKVEGDLKlAQ----------EAVADLEKNKKEMEQNLQRKEKEMASLAAKLEDE 1092
Cdd:PRK02224 161 LGKLEEYRERASDARlgvERVLSDQRGSLDQLK-AQieekeekdlhERLNGLESELAELDEEIERYEEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1093 QALVAKLQkqikELQARIEELEEELEAERQARAKAEKQRADLAReieelserleesggATSSQIELNKRREAELSKLRRD 1172
Cdd:PRK02224 240 DEVLEEHE----ERREELETLEAEIEDLRETIAETEREREELAE--------------EVRDLRERLEELEEERDDLLAE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1173 LEESNLQHEQAmsnlrkkhndtvaemSEQIDQLNKHKAKVEKERATMSAEVSDlqslldHSNKAQANAEKqVKQLEVQLA 1252
Cdd:PRK02224 302 AGLDDADAEAV---------------EARREELEDRDEELRDRLEECRVAAQA------HNEEAESLRED-ADDLEERAE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1253 DAQFKVDEmnrtlndLDGGKKKLAVENSELQRQLEESESQVAQLNKIKASLATQLEEAKRMADEEARERAAILGKYRNLE 1332
Cdd:PRK02224 360 ELREEAAE-------LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELE 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1333 HDLDNLRESVEEEQEakadfqrqLSKANAEAQLWRSKYESEGLARLEELEEAKRKLHGKLQEAEEAMEQLNAKCSGLEKT 1412
Cdd:PRK02224 433 ATLRTARERVEEAEA--------LLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1413 KshlqgeledmsievdKANALASSLEKRQKSFDKVIAEWKAKVDDLAAELDASQKECRNYSTEVFKLRAAYEESQEHYES 1492
Cdd:PRK02224 505 V---------------EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1493 VkrenknlQDEVKDLMDQLGEGGRSVHELEKSRKRLEmekeelqaaleeaeaaleqeenkvlraqlELSQVRQEIDRRiQ 1572
Cdd:PRK02224 570 A-------REEVAELNSKLAELKERIESLERIRTLLA-----------------------------AIADAEDEIERL-R 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1573 EKEEEFentrknhqraldsmqASLEAEAKGKAEALRLKKK-LESDINELEIALDHANKANAEaqknlkKYQQNVK----- 1646
Cdd:PRK02224 613 EKREAL---------------AELNDERRERLAEKRERKReLEAEFDEARIEEAREDKERAE------EYLEQVEeklde 671
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 556079866 1647 ------DLQ---GALEEEQRARDEAREQYASAERRCNAMHGELEESRQL 1686
Cdd:PRK02224 672 lreerdDLQaeiGAVENELEELEELRERREALENRVEALEALYDEAEEL 720
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
27-70 |
1.74e-12 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 63.60 E-value: 1.74e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 556079866 27 DGKKMVWVPDEKEGFILGNISSTKGDMVTVDCPGG-ERVFKKDQL 70
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGkTVTVKKDDV 45
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
840-1344 |
2.00e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.79 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 840 VEDELKAMEEKLKKTEEALAKEEKLRKE--LEEHNVKVLQEKNDLFLQLEAERMGAGDVEERLNKALtqkGDLESQLADL 917
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEEleEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL---SRLEEEINGI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 918 NDRLSHEEdahaSLSQSKKKLEGEISGLKKDIEDMELALQKAEQDKATKDhQIRNLNDEIqhQDELINKLNKEKKHLQEA 997
Cdd:PRK03918 327 EERIKELE----EKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE-ELERLKKRL--TGLTPEKLEKELEELEKA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 998 SQKtsedlqaTEDKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKRKVEGD-----LKLAQEAVADLEKNKKEME 1072
Cdd:PRK03918 400 KEE-------IEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRIEKELKEIE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1073 QNLQRKEKEMASLAAKLEDEQALVA--KLQKQIKELQARIEELEEEleaerQARAKAEKQRADLAREIEELSERLEESGG 1150
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKESELIKlkELAEQLKELEEKLKKYNLE-----ELEKKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1151 ATSSQiELNKRREAELSKLRRDLEE-SNLQHEqamsnLRKKHNDTVAEMSEQIDQLNkhkaKVEKERATMSAEVSDLQSL 1229
Cdd:PRK03918 548 LEKLE-ELKKKLAELEKKLDELEEElAELLKE-----LEELGFESVEELEERLKELE----PFYNEYLELKDAEKELERE 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1230 LDHSNKAQANAEKQVKQLEVQLADAQF---KVDEMNRTLNDLDggKKKLAVENSELQRQLEESESQVAQLNKIKASLATQ 1306
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLEElrkELEELEKKYSEEE--YEELREEYLELSRELAGLRAELEELEKRREEIKKT 695
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 556079866 1307 LEEAKRMADE--EARERAAILGKYRNlehDLDNLRESVEE 1344
Cdd:PRK03918 696 LEKLKEELEEreKAKKELEKLEKALE---RVEELREKVKK 732
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
839-1477 |
2.19e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.79 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 839 RVEDELKAMEEKLKKTEEALAKEEKLRKELEEHNVKVLQEKNDLFLQLEaermgagDVEERLNKALTQKGDLESqladLN 918
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELP-------ELREELEKLEKEVKELEE----LK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 919 DRLSHEEDAHASLSQSKKKLEGEISGLKKDIEDMELALQKAEQdkatkdhQIRNLNdEIQHQDELINKLNKEKKHLQEAS 998
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE-------KVKELK-ELKEKAEEYIKLSEFYEEYLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 999 QKTSEDLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKargdIEKNKRKVEGDLKLAQEAVAdLEKNKKEMEQNLQRK 1078
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE----LEKRLEELEERHELYEEAKA-KKEELERLKKRLTGL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1079 EKEmaSLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRadlareieelserleesGGATSSQIEL 1158
Cdd:PRK03918 385 TPE--KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAK-----------------GKCPVCGREL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1159 NKRREAELskLRRDLEEsnlqheqaMSNLRKKhndtVAEMSEQIDQLNKHKAKVEKERATMSaEVSDLQSLLDHSNkaqa 1238
Cdd:PRK03918 446 TEEHRKEL--LEEYTAE--------LKRIEKE----LKEIEEKERKLRKELRELEKVLKKES-ELIKLKELAEQLK---- 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1239 NAEKQVKqlEVQLADAQFKVDEMNRTLNDLDGGKKKLAVENSELQR------QLEESESQVAQLNKIKASLATQLEEAKR 1312
Cdd:PRK03918 507 ELEEKLK--KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKleelkkKLAELEKKLDELEEELAELLKELEELGF 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1313 MADEEARERAAILGKYRNLEHDLDNLRESVEEEQEAKADFQRQLSKANAEAQLWRSKYEsEGLARLEEL-----EEAKRK 1387
Cdd:PRK03918 585 ESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE-ELRKELEELekkysEEEYEE 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1388 LHGKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEVDKANALASSLEKRQKSFDKViAEWKAKVDDLAAEL-DASQ 1466
Cdd:PRK03918 664 LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERV-EELREKVKKYKALLkERAL 742
|
650
....*....|.
gi 556079866 1467 KECRNYSTEVF 1477
Cdd:PRK03918 743 SKVGEIASEIF 753
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
840-1480 |
2.75e-12 |
|
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: 72.46 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 840 VEDELKAMEEKLKKTEEALakeeklrkeleehnvkvLQEKNDLFLQLEAE-RMGAGDVEERLNKALTQKGDLESQLADLN 918
Cdd:pfam15921 243 VEDQLEALKSESQNKIELL-----------------LQQHQDRIEQLISEhEVEITGLTEKASSARSQANSIQSQLEIIQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 919 DR--------LSHEEDAHASLSQ-------SKKKLEGEISGLKKDI--EDMELALQKAEQDKATKDHQirNLNDEIQhqd 981
Cdd:pfam15921 306 EQarnqnsmyMRQLSDLESTVSQlrselreAKRMYEDKIEELEKQLvlANSELTEARTERDQFSQESG--NLDDQLQ--- 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 982 ELINKLNKEKKHL---QEASQKTSEDLQATEDKVNHLNKvkakleqtldELEDSLEREKKARGDIEKNKRKVEGDLklaQ 1058
Cdd:pfam15921 381 KLLADLHKREKELsleKEQNKRLWDRDTGNSITIDHLRR----------ELDDRNMEVQRLEALLKAMKSECQGQM---E 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1059 EAVADLEKNKKEMEQnlqrkekeMASLAAKLEDEQALvakLQKQIKELQARieeleeeleaeRQARAKAEKQRADLarei 1138
Cdd:pfam15921 448 RQMAAIQGKNESLEK--------VSSLTAQLESTKEM---LRKVVEELTAK-----------KMTLESSERTVSDL---- 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1139 eelserleesggaTSSQIELNKRREA---ELSKLRR--DLEESNLQHeqamsnlRKKHNDTVAEMSEQIDQLNKHKAKVE 1213
Cdd:pfam15921 502 -------------TASLQEKERAIEAtnaEITKLRSrvDLKLQELQH-------LKNEGDHLRNVQTECEALKLQMAEKD 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1214 KERATMSAEVSDLQSLLDHSNKAQANAEKQVKQLEVQLADAQFKVDEMnRTLNDLDGGKkklavenselqrqLEESESQV 1293
Cdd:pfam15921 562 KVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEF-KILKDKKDAK-------------IRELEARV 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1294 AQLNKIKASLATQLEEAKRMADEEARERAAILGKYRNLEHDLDNLRESVE----------EEQEAKAD-FQRQLSKANAE 1362
Cdd:pfam15921 628 SDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEvlkrnfrnksEEMETTTNkLKMQLKSAQSE 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1363 AQLWRSKYES----EGLAR-----LEELEEAKR----KLHGKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEVDK 1429
Cdd:pfam15921 708 LEQTRNTLKSmegsDGHAMkvamgMQKQITAKRgqidALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNK 787
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 556079866 1430 ANALASSLEKRQKSFDKVIAEWKAKVDDLAAELDASQKECRNYSTEVFKLR 1480
Cdd:pfam15921 788 MAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLK 838
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
760-1106 |
3.86e-12 |
|
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: 72.01 E-value: 3.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 760 FRAGVLGRLEEMrdERLSKIMTMIQAAVRwyickkhfqKLKEQRVALLVIQRNLRKFLQLRNWLWWKLYSKVkpllsaVR 839
Cdd:TIGR02168 668 TNSSILERRREI--EELEEKIEELEEKIA---------ELEKALAELRKELEELEEELEQLRKELEELSRQI------SA 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 840 VEDELKAMEEKLKKTEEALAKEEKLRKELEEHNVKVLQEKNDLFLQLEAERMGAGDVEERLNKALTQKGDLESQLADLND 919
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 920 RLSHEEDAHASLSQSKKKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLNDEIQHQDELINKLNKEKKHLQEASQ 999
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1000 KTSEDLQATEDKVNHLNKVKAKLEQTLDELEDSLE----REKKARGDIEKNKRKVEGDLKLAQEAVADLEKNKKEMEQNL 1075
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAqlelRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEA 970
|
330 340 350
....*....|....*....|....*....|.
gi 556079866 1076 QRKekemaslaakledeqalVAKLQKQIKEL 1106
Cdd:TIGR02168 971 RRR-----------------LKRLENKIKEL 984
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1021-1444 |
5.73e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.95 E-value: 5.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1021 KLEQTLDELEDsLEREKKARGDIEKNKRKVEGDLKLAQEAVADLEKNKKEMEQNLQRKEK--EMASLAAKLEDEQALVAK 1098
Cdd:COG4717 65 KPELNLKELKE-LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1099 LQKQIKELQARIEELEEELEAERQARAKAEKQRADLAREIEELSERLEESGGATSSQIELNKRREAELSKLRRDLEESNL 1178
Cdd:COG4717 144 LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1179 QHEQAMSNLRKKHndTVAEMSEQIDQLN-----------------KHKAKVEKERATMSAEVSDLQSLLDHSNKAQANAE 1241
Cdd:COG4717 224 ELEEELEQLENEL--EAAALEERLKEARlllliaaallallglggSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1242 KQVKQLEVQLADAQFKVDEMNRTLNDLDGGKKKLAVENSELQRQLEESESQVAQLNKIKASLATQLEEAKRMA------- 1314
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllaeagv 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1315 --DEEARERAAILGKYRNLEHDLDNLRESVEEEQEAKADFQRQLSKANAEAQLWRSKyeseglARLEELEEAKRKLHGKL 1392
Cdd:COG4717 382 edEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELE------EELEELEEELEELREEL 455
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 556079866 1393 QEAEEAMEQL--NAKCSGLEKTKSHLQGELEDMSIEVDKANALASSLEKRQKSF 1444
Cdd:COG4717 456 AELEAELEQLeeDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEY 509
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
929-1175 |
6.99e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.79 E-value: 6.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 929 ASLSQSKKKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLNDEIQHQDELINKLNKEkkhlqeasqktsedLQAT 1008
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE--------------LAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1009 EDKVNHLNKVKAKLEQTLDELEDSLEREKKArgdIEKNKRKVEGDLKLAQEAVADLEKNKKEMEQNLQRKEKEMASLAAK 1088
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRA---LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1089 LEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLAREIEelserleesggATSSQIELNKRREAELSK 1168
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA-----------ELAAELAELQQEAEELEA 227
|
....*..
gi 556079866 1169 LRRDLEE 1175
Cdd:COG4942 228 LIARLEA 234
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1193-1730 |
9.87e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 70.71 E-value: 9.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1193 DTVAEMSEQIDQLNKHKAKVEKERAtmsaEVSDLQSLLDHSNKAQANAEKQVKQ----LEVQLADAQFKVDEMNRTLNDL 1268
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDARE----QIELLEPIRELAERYAAARERLAELeylrAALRLWFAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1269 DGGKKKLAVENSELQRQLEESESQVAQL-NKIKASLATQLEEAKRMADEEARERAAILGKYRNLEHDLDNLRESVEEEQE 1347
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELeAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1348 akaDFQRQLSKANAEAQLWRskyeseglARLEELEEAKRKLHGKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMS--- 1424
Cdd:COG4913 381 ---EFAALRAEAAALLEALE--------EELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRdal 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1425 -----------------IEVDKANA------------LASSLEKRQKSFDKViAEW------------------------ 1451
Cdd:COG4913 450 aealgldeaelpfvgelIEVRPEEErwrgaiervlggFALTLLVPPEHYAAA-LRWvnrlhlrgrlvyervrtglpdper 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1452 -KAKVDDLAAELDASQKECRNYSTEVFKLRAAYE--ESQEHyesvkrenknLQDEVKDLMDQ-LGEGGRSVHELEK---- 1523
Cdd:COG4913 529 pRLDPDSLAGKLDFKPHPFRAWLEAELGRRFDYVcvDSPEE----------LRRHPRAITRAgQVKGNGTRHEKDDrrri 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1524 ---------SRKRLEmekeelqaaleeaeaaleqeenkVLRAQL-ELSQVRQEIDRRIQEKEEEFENTRKnHQRALDSMQ 1593
Cdd:COG4913 599 rsryvlgfdNRAKLA-----------------------ALEAELaELEEELAEAEERLEALEAELDALQE-RREALQRLA 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1594 ASLEAE--AKGKAEAL-RLKKKLE------SDINELEIALDHANKANAEAQKNLKKYQQNVKDLQGALEEEQRARDEARE 1664
Cdd:COG4913 655 EYSWDEidVASAEREIaELEAELErldassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556079866 1665 QYASAERRCNAMHGELEESRQLLASSKNSHLRHIEQMEGEellmQKKLRTEVIRLEDALVQVRKEY 1730
Cdd:COG4913 735 RLEAAEDLARLELRALLEERFAAALGDAVERELRENLEER----IDALRARLNRAEEELERAMRAF 796
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
925-1621 |
1.80e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.17 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 925 EDAHASLSQSKKKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLNDEIQHQDElinKLNKEKKHLQEAsqKTSED 1004
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDA---KRVEIARKAEDA--RKAEE 1168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1005 LQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKRKVEG-----DLKLAQEAVADLEKNKKEMEQNLQRKE 1079
Cdd:PTZ00121 1169 ARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEarkaeDAKKAEAVKKAEEAKKDAEEAKKAEEE 1248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1080 KEMASLAAKLEDEQALVAKLQKQIKELQARieeleeeleAERQARAKAEKQRADLAREIEELSERLEESGGATSSQIELN 1159
Cdd:PTZ00121 1249 RNNEEIRKFEEARMAHFARRQAAIKAEEAR---------KADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADE 1319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1160 KRREAELSK-----LRRDLEESNLQHEQAMSNLRKKHNDtvAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDHSN 1234
Cdd:PTZ00121 1320 AKKKAEEAKkkadaAKKKAEEAKKAAEAAKAEAEAAADE--AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK 1397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1235 KAQANAEKQVKQLEvQLADAQFKVDEMNRTLNDL---DGGKKKL--AVENSELQRQLEES-----------ESQVAQLNK 1298
Cdd:PTZ00121 1398 KKAEEDKKKADELK-KAAAAKKKADEAKKKAEEKkkaDEAKKKAeeAKKADEAKKKAEEAkkaeeakkkaeEAKKADEAK 1476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1299 IKASLATQLEEAKRMAdEEARERAAILGKYRNLEHDLDNLRESvEEEQEAKADFQRQLSKANAEAQLWRSKYESEGLARL 1378
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKA-EEAKKKADEAKKAAEAKKKADEAKKA-EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKA 1554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1379 EELEEAKRKlhGKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEVDKANALASSlEKRQKSFDKVIAEWKAKVDDL 1458
Cdd:PTZ00121 1555 EELKKAEEK--KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE-EAKKAEEAKIKAEELKKAEEE 1631
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1459 AAELDASQKECRNYSTEVFKLRAAYEESQEHYESVKR---ENKNLQDEVKDLMDQLGEGGRSVHELEKSRKRLEMEKEEL 1535
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKkaeEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1536 QAALEEAEAALEQEENKVLRAQlELSQVRQEIDRRIQE-KEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRLKKKLE 1614
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEENKIKAE-EAKKEAEEDKKKAEEaKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE 1790
|
....*..
gi 556079866 1615 SDINELE 1621
Cdd:PTZ00121 1791 KRRMEVD 1797
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1231-1982 |
2.38e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.78 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1231 DHSNKAQANAEKQVKQLE-VQLADAQFKVDEMNRTLNDLDGGKKKLAVENSELQRQLEESESQVAQLNKIKASLATQLEE 1309
Cdd:PTZ00121 1053 DGNHEGKAEAKAHVGQDEgLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEE 1132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1310 AKRMAD----EEAR--ERAAILGKYRNLEhDLDNLRESVEEEQEAKADFQRQLSKANAEAQLwRSKYESEGLARLEELEE 1383
Cdd:PTZ00121 1133 ARKAEDarkaEEARkaEDAKRVEIARKAE-DARKAEEARKAEDAKKAEAARKAEEVRKAEEL-RKAEDARKAEAARKAEE 1210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1384 AKRKLHGKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEVDKANALASSLEKRQKSFDKviAEWKAKVDDLAAELD 1463
Cdd:PTZ00121 1211 ERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK--AEEARKADELKKAEE 1288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1464 ASQKECRNYSTEVFK---LRAAYEESQEHYESVKR--ENKNLQDEVKDLMDQLGEGGRSVHELEKSRKRlEMEKEELQAA 1538
Cdd:PTZ00121 1289 KKKADEAKKAEEKKKadeAKKKAEEAKKADEAKKKaeEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD-EAEAAEEKAE 1367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1539 LEEAEAALEQEENKVLRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRLKKKLESDIN 1618
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAD 1447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1619 ELEIALDHANKAnaeaqKNLKKYQQNVKDLQGALE--EEQRARDEAREQYASAERRCNAMHGELEESRQLLASSKNSHLR 1696
Cdd:PTZ00121 1448 EAKKKAEEAKKA-----EEAKKKAEEAKKADEAKKkaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1697 HIEQMEGEEllmQKKLRTEVIRLEdalvQVRKEYEMLRIEFEQNLAATEQTGPINREMRHLITSLQSHNRQLKGEVSRYK 1776
Cdd:PTZ00121 1523 KADEAKKAE---EAKKADEAKKAE----EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE 1595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1777 RKLREAAAEAARLKQTLEMSNVAVSSTTVPSSASSTSSDNGSSRGEEGAPVScpQPGQGGREEGGTPSASSQRREEEARE 1856
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK--KAEELKKAEEENKIKAAEEAKKAEED 1673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1857 EEPIPEREKGKSDLdiiRDLKAQLKKSQEAQRELKlllDMYKGAPKEQRDKVQLMAAEKKARAEVEehrqQLKKLAEHER 1936
Cdd:PTZ00121 1674 KKKAEEAKKAEEDE---KKAAEALKKEAEEAKKAE---ELKKKEAEEKKKAEELKKAEEENKIKAE----EAKKEAEEDK 1743
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 556079866 1937 KERRKL-ADEDAMKKIRGLEETVASLHKSLTAQKQEVWEEALLSEME 1982
Cdd:PTZ00121 1744 KKAEEAkKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE 1790
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
895-1155 |
2.39e-11 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 67.93 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 895 DVEERLNKALTQKGDLESQLADLNDRLsheedahASLSQSKKKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLN 974
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAEL-------EELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 975 DEIQHQDELINKLNkekkhlqeaSQKTSEDLQATEDKVNHLNKVKAKLEQTLDELedslereKKARGDIEKNKRKVEGDL 1054
Cdd:COG3883 93 RALYRSGGSVSYLD---------VLLGSESFSDFLDRLSALSKIADADADLLEEL-------KADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1055 KLAQEAVADLEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADL 1134
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
250 260
....*....|....*....|.
gi 556079866 1135 AREIEELSERLEESGGATSSQ 1155
Cdd:COG3883 237 AAAAAAAASAAGAGAAGAAGA 257
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
832-1327 |
3.89e-11 |
|
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: 68.66 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 832 KPLLSAVRVEDELKAMEEKLKKTEEALAKEEKLRKELEEHN---VKVLQEKNDLFLQLEAER--MGAGDVEERlNKALTQ 906
Cdd:pfam01576 552 RELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQrqlVSNLEKKQKKFDQMLAEEkaISARYAEER-DRAEAE 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 907 KGDLESQLADLNDRLSHEEDAHASLSQSKKKLEGEISGL-------KKDIEDMELALQKAEQDKATKDHQIRNLNDEIQH 979
Cdd:pfam01576 631 AREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLvsskddvGKNVHELERSKRALEQQVEEMKTQLEELEDELQA 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 980 QDEliNKLNKEKkHLQEASQKTSEDLQATEDKVNhlnKVKAKLEQTLDELEDSLEREKKARGDIEKNKRKVEGDLKLAQE 1059
Cdd:pfam01576 711 TED--AKLRLEV-NMQALKAQFERDLQARDEQGE---EKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEA 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1060 AVADLEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKL-------QKQIKELQARIEELEEELEAERQARAKAEKQRA 1132
Cdd:pfam01576 785 QIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEIlaqskesEKKLKNLEAELLQLQEDLAASERARRQAQQERD 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1133 DLAREIEELSERLeesggatSSQIELNKRREAELSKLRRDLEESNLQHEQAMSNLRKK-------HNDTVAEMS------ 1199
Cdd:pfam01576 865 ELADEIASGASGK-------SALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKStlqveqlTTELAAERStsqkse 937
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1200 ---EQIDQLNKH------------KAKVEKERATMSAEVSDLQSLLDHSNKAQANAEKQVKQLEVQLADAQFKVDEMNRT 1264
Cdd:pfam01576 938 sarQQLERQNKElkaklqemegtvKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRH 1017
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556079866 1265 LNDLDGGKKKLAVENSELQRQLEESESQVAQLNKIKASLATQLEEAKRMADEEARERAAILGK 1327
Cdd:pfam01576 1018 ADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1267-1647 |
5.49e-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: 68.17 E-value: 5.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1267 DLDGGKKKLAVENSELQRQLEESESQVAQLNKIKASLATQLEEAKRMAD--EEARERAA--ILGKYRNLEHDLDNLRESV 1342
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQAllKEKREYEGyeLLKEKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1343 EEEQEAKADFQRQLSKANAEAQlwrskyesEGLARLEELEEAKRKLHGKLQEA-EEAMEQLNAKCSGLEKTKSHLQGELE 1421
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLE--------EIEQLLEELNKKIKDLGEEEQLRvKEKIGELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1422 DMSIEVDKANALASSLEKRQKSFDKVIAEWKAKVDDLAAELDASQKEcrnystevfklraaYEESQEHYESVKRENKNLQ 1501
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE--------------LEDLRAELEEVDKEFAETR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1502 DEVKDLMDQLGEGGRSVHELEKSRKRLEMEKEelqaaleeaeaaleqeenkvlRAQLELSQVRQEIdRRIQEKEEEFENT 1581
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQ---------------------RLSEELADLNAAI-AGIEAKINELEEE 442
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556079866 1582 RKNHQRALDSMQASLEAEAKGKAEALRLKKKLESDINELEIALDHANKANAEAQKNLKKYQQNVKD 1647
Cdd:TIGR02169 443 KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
843-1130 |
7.28e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 67.82 E-value: 7.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 843 ELKAMEEKLKKTEEALAKEEKLRKELEEHNVKVLQEKNDLFLQLEAERMGAGDVEERLNKALTQKGDLESQLADLNDRLs 922
Cdd:pfam05483 472 EVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDEL- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 923 heEDAHASLSQSKKKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLNDEIQHQDELINKLNKEKKHLQEASQKTS 1002
Cdd:pfam05483 551 --ESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAEN 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1003 EDLQATEDKVN----HLNKVKAKLEQTLD----ELEDSLEREKKARGDIEKNKRKVEGDLKLAQE-----------AVAD 1063
Cdd:pfam05483 629 KQLNAYEIKVNklelELASAKQKFEEIIDnyqkEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEidkrcqhkiaeMVAL 708
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556079866 1064 LEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQ 1130
Cdd:pfam05483 709 MEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKME 775
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1871-2147 |
8.06e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 8.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1871 DIIRDLKAQLKK-SQEAQ-----RELKllldmykgAPKEQRDKVQLMAAEKKARAEVEEHRQQLKKLAEHERKERRKLAD 1944
Cdd:COG1196 193 DILGELERQLEPlERQAEkaeryRELK--------EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1945 EDAmkKIRGLEETVASLHKSLTAQKQEvwEEALLSEMEVTGQAFEDMQEQNLRLIQQLREKDDANFKLMSERIKSNQIHK 2024
Cdd:COG1196 265 LEA--ELEELRLELEELELELEEAQAE--EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 2025 LLQEEKAMLSEQGATLQAQVEAQNQVVRKLEEKERLLQNSLSTLEKELSLRQQAAEMHRRKAVESAQSAADLKLHLEKYL 2104
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 556079866 2105 AQLKDAQGIVTDRTAVLSQETFKTKRLQEEILSLRRKVERAKK 2147
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1280-1688 |
9.13e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.37 E-value: 9.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1280 SELQRQLEESESQ--VAQLNKIKASLATQLEEAKRMadEEARERAA--------ILGKYRNLEHDLDNLRESVEEEQEAK 1349
Cdd:PRK02224 190 DQLKAQIEEKEEKdlHERLNGLESELAELDEEIERY--EEQREQARetrdeadeVLEEHEERREELETLEAEIEDLRETI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1350 ADFQRQLSKANAEAQLWRskyeseglARLEELEEAKRKLHGKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEVDK 1429
Cdd:PRK02224 268 AETEREREELAEEVRDLR--------ERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1430 ANALASSLEKRQKSFDKVIAEWKAKVDDLAAELDASQKECRNYSTEVFKLRAAYEESQEHYESVKRENKNLQDEVKDLMD 1509
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1510 QLGEGGRSVHELEKSRKRLE---------------------MEKEELQAALEEAEAALEQEENKVLRAQLELSQVRQEID 1568
Cdd:PRK02224 420 ERDELREREAELEATLRTARerveeaealleagkcpecgqpVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1569 RRIQEKE-----EEFENTRKNHQRALDSMQASLEAEAKgKAEALRLKKklesdiNELEIALDHANKANAEAQKNLKKYQQ 1643
Cdd:PRK02224 500 RAEDLVEaedriERLEERREDLEELIAERRETIEEKRE-RAEELRERA------AELEAEAEEKREAAAEAEEEAEEARE 572
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 556079866 1644 NVKDLQGALEEEQRARDEAREQYASAERRCNAMH--GELEESRQLLA 1688
Cdd:PRK02224 573 EVAELNSKLAELKERIESLERIRTLLAAIADAEDeiERLREKREALA 619
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1241-2147 |
1.44e-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: 67.12 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1241 EKQVKQLEVQLADAQFKVDEMNRTLNDLDGGKKKLAVENSELQRQLE-------ESESQVAQLNKIKASLATQLEEAKRM 1313
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQaetelcaEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1314 ADEEARERAAILGKYRNLEHDLDNLRESVEEEQEAKADFQrqLSKANAEAQLwrsKYESEGLARLEE----LEEAKRKLH 1389
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQ--LEKVTTEAKI---KKLEEDILLLEDqnskLSKERKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1390 GKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEVDKANALASSLEKRQKSFDKVIAEWKAKVDDLAAELDASQKEC 1469
Cdd:pfam01576 159 ERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1470 RNYSTEVFKLRAAYEESQEHYESVKRENKNLQDEVKDLMDQLGEGGRSVHELEKSRKRLEMEKEELQAALEEAEAALEQE 1549
Cdd:pfam01576 239 AKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1550 ENKVLRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRLKKKLESDINELEIALDHANK 1629
Cdd:pfam01576 319 QELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1630 ANAEAQKNLKKYQQNVKDLQGALEEEQRARDEAREQYASAERRCNAMHGELEESRQLL------ASSKNSHLRHIEQMEG 1703
Cdd:pfam01576 399 AKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNiklskdVSSLESQLQDTQELLQ 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1704 EELLMQKKLRTEVIRLEDALVQVRkeyEMLRIEFEQNLAATEQtgpinremrhlitsLQSHNRQLkgevSRYKRKlreaa 1783
Cdd:pfam01576 479 EETRQKLNLSTRLRQLEDERNSLQ---EQLEEEEEAKRNVERQ--------------LSTLQAQL----SDMKKK----- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1784 aeaarlkqtLEMSNVAVSSttvpssasstssdngssrGEEGAPvscpqpgqggREEGGTPSASSQRREEEAREEEPIPER 1863
Cdd:pfam01576 533 ---------LEEDAGTLEA------------------LEEGKK----------RLQRELEALTQQLEEKAAAYDKLEKTK 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1864 EKGKSDLDiirdlkaQLKKSQEAQRELKLLLDmykgapKEQRDKVQLMAAEKKARAEVEEHRQQLKklAEHERKERRKLA 1943
Cdd:pfam01576 576 NRLQQELD-------DLLVDLDHQRQLVSNLE------KKQKKFDQMLAEEKAISARYAEERDRAE--AEAREKETRALS 640
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1944 DEDAMKKIRGLEETVASLHKSLTAQKqevweEALLSEMEVTG--------------QAFEDMQEQNLRLIQQLREKDDAN 2009
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEM-----EDLVSSKDDVGknvhelerskraleQQVEEMKTQLEELEDELQATEDAK 715
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 2010 FKLMSERiksnqihkllqeeKAMLSEQGATLQAQVEAQnqvvrklEEKERLLQNSLSTLEKEL--SLRQQAAEMHRRKAV 2087
Cdd:pfam01576 716 LRLEVNM-------------QALKAQFERDLQARDEQG-------EEKRRQLVKQVRELEAELedERKQRAQAVAAKKKL 775
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556079866 2088 ESAQSaaDLKLHL-------EKYLAQLKDAQGIVTDrtavLSQETFKTKRLQEEILSLRRKVERAKK 2147
Cdd:pfam01576 776 ELDLK--ELEAQIdaankgrEEAVKQLKKLQAQMKD----LQRELEEARASRDEILAQSKESEKKLK 836
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1569-2144 |
2.36e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1569 RRIQEKEEEFENTRKnhQRALDSMQASLEAEAKGKAEALRLKKKLESDINELEIALDHANKANAEAQKNLKKYQQNVKDL 1648
Cdd:COG1196 216 RELKEELKELEAELL--LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1649 QGALEEEQRARDEAREQYASAERRCNAMHGELEE--SRQLLASSKNSHLRHIEQMEGEELLMQKKLRTEVIRLEDALVQV 1726
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAEleEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1727 RKEYEMLRIEFEQNLAATEQTgpiNREMRHLITSLQSHNRQLKGEVSRYKRKLREAAAEAARLKQTLEMSNVAVSSTTVP 1806
Cdd:COG1196 374 LAEAEEELEELAEELLEALRA---AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1807 SSASSTSSDNGSSRGEEgapvscpqpgQGGREEGGTPSASSQRREEEAREEEPIPEREKGKSDLDIIRDLKAQLKKSQea 1886
Cdd:COG1196 451 EAELEEEEEALLELLAE----------LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG-- 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1887 QRELKLLLDMYKGAPKEQRDKVQLmAAEKKARAEVEEHRQQLKKLAEHERKERRKLADEDAMKKIRGLEETVASLHKSLT 1966
Cdd:COG1196 519 LRGLAGAVAVLIGVEAAYEAALEA-ALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1967 AQKQEVWEEALLSEMEVTGQAFEDMQEQNL---RLIQQLREKDDANFKLMSERIKSNQIHKLLQEEKAMLSEQGATLQAQ 2043
Cdd:COG1196 598 GAAVDLVASDLREADARYYVLGDTLLGRTLvaaRLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEA 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 2044 VEAQNQVVRKLEEKERLLQNSLSTLEKELSLRQQAAEMHRRKAVESAQSAADLKLHLEKYLAQLKDAQGIVTDRTAVLSQ 2123
Cdd:COG1196 678 EAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELP 757
|
570 580
....*....|....*....|.
gi 556079866 2124 ETFKTKRLQEEILSLRRKVER 2144
Cdd:COG1196 758 EPPDLEELERELERLEREIEA 778
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
904-1735 |
2.39e-10 |
|
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: 66.22 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 904 LTQKGDLESQLADLNDRLSHEEDAHASLSQSKKK-LEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLNDEIQHQDE 982
Cdd:TIGR00606 261 LSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKvFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQ 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 983 LINKLNKEKKHLQEASQKTSEDLQATEDKVNHLnkvkaKLEQTLDELEDSLEREKKARGDIEKNKRKVEGDLKLAQEAVA 1062
Cdd:TIGR00606 341 EKTELLVEQGRLQLQADRHQEHIRARDSLIQSL-----ATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCA 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1063 DLEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLAREIEels 1142
Cdd:TIGR00606 416 DLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEK--- 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1143 erleesggatSSQIELNKRREAELSKLRRDLEESNLQHEQAMSNLrKKHNDTVAEMSeqidqlnkhkaKVEKERATMSAE 1222
Cdd:TIGR00606 493 ----------NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQL-NHHTTTRTQME-----------MLTKDKMDKDEQ 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1223 VSDLQSLLDHSNKAQANAEKQVKQLEVQLADAQFKVDEMNRTLNDLDGGKKKLAVENSELQRQLEESESQVaqlnkikAS 1302
Cdd:TIGR00606 551 IRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQL-------SS 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1303 LATQLEEAKRMADEEAreraailgkyrnlehDLDNLRESVEEEQEAKAdfqrQLSKANA--EAQLWRSKYESEGLARL-- 1378
Cdd:TIGR00606 624 YEDKLFDVCGSQDEES---------------DLERLKEEIEKSSKQRA----MLAGATAvySQFITQLTDENQSCCPVcq 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1379 ------EELEEAKRKLHGKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEVDKANALASSLEKRQKSFDKVIAEWK 1452
Cdd:TIGR00606 685 rvfqteAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLK 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1453 AKVDD---LAAELDASQKECRNYSTEVFKLRAAYEESQEHYESVKRENKNLQDEvkdlmdqlgEGGRSVHEL--EKSRKR 1527
Cdd:TIGR00606 765 NDIEEqetLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGS---------DLDRTVQQVnqEKQEKQ 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1528 LEMEKEELQAALEEAEAALEQEENKVLRAQL-ELSQVRQEIDRRIQEKEEEFENTrknhQRALDSMQASLEAEAKGKAEA 1606
Cdd:TIGR00606 836 HELDTVVSKIELNRKLIQDQQEQIQHLKSKTnELKSEKLQIGTNLQRRQQFEEQL----VELSTEVQSLIREIKDAKEQD 911
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1607 LRLKKKLESDINELEIALDHANKANAEAQKNLKKYQQNVKDLQGALEE-EQRARDEAREQYASAERRCNAMHGELEESRQ 1685
Cdd:TIGR00606 912 SPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDiENKIQDGKDDYLKQKETELNTVNAQLEECEK 991
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 556079866 1686 --------LLASSKNSHLRHIEQMEGEELLMQKKLRTEVIRLEDALVQVRKEYEMLRI 1735
Cdd:TIGR00606 992 hqekinedMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQV 1049
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
955-1368 |
2.72e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.56 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 955 ALQKAEQDKATKDHQIRNLNDEIQHQDELINKLNKEKKHLQEASQKTSEDLQATED--KVNHLNKVKAKLEQTLDELEDS 1032
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1033 LEREKKARGDIEKNKRKVEgdlKLAQEAVADLEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEE 1112
Cdd:COG4717 155 LEELRELEEELEELEAELA---ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1113 LEEELEAERQARAKAEKQR--------ADLAREIEELSERLEESGGATSSQIEL-----------NKRREAELSKLRRDL 1173
Cdd:COG4717 232 LENELEAAALEERLKEARLllliaaalLALLGLGGSLLSLILTIAGVLFLVLGLlallflllareKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1174 EESNLQHEQAMSNLRKKHNDTVAEMSEQIDQLNKHKAKVEKERATMSAEvsdlqslldhsnkAQANAEKQVKQLEVQLAD 1253
Cdd:COG4717 312 ALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE-------------EELQLEELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1254 AQFKVDEMNRTLNDLDGGKKKLAVENSELQRQLEESESQVAQLNKI--KASLATQLEEAKRMADEEARERAAILGKYRNL 1331
Cdd:COG4717 379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAldEEELEEELEELEEELEELEEELEELREELAEL 458
|
410 420 430
....*....|....*....|....*....|....*..
gi 556079866 1332 EHDLDNLRESvEEEQEAKADFQRQLSKANAEAQLWRS 1368
Cdd:COG4717 459 EAELEQLEED-GELAELLQELEELKAELRELAEEWAA 494
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1038-1268 |
4.46e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.01 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1038 KARGDIEKNKRKVEGDLKLAQEAVADLEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIeeleeel 1117
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1118 eaeRQARAKAEKQRADLAReieeLSERLEESGGATSSQIELNKRREAELSKLRRDLEESNLQHEQAMSNLRKkhndTVAE 1197
Cdd:COG4942 93 ---AELRAELEAQKEELAE----LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRA----DLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556079866 1198 MSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDHSNKAQANAEKQVKQLEVQLADAQFKVDEMNRTLNDL 1268
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1199-1768 |
5.90e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 64.99 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1199 SEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDHSNKAQANAEKQVKQLEVQLADAQFKVDEMNRTLNDLDgGKKKLAVE 1278
Cdd:TIGR00618 183 LMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQE-EQLKKQQL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1279 NSELQRQLEESESQVAQLNKIKASLATQ------LEEAKRMAD-------------EEARERAAILGKYRNLEHDldnlR 1339
Cdd:TIGR00618 262 LKQLRARIEELRAQEAVLEETQERINRArkaaplAAHIKAVTQieqqaqrihtelqSKMRSRAKLLMKRAAHVKQ----Q 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1340 ESVEEEQEAKADFQRQ---LSKANAEAQLWRSKYESEglarLEELEeakrKLHGKLQEAEEAMEQLNAKCSGLEK-TKSH 1415
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQeihIRDAHEVATSIREISCQQ----HTLTQ----HIHTLQQQKTTLTQKLQSLCKELDIlQREQ 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1416 LQGELEDMSIEVDKAN-ALASSLEKRQKSFDKVIAEWKAKV-DDLAAELDASQKECRNYSTEVFKLRAA------YEESQ 1487
Cdd:TIGR00618 410 ATIDTRTSAFRDLQGQlAHAKKQQELQQRYAELCAAAITCTaQCEKLEKIHLQESAQSLKEREQQLQTKeqihlqETRKK 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1488 EHYESVKRENKNLQDEVKD----------LMDQLGEGGRSVHELEKSRKRLEMEKEELQAALEEAEAALEQEENKVLRAQ 1557
Cdd:TIGR00618 490 AVVLARLLELQEEPCPLCGscihpnparqDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQ 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1558 LELSQVRQeidrRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRLKKKLESDINELEIALDHANKANAEAQKN 1637
Cdd:TIGR00618 570 QSFSILTQ----CDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKL 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1638 LKKYQQNVKDLQG----------ALEEEQRARDEAREQYASAERRCNAMHGELEESRQLLASSKNSHL----RHIEQMEG 1703
Cdd:TIGR00618 646 TALHALQLTLTQErvrehalsirVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIeeydREFNEIEN 725
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556079866 1704 EELLMQKKLRTEvirlEDALVQVRKEYEMLR---------IEFEQNLAAT--EQTGpinREMRHLITSLQSHNRQL 1768
Cdd:TIGR00618 726 ASSSLGSDLAAR----EDALNQSLKELMHQArtvlkarteAHFNNNEEVTaaLQTG---AELSHLAAEIQFFNRLR 794
|
|
| RING-HC |
cd16449 |
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ... |
2169-2209 |
7.18e-10 |
|
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers. Some have a different Cys/His pattern. Some lack a single Cys or His residue at typical Zn ligand positions, especially, the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can chelate Zn in a RING finger as well. This family corresponds to the HC subclass of RING (RING-HC) fingers that are characterized by containing C3HC4-type canonical RING-HC fingers or noncanonical RING-HC finger variants, including C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type modified RING-HC fingers. The canonical RING-HC finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-HC fingers can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle, and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.
Pssm-ID: 438113 [Multi-domain] Cd Length: 41 Bit Score: 55.95 E-value: 7.18e-10
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 556079866 2169 LTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYETRQRKCPKC 2209
Cdd:cd16449 1 LECPICLERLKDPVLLPCGHVFCRECIRRLLESGSIKCPIC 41
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
797-1718 |
7.27e-10 |
|
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: 64.68 E-value: 7.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 797 QKLKEQRVALLVIQRNLRKFLQLRNWLWWKLYSKVKPLLSAVRVEDELKAMEEKLKKTEEALAKEEKLRKELEEHNVKVL 876
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 877 QEKND-LFLQLEAERMGAGdVEERLNKALTQKG----DLESQLADLNDRLSHEEDAHASLSQSKKKLEGEISGLKKDIED 951
Cdd:TIGR00606 280 QMEKDnSELELKMEKVFQG-TDEQLNDLYHNHQrtvrEKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 952 MELALQKaeQDKATKDHQIRNLNDEIQH---QDELINKLNKEKKHLQEASQKTSEDLqatedkVNHLNKVKAKLEQTLDE 1028
Cdd:TIGR00606 359 HQEHIRA--RDSLIQSLATRLELDGFERgpfSERQIKNFHTLVIERQEDEAKTAAQL------CADLQSKERLKQEQADE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1029 LEDslerEKKARGDIEKNKRkvegdlklaqeavadlEKNKKEMEQnLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQA 1108
Cdd:TIGR00606 431 IRD----EKKGLGRTIELKK----------------EILEKKQEE-LKFVIKELQQLEGSSDRILELDQELRKAERELSK 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1109 RIEELEEELEAERQARAKAEKQRADLAREIEELSERLEESGGATSSQIELNKRREAELSKLRRDLeesNLQHEQAMSNLR 1188
Cdd:TIGR00606 490 AEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKI---KSRHSDELTSLL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1189 KKHNDTvAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDHSNKAQANAEKQVKQLEVQLADA----QFKVD----- 1259
Cdd:TIGR00606 567 GYFPNK-KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsqDEESDlerlk 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1260 -EMNRTLNDLDGGKKKLAVENSELQRQLEESES----------QVAQLNKIKASL-------ATQLEEAKRMADEEARER 1321
Cdd:TIGR00606 646 eEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpvcqrvfqTEAELQEFISDLqsklrlaPDKLKSTESELKKKEKRR 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1322 AAILGKYRNLEHDLD----NLRESVEEEQEAKADFQRQLSKANAEAQLWRSKYESEGLARLEELE-EAKRKLHGKLQEAE 1396
Cdd:TIGR00606 726 DEMLGLAPGRQSIIDlkekEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDvTIMERFQMELKDVE 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1397 EAMEQLNAKCSG--LEKTKSHLQGELEDMSIEVDKANALASSLEKRQKSFDKVIAEWKAKVDDLAAEldasqkecRNYST 1474
Cdd:TIGR00606 806 RKIAQQAAKLQGsdLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE--------KLQIG 877
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1475 EVFKLRAAYEESQEhyesvkrenkNLQDEVKDLMDQLGEGGRSVHELEKSRKRLEMEKEELQAALEEAEAALEQEENKVL 1554
Cdd:TIGR00606 878 TNLQRRQQFEEQLV----------ELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIK 947
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1555 RAQLELSQVRQEIDRRIQEKEEEFENTRKNHqraLDSMQASLEaeakgkaEALRLKKKLESDINELEIALDHANKANAEA 1634
Cdd:TIGR00606 948 EKVKNIHGYMKDIENKIQDGKDDYLKQKETE---LNTVNAQLE-------ECEKHQEKINEDMRLMRQDIDTQKIQERWL 1017
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1635 QKNLKKYQQNVKDLQgaLEEEQRARDEAREQYASAERRcnAMHGELEESRQLLASSKNSHLRHIEQMEGEELLMQKKLRT 1714
Cdd:TIGR00606 1018 QDNLTLRKRENELKE--VEEELKQHLKEMGQMQVLQMK--QEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE 1093
|
....
gi 556079866 1715 EVIR 1718
Cdd:TIGR00606 1094 PQFR 1097
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1559-2108 |
1.25e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1559 ELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRLKKKLESDINELEIALDHANKANAEAQKNL 1638
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1639 KKYQQNVKDLQgALEEEQRARDEAREQYASAERRCNAMHGELEESRQLLASSKNSHLRHIEQMEGEELLMQKKLRTEVIR 1718
Cdd:COG1196 330 EELEELEEELE-ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1719 LEDALVQVRKEYEMLRIEFEQNLAATEQTGPINREMRHLITSLQSHNRQLKGEVSRYKRKLREAAAEAARLKQTLEMSNV 1798
Cdd:COG1196 409 EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1799 AVSSTTVPSSASSTSSDNGSSRGEEGAPVSCPQPGQGGREEGGTPSASSQRREEEAREEEPIPEREKGKSDLDIIRDLKA 1878
Cdd:COG1196 489 AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKA 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1879 QLkksqeAQRELKLLLDMYKGAPKEQRDKVQLMAAEKKARAEVEEHRQQLKKLAEHERKERRKLADEDAMKKIRGLEETV 1958
Cdd:COG1196 569 AK-----AGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLA 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1959 ASLHKSLTAQkqevwEEALLSEMEVTGQAFEDMQEQNLRLIQQLREKDdanfklmseriksnQIHKLLQEEKAMLSEQGA 2038
Cdd:COG1196 644 GRLREVTLEG-----EGGSAGGSLTGGSRRELLAALLEAEAELEELAE--------------RLAEEELELEEALLAEEE 704
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 2039 TLQAQVEAQNQVVRKLEEKERLLQNSLSTLEKELSLRQQAAEMHRRKAVESAQSAADLKlHLEKYLAQLK 2108
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE-ELERELERLE 773
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1163-1361 |
1.54e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 63.11 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1163 EAELSKLRRDLEESnlqhEQAMSNLRKKHNDTVAE-----MSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDHSNKA- 1236
Cdd:COG3206 181 EEQLPELRKELEEA----EAALEEFRQKNGLVDLSeeaklLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDAl 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1237 -QANAEKQVKQLEVQLADAQFKVDEMNRTLND-----------LDGGKKKLAvenSELQRQLEESESQVAQLNKIKASLA 1304
Cdd:COG3206 257 pELLQSPVIQQLRAQLAELEAELAELSARYTPnhpdvialraqIAALRAQLQ---QEAQRILASLEAELEALQAREASLQ 333
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 556079866 1305 TQLEEAKrmadEEARERAAILGKYRNLEHDLDNLRESVEE--EQEAKADFQRQLSKANA 1361
Cdd:COG3206 334 AQLAQLE----ARLAELPELEAELRRLEREVEVARELYESllQRLEEARLAEALTVGNV 388
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
823-1637 |
1.85e-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: 63.20 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 823 LWWKLYSKVKPLLS-AVRVEDELKAMEEKLKKTEEALAKEEKLRKELEEHNVKV-------LQEKNDLFLQLEAERMGAG 894
Cdd:pfam05483 79 LYSKLYKEAEKIKKwKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVslkleeeIQENKDLIKENNATRHLCN 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 895 DVEERLNKALTQKGDLESQ-------LADLNDRLSHEEDAHASLSQSKKKLEGEIS-GLKKDIEDMELALQKAEQDKATK 966
Cdd:pfam05483 159 LLKETCARSAEKTKKYEYEreetrqvYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYKKEINDK 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 967 DHQIRNLNDEIQHQDELINKLNKEKKHLQEASQKTSEDLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKkargdieKN 1046
Cdd:pfam05483 239 EKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSM-------ST 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1047 KRKVEGDLKLAQEAVADLEKNKkemEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAK 1126
Cdd:pfam05483 312 QKALEEDLQIATKTICQLTEEK---EAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQK 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1127 AEKQRADLAReieelserleesggatssqieLNKRREAELSKLRRDLEEsnlqheqamsnlrkkhNDTVAEMSEQIDQLN 1206
Cdd:pfam05483 389 KSSELEEMTK---------------------FKNNKEVELEELKKILAE----------------DEKLLDEKKQFEKIA 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1207 KHKAKVEKERA----TMSAEVSDLQSLLDHSNKAQANAEKQVKQLEVQLADAQFKVDEMNRTLNDLDGGKKKLAVENSEL 1282
Cdd:pfam05483 432 EELKGKEQELIfllqAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDM 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1283 QRQLEESESQVAQLNKIKASLATQLEEAKRMadeeareraailgkyrnlEHDLDNLRESVEEEQEAKADfqrqlskanae 1362
Cdd:pfam05483 512 TLELKKHQEDIINCKKQEERMLKQIENLEEK------------------EMNLRDELESVREEFIQKGD----------- 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1363 aqlwrskyesEGLARLEELEEAKRKLHGKLQEAEEAMEQLNAKCSGLEKtkshlqgELEDMSIEVDKANALASSLEKRQK 1442
Cdd:pfam05483 563 ----------EVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKK-------QIENKNKNIEELHQENKALKKKGS 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1443 SFDKVIAEWKAKVDDLAAELDASQKEcrnystevfklraaYEESQEHYESvKRENKNLQDEvkDLMDQLGEGGRSVHELE 1522
Cdd:pfam05483 626 AENKQLNAYEIKVNKLELELASAKQK--------------FEEIIDNYQK-EIEDKKISEE--KLLEEVEKAKAIADEAV 688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1523 KSRKRLEMEkeelqaaleeaeaaleqEENKVLRAQLELSQVRQEIDRRIQEKEEEFeNTRKNHQRALDSMQASLEAEAKG 1602
Cdd:pfam05483 689 KLQKEIDKR-----------------CQHKIAEMVALMEKHKHQYDKIIEERDSEL-GLYKNKEQEQSSAKAALEIELSN 750
|
810 820 830
....*....|....*....|....*....|....*.
gi 556079866 1603 -KAEALRLKKKLESDINELEialdhanKANAEAQKN 1637
Cdd:pfam05483 751 iKAELLSLKKQLEIEKEEKE-------KLKMEAKEN 779
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
896-1508 |
2.12e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 63.32 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 896 VEERLNKALTQKGDLESQLADLNDRLSHEEDAhasLSQSKKKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLND 975
Cdd:pfam12128 274 IASRQEERQETSAELNQLLRTLDDQWKEKRDE---LNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLP 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 976 EIQHQdelINKLNKEKKHLQEASQKTSEDLQATEDKVNhlnkvkaklEQTLDELEDSLEREKKARGDIEKNKRKVEGDLK 1055
Cdd:pfam12128 351 SWQSE---LENLEERLKALTGKHQDVTAKYNRRRSKIK---------EQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1056 lAQEAVADLEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVA-KLQKQIKELQARIEELEEELEaerQARAKAEKQRADL 1134
Cdd:pfam12128 419 -ALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATpELLLQLENFDERIERAREEQE---AANAEVERLQSEL 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1135 AREIeelserleesgGATSSQIELNKRREAELSKLRRDLEESNLQHEQAMSNLRKKHNDTVAEMSEQI------------ 1202
Cdd:pfam12128 495 RQAR-----------KRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIgkvispellhrt 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1203 ------------DQLNKHKAKVEKER----------ATMSAEVSDLQSLLDHSNKAQANAEKQVKQLEVQLADAQFKVDE 1260
Cdd:pfam12128 564 dldpevwdgsvgGELNLYGVKLDLKRidvpewaaseEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETF 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1261 MNRTLNDLDGGKKKLAVENSELQRQLEES--------ESQVAQLNKIKASLATQLEEAKRMADEEARE-RAAILGKYRNL 1331
Cdd:pfam12128 644 ARTALKNARLDLRRLFDEKQSEKDKKNKAlaerkdsaNERLNSLEAQLKQLDKKHQAWLEEQKEQKREaRTEKQAYWQVV 723
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1332 EHDLDN----LRESVEEEQEAKADFQRQLSKANAEaQLWRSKYESEGLARLE-ELEEAKRKLHGKLQEAEEAME------ 1400
Cdd:pfam12128 724 EGALDAqlalLKAAIAARRSGAKAELKALETWYKR-DLASLGVDPDVIAKLKrEIRTLERKIERIAVRRQEVLRyfdwyq 802
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1401 --------QLNAKCSGLEKTKSHLQGELEDMSIEV--------------DKANALASSLEKRQKSFDKVIAEWkaKVDDL 1458
Cdd:pfam12128 803 etwlqrrpRLATQLSNIERAISELQQQLARLIADTklrraklemerkasEKQQVRLSENLRGLRCEMSKLATL--KEDAN 880
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 556079866 1459 AAELDASQKECRNYSTEvFKLRAAYEEsqehyESVKRENKNLQDEVKDLM 1508
Cdd:pfam12128 881 SEQAQGSIGERLAQLED-LKLKRDYLS-----ESVKKYVEHFKNVIADHS 924
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
911-1155 |
2.12e-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: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 911 ESQLADLNDRLSheedahaSLSQSKKKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLNDEIQHQDELINKLNKE 990
Cdd:COG3883 15 DPQIQAKQKELS-------ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 991 KKHLQEASQKT------------SEDLQATEDKVNHLNKVKAKLEQTLDELEDslerekkargdieknkrkvegDLKLAQ 1058
Cdd:COG3883 88 LGERARALYRSggsvsyldvllgSESFSDFLDRLSALSKIADADADLLEELKA---------------------DKAELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1059 EAVADLEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLAREI 1138
Cdd:COG3883 147 AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
250
....*....|....*..
gi 556079866 1139 EELSERLEESGGATSSQ 1155
Cdd:COG3883 227 AAAAAAAAAAAAAAAAA 243
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
841-1529 |
2.77e-09 |
|
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: 62.68 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 841 EDELKAMEEKLKKTEEALAKeeklrkeleehnvkvLQEKNDLFLQLEAERMGAGDVEERLNKALTQKGDLESQLADLN-- 918
Cdd:TIGR00618 225 EKELKHLREALQQTQQSHAY---------------LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINra 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 919 ---DRLSHEEDAHASLSQSKKKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLNDEIQHQDELINKLNKEKKHLQ 995
Cdd:TIGR00618 290 rkaAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIRE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 996 EASQKTS---------EDLQATEDKVNHLnkvkAKLEQTLDELEDSLEREKKARGDIEKNKRKVEGDLKLAQEAVADLEK 1066
Cdd:TIGR00618 370 ISCQQHTltqhihtlqQQKTTLTQKLQSL----CKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1067 NKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKelqarieeleeeleaeRQARAKAEKQradlareieelserle 1146
Cdd:TIGR00618 446 AITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHL----------------QETRKKAVVL---------------- 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1147 esggatssqielnkRREAELSKLRRDLEESNLQHEQAMSNLRKKHNDTvAEMSEQIDQLNKHKAKVEKERATMSAEVSDL 1226
Cdd:TIGR00618 494 --------------ARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLT-RRMQRGEQTYAQLETSEEDVYHQLTSERKQR 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1227 QSLldhsnKAQANAEKQVKQLEVQLADAQfkVDEMNRTLNDLDGGKKKLAVENSELQRQLEESESQVAQLNKIKASLATQ 1306
Cdd:TIGR00618 559 ASL-----KEQMQEIQQSFSILTQCDNRS--KEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVR 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1307 LEEaKRMADEEARERAAILGKYRNLEHDLDNLRESVEEEQEAKADFQRQLSKANAEAQLWRSKYESEGLAR----LEELE 1382
Cdd:TIGR00618 632 LHL-QQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQcqtlLRELE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1383 EAKRKLHGKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEVDKanalASSLEKRQKSFDKVIAEWK-AKVDDLAAE 1461
Cdd:TIGR00618 711 THIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLK----ARTEAHFNNNEEVTAALQTgAELSHLAAE 786
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556079866 1462 LDASQKECRNYSTEVFKLRAAYEESQEHYESVKR-ENKNLQDEVKDLMDQLGEGGRSVHELEKSRKRLE 1529
Cdd:TIGR00618 787 IQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNlQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYE 855
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1306-2167 |
3.96e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.39 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1306 QLEEAKRMADEEARERAAILGKYRNLEHDLDNLRESVEEEQEAKADFQrQLSKANAEAQLWrskyesEGLARLEELEEAK 1385
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQ-ALLKEKREYEGY------ELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1386 RKLHGKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEV-DKANALASSLEKRQKSFDKVIAEWKAKVDDLAAELDA 1464
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1465 SQKECRNYSTEVFKLRAAYEESQEHYESVKRENKNLQDEVKDLMDqlgeggrsvhELEKSRKRLEMEkeelqaaleeaea 1544
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE----------ELEDLRAELEEV------------- 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1545 aleQEENKVLRAqlELSQVRQEIDRRIQEKEEEFENTRKNHQRA--LDSMQASLEAEAKGKAEALrlkKKLESDINELEI 1622
Cdd:TIGR02169 377 ---DKEFAETRD--ELKDYREKLEKLKREINELKRELDRLQEELqrLSEELADLNAAIAGIEAKI---NELEEEKEDKAL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1623 ALDHANKANAEAQKNLKKYQQNVKDLQGALEEEQRARDEAREQYASAERRCNAMHGELEESR---QLLASSKNSHLRHIE 1699
Cdd:TIGR02169 449 EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRaveEVLKASIQGVHGTVA 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1700 QMEGEELLMQKKL------RTEVIRLEDALVQVRKeyemlrIEFEQNLAATEQTG-PINReMR--HLITSLQSHNRQLKG 1770
Cdd:TIGR02169 529 QLGSVGERYATAIevaagnRLNNVVVEDDAVAKEA------IELLKRRKAGRATFlPLNK-MRdeRRDLSILSEDGVIGF 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1771 EVSRYKRKLREAAAEAARLKQTLEMSNVAVSSTTVPSSASSTSsdngssrgeEGAPVScpqpgQGGREEGGTPSASSQRR 1850
Cdd:TIGR02169 602 AVDLVEFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYRMVTL---------EGELFE-----KSGAMTGGSRAPRGGIL 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1851 EEEAREEEPIPEREKgksdldiIRDLKAQLKKSQEAQRELKLLLDMYKgapkeqrdkvQLMAAEKKARAEVEEHRQQLK- 1929
Cdd:TIGR02169 668 FSRSEPAELQRLRER-------LEGLKRELSSLQSELRRIENRLDELS----------QELSDASRKIGEIEKEIEQLEq 730
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1930 -------KLAEHERK----ERRKLADEDAMKKIRG-LEETVASLHKsLTAQKQEVWEEALLSEMEVTGQAFEDMQEQNLR 1997
Cdd:TIGR02169 731 eeeklkeRLEELEEDlsslEQEIENVKSELKELEArIEELEEDLHK-LEEALNDLEARLSHSRIPEIQAELSKLEEEVSR 809
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1998 LIQQLREKDDANFKLMSERIKSNQIHKLLQEEKAMLSEQGATLQAQVEAQNQVVRKLEEKERLLQNSLSTLEKELS---- 2073
Cdd:TIGR02169 810 IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGdlkk 889
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 2074 ----LRQQAAEMHRRKavESAQSAADLKlhlEKYLAQLKDAQGIVTDRTAVLSQETFKTKRLQEEILSLRRKVERAKKFE 2149
Cdd:TIGR02169 890 erdeLEAQLRELERKI--EELEAQIEKK---RKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVE 964
|
890
....*....|....*....
gi 556079866 2150 LATNT-DEVLMEEIKEYKE 2167
Cdd:TIGR02169 965 EEIRAlEPVNMLAIQEYEE 983
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1057-1323 |
5.12e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.61 E-value: 5.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1057 AQEAVADLEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLAR 1136
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1137 eieelserLEESGGATSSQIELnkrreaelsklrrdLEESN-----LQHEQAMSNLRKKHNDTVAEMSEQIDQLNKHKAK 1211
Cdd:COG3883 94 --------ALYRSGGSVSYLDV--------------LLGSEsfsdfLDRLSALSKIADADADLLEELKADKAELEAKKAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1212 VEkeratmsaevsdlqslldhsnKAQANAEKQVKQLEVQLADAQFKVDEMNRTLNDLDGGKKKLAVENSELQRQLEESES 1291
Cdd:COG3883 152 LE---------------------AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
250 260 270
....*....|....*....|....*....|..
gi 556079866 1292 QVAQLNKIKASLATQLEEAKRMADEEARERAA 1323
Cdd:COG3883 211 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1225-1672 |
6.67e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 6.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1225 DLQSLLDHSNKAQANAEKQVKQLEVQLADAQFKVDEMNRTLNDLDGGKKKLAvensELQRQLEESESQVAQLNKIKasla 1304
Cdd:COG4717 54 EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELE----ELEAELEELREELEKLEKLL---- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1305 tQLEEAKRMADEEARERAAILGKYRNLEHDLDNLRESVEEEQEAKADF---QRQLSKANAEAQLWRSKYESEGLARLEEL 1381
Cdd:COG4717 126 -QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELaelQEELEELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1382 EEAKRKLHGKLQEAEEAMEQLNAKCSGLEKTK--SHLQGELEDMSIEVdKANALASSLEKRQKSFDKVIAEWKAKVDDLA 1459
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELeaAALEERLKEARLLL-LIAAALLALLGLGGSLLSLILTIAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1460 A-------ELDASQKECRNYSTEVFKLRAAYEESQEHYESVKRE----NKNLQDEVKDLMDQLGEGGRSVHELEKSRKRL 1528
Cdd:COG4717 284 GllallflLLAREKASLGKEAEELQALPALEELEEEELEELLAAlglpPDLSPEELLELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1529 EMEKEELQAALEEAEAALEQEenKVLRAQLELSQVRQEIDRRIQEKEEEFENtrknhqrALDSMQASLEAEAkgkaealr 1608
Cdd:COG4717 364 QLEELEQEIAALLAEAGVEDE--EELRAALEQAEEYQELKEELEELEEQLEE-------LLGELEELLEALD-------- 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556079866 1609 lKKKLESDINELEIALdhankanAEAQKNLKKYQQNVKDLQGALE--EEQRARDEAREQYASAERR 1672
Cdd:COG4717 427 -EEELEEELEELEEEL-------EELEEELEELREELAELEAELEqlEEDGELAELLQELEELKAE 484
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1382-2143 |
7.48e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 7.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1382 EEAKRKLHgklqEAEEAMEQLNAKCSGLEKTKSHLQgeledmsIEVDKANALassLEKRQKSFDKVIAEWKAKVDDLAAE 1461
Cdd:TIGR02168 175 KETERKLE----RTRENLDRLEDILNELERQLKSLE-------RQAEKAERY---KELKAELRELELALLVLRLEELREE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1462 LDASQKECRNYSTEVFKLRAAYEESQEHYESVKRENKNLQDEVKDLMDQLGEGGRSVHELEKsrkrlemekeelqaalee 1541
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ------------------ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1542 aeaaleqeenkvlraQLELSQVRQEidrRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRLKKKLESDINELE 1621
Cdd:TIGR02168 303 ---------------QKQILRERLA---NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1622 IALDHANKANAEAQKNLKKYQQNVKDLqgaleEEQRARDEAREQYASAERRcnamhgELEESRQLLASSKNSHLRHIEQM 1701
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQL-----ELQIASLNNEIERLEARLE------RLEDRRERLQQEIEELLKKLEEA 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1702 EGEELLMQ-KKLRTEVIRLEDALVQVRKEYEMLRIEFEQNLAATEQTGPINREMRHLITSLQSHNRQLKGEVSRYKRKLR 1780
Cdd:TIGR02168 434 ELKELQAElEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1781 EAAAEAARLKQTLEMSNVAVSSTTVPSSASSTSSDNGSSRGEEGA--PVSCPQPGQGGR-------EEGGTPSASSQRRE 1851
Cdd:TIGR02168 514 NQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAAkkAIAFLKQNELGRvtflpldSIKGTEIQGNDREI 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1852 EEAREEEPIPEREKGKSDLDIIRDLKAQLKKS------QEAQRELKLLLDMY------------KGAPKEQRDKVQLMAA 1913
Cdd:TIGR02168 594 LKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvddlDNALELAKKLRPGYrivtldgdlvrpGGVITGGSAKTNSSIL 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1914 EKkaRAEVEEHRQQLKKLAEHERKERRKLAdeDAMKKIRGLEETVASLHKSLTAQKQEVWE-EALLSEMEVTGQAFEDMQ 1992
Cdd:TIGR02168 674 ER--RREIEELEEKIEELEEKIAELEKALA--ELRKELEELEEELEQLRKELEELSRQISAlRKDLARLEAEVEQLEERI 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1993 EQNLRLIQQLREKDDAnfkLMSERIKSNQIHKLLQEEKAMLSEQGATLQAQVEAQNQVVRKLEEKERLLQNSLSTLEKEL 2072
Cdd:TIGR02168 750 AQLSKELTELEAEIEE---LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556079866 2073 SLRQQAAEMHRRKAVESAQSAADLKLHLEKYLAQLKDAQGIVTDRTAVLSQETFKTKRLQEEILSLRRKVE 2143
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
839-1427 |
8.63e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 8.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 839 RVEDELKAMEEKLKKTEEALAKEEKLRKELEEhnvkVLQEKNDLFLQLEAERMGAGDVEERLNKALTQKGDLESQLADLN 918
Cdd:PRK02224 224 RYEEQREQARETRDEADEVLEEHEERREELET----LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 919 DRLSHEEDAHASLSQSKKKLEGEISGLKKDIEDMELALQKAeqdkatkdhqirnlNDEIQHQDELINKLNKEKKHLQEAS 998
Cdd:PRK02224 300 AEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAH--------------NEEAESLREDADDLEERAEELREEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 999 QKTSEDLQATEDKVnhlnkvkAKLEQTLDELEDSLEREKKARGDIEKNKRKVEGDLKLAQEAVADLEKNKKEMEQNLQrk 1078
Cdd:PRK02224 366 AELESELEEAREAV-------EDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR-- 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1079 ekemaSLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLAreieelserleesggatSSQIEL 1158
Cdd:PRK02224 437 -----TARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLE-----------------EEVEEV 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1159 NKR--REAELSKLRRDLEESnLQHEQAMSNLRKKHNDTVAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSlldhsnKA 1236
Cdd:PRK02224 495 EERleRAEDLVEAEDRIERL-EERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE------EA 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1237 QANAEKqVKQLEVQLADAQFKVDEMNR------TLNDLDGGKKKLAVENSELQRQLEESESQVAQLNKIKASLATQLEEA 1310
Cdd:PRK02224 568 EEAREE-VAELNSKLAELKERIESLERirtllaAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEA 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1311 krmADEEARERAAilgkyrNLEHDLDNLRESVEEEQEAKADFQRQLSKANAEaqlwrskyesegLARLEELeeakRKLHG 1390
Cdd:PRK02224 647 ---RIEEAREDKE------RAEEYLEQVEEKLDELREERDDLQAEIGAVENE------------LEELEEL----RERRE 701
|
570 580 590
....*....|....*....|....*....|....*..
gi 556079866 1391 KLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEV 1427
Cdd:PRK02224 702 ALENRVEALEALYDEAEELESMYGDLRAELRQRNVET 738
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
842-1364 |
9.71e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 9.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 842 DELKAMEEKLKKTEEalakeeklrkeleehNVKVLQEKNDLFLQLEAERMGAGDVEERLNKALTQKGDLESQLadLNDRL 921
Cdd:COG4913 235 DDLERAHEALEDARE---------------QIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 922 SHEEDAHASLSQSKKKLEGEISGLKKDIEDMELALQKAEQDkatkdhQIRNLNDEIQHQDELINKLNKEKKHLQEASQKT 1001
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD------RLEQLEREIERLERELEERERRRARLEALLAAL 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1002 SEDLQATEDKvnhLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKRKVEGDLKLAQEAVADLEKNKKEMEQNLQRKEKE 1081
Cdd:COG4913 372 GLPLPASAEE---FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1082 MASLAAKLEDEQALVAKLQkQIKELQAR----------------IEELEEELEAERQARAKAEKQRADLAREIEELSERL 1145
Cdd:COG4913 449 LAEALGLDEAELPFVGELI-EVRPEEERwrgaiervlggfaltlLVPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1146 EESGGATS----SQIELNKRR---EAELSKlRRDLE----ESNL-QHEQAM--------SNLRKKHNDT----------- 1194
Cdd:COG4913 528 RPRLDPDSlagkLDFKPHPFRawlEAELGR-RFDYVcvdsPEELrRHPRAItragqvkgNGTRHEKDDRrrirsryvlgf 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1195 -----VAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDHSNKAQ--ANAEKQVKQLEVQLADAQFKVDEMNRTLND 1267
Cdd:COG4913 607 dnrakLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAeySWDEIDVASAEREIAELEAELERLDASSDD 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1268 LDGGKKKLAvensELQRQLEESESQVAQLNKIKASLATQLEEAKRMADE-----EARERAAILGKYRNLEHDLDNLRESv 1342
Cdd:COG4913 687 LAALEEQLE----ELEAELEELEEELDELKGEIGRLEKELEQAEEELDElqdrlEAAEDLARLELRALLEERFAAALGD- 761
|
570 580
....*....|....*....|..
gi 556079866 1343 EEEQEAKADFQRQLSKANAEAQ 1364
Cdd:COG4913 762 AVERELRENLEERIDALRARLN 783
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1053-1665 |
9.80e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 9.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1053 DLKLAQEAVADLEKnKKEMEQNLQRKEKEMASLAAKLEDEQALVAKL-----QKQIKELQARIEELEEELEAERQARAKA 1127
Cdd:COG4913 236 DLERAHEALEDARE-QIELLEPIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1128 EKQRADLAREIEELSERLEESGGATSSQIE-----LNKRRE------AELSKLRRDLEESNLQHEQAMSNLRKKHNDTVA 1196
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQLEreierLERELEererrrARLEALLAALGLPLPASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1197 EMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDHSNKAQANAEKQVKQLEVQLADA---------------QFKVDE- 1260
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAlgldeaelpfvgeliEVRPEEe 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1261 -----MNRTLNdldGGKKKLAVEnselqrqlEESESQVAQ-LNKIKASLATQLEEAKRMADEEARERA---AILGK---- 1327
Cdd:COG4913 475 rwrgaIERVLG---GFALTLLVP--------PEHYAAALRwVNRLHLRGRLVYERVRTGLPDPERPRLdpdSLAGKldfk 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1328 ---YRN-LEHDLDNLR-----ESVEE-EQEAKADFQRQLSKANAEA-QLWRSKYESEGL-------ARLEELEEAKRKLH 1389
Cdd:COG4913 544 phpFRAwLEAELGRRFdyvcvDSPEElRRHPRAITRAGQVKGNGTRhEKDDRRRIRSRYvlgfdnrAKLAALEAELAELE 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1390 GKLQEAEEAMEQLNAKCSGLEKTKSHLQG--ELEDMSIEVDKANALASSLEKRQKSFDK---VIAEWKAKVDDLAAELDA 1464
Cdd:COG4913 624 EELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERLDAssdDLAALEEQLEELEAELEE 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1465 SQKECRNYSTEVFKLRAAYEESQEhyesvkrenknLQDEVKDLMDQLGEGGRSVH--ELEKSRKRLEMEKEELqaaleea 1542
Cdd:COG4913 704 LEEELDELKGEIGRLEKELEQAEE-----------ELDELQDRLEAAEDLARLELraLLEERFAAALGDAVER------- 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1543 eaaleqeenkvlRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRLKKKLESDinELei 1622
Cdd:COG4913 766 ------------ELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEED--GL-- 829
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 556079866 1623 aldHANKANAEAQKNlKKYQQNVKDLQGALEeeqRARDEAREQ 1665
Cdd:COG4913 830 ---PEYEERFKELLN-ENSIEFVADLLSKLR---RAIREIKER 865
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
957-1330 |
1.37e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 957 QKAEQDKATKDHQIRNLNDEIQHQDELINKLNKEKKHLQEASQKTSEDLQATEDKVNHlnkvkAKLEQTLDELEDSLERE 1036
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV-----ASAEREIAELEAELERL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1037 KKArgdieknkrkvEGDLKLAQEAVADLEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEE 1116
Cdd:COG4913 681 DAS-----------SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1117 LEAERQARAKAEKQRADLAREieelserleesggATSSQIELNKRREAELSKLRRDLEESNLQHEQAMSNLRkkhnDTVA 1196
Cdd:COG4913 750 LLEERFAAALGDAVERELREN-------------LEERIDALRARLNRAEEELERAMRAFNREWPAETADLD----ADLE 812
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1197 EMSEQIDQLNK--------HKAKVEKERATMS-AEVSDLQSLLDhsnKAQANAEKQVKQLEVQLADAQFKVD-----EMN 1262
Cdd:COG4913 813 SLPEYLALLDRleedglpeYEERFKELLNENSiEFVADLLSKLR---RAIREIKERIDPLNDSLKRIPFGPGrylrlEAR 889
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1263 RTLN-DLDGGKKKL-AVENSELQRQLEESESQVAQLNKIKASLATQLEEAKRmadeeaRERAAILgKYRN 1330
Cdd:COG4913 890 PRPDpEVREFRQELrAVTSGASLFDEELSEARFAALKRLIERLRSEEEESDR------RWRARVL-DVRN 952
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
830-1394 |
1.65e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 830 KVKPLLSAVRVEDELKAMEEKLKKTEEALAKEEKLRKELEEHnvKVLQEKNdlflqlEAERMGAGDVEERLNKALTQKGD 909
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK--KKAEEAK------KAEEAKKKAEEAKKADEAKKKAE 1480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 910 lESQLADLNDRLSHE-----EDAHASLSQSKKKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLnDEIQHQDELi 984
Cdd:PTZ00121 1481 -EAKKADEAKKKAEEakkkaDEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA-DELKKAEEL- 1557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 985 nKLNKEKKHLQEAsQKTSEDLQATEDKVNHLNKVKaklEQTLDELEDSLEREKKARGdiEKNKRKVEGDLKLAQEAVADL 1064
Cdd:PTZ00121 1558 -KKAEEKKKAEEA-KKAEEDKNMALRKAEEAKKAE---EARIEEVMKLYEEEKKMKA--EEAKKAEEAKIKAEELKKAEE 1630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1065 EKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLAREIEelser 1144
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE----- 1705
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1145 leesggatssqiELNKRREAELSK---LRRDLEESNLQHEQAmsnlrKKHNDTVAEMSEQIDQLNKHKAKVEKERATMSA 1221
Cdd:PTZ00121 1706 ------------ELKKKEAEEKKKaeeLKKAEEENKIKAEEA-----KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK 1768
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1222 EVSDLQSLLDHSNKAQANAEKQVKQLEVqlaDAQFKvDEMNRTLNDLDGGKKKLAVENselqrqlEESESQVAQLNKIKA 1301
Cdd:PTZ00121 1769 KAEEIRKEKEAVIEEELDEEDEKRRMEV---DKKIK-DIFDNFANIIEGGKEGNLVIN-------DSKEMEDSAIKEVAD 1837
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1302 SLATQLEEAKRM----------ADEEARERAAILGKYRNLEHDLDNLRESVEEEQEAKADFQRQLSKANAEAQLWRSKYE 1371
Cdd:PTZ00121 1838 SKNMQLEEADAFekhkfnknneNGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDD 1917
|
570 580
....*....|....*....|...
gi 556079866 1372 seglaRLEELEEAKRKLHGKLQE 1394
Cdd:PTZ00121 1918 -----KLDKDEYIKRDAEETREE 1935
|
|
| zf-C3HC4 |
pfam00097 |
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ... |
2171-2209 |
1.83e-08 |
|
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a cysteine-rich domain of 40 to 60 residues that coordinates two zinc ions, and has the consensus sequence: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C where X is any amino acid. Many proteins containing a RING finger play a key role in the ubiquitination pathway.
Pssm-ID: 395049 [Multi-domain] Cd Length: 40 Bit Score: 51.97 E-value: 1.83e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 556079866 2171 CPSCKVKRKDAV-LIKCFHVFCYDCLKTRYETRQRKCPKC 2209
Cdd:pfam00097 1 CPICLEEPKDPVtLLPCGHLFCSKCIRSWLESGNVTCPLC 40
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1177-1739 |
2.25e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1177 NLQHEQAMSNLRKKHNDTVAEMSEQIDQLNKHKakvEKERATMSAEVSDLQSLLDHSNKAQANAEKQVKQLEvqlaDAQF 1256
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTENIEELIKEK---EKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1257 KVDEMNRTLNDLDGGKKKLAVENSELQRQLEESESQVAQLNKIKASLaTQLEEAKRMADEEARERAAILGKYRNLEHDLD 1336
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1337 NLRESVEEeqeakadFQRQLSKAnaeaqlwrSKYESEGLARLEELEEAKRKLhGKLQEAEEAMEQLNAKCSGLEKTKSHL 1416
Cdd:PRK03918 318 RLEEEING-------IEERIKEL--------EEKEERLEELKKKLKELEKRL-EELEERHELYEEAKAKKEELERLKKRL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1417 QGEledmsiEVDKANALASSLEKRQKSFDKVIAEWKAKVddlaAELDASQKECRNYSTEVFKLRA-----AYEESQEHYE 1491
Cdd:PRK03918 382 TGL------TPEKLEKELEELEKAKEEIEEEISKITARI----GELKKEIKELKKAIEELKKAKGkcpvcGRELTEEHRK 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1492 SVKRENKnlqDEVKDLMDQLGEGGRSVHELEKSRKRLEMEkeelqAALEEAEAALEQEENKVLRAQLELSQVRQEidrRI 1571
Cdd:PRK03918 452 ELLEEYT---AELKRIEKELKEIEEKERKLRKELRELEKV-----LKKESELIKLKELAEQLKELEEKLKKYNLE---EL 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1572 QEKEEEFENTRKNhqraldsmQASLEAEAKGKAEALRLKKKLESDINELEIALDHANKANAEAQKNLKKYQ-QNVKDLQG 1650
Cdd:PRK03918 521 EKKAEEYEKLKEK--------LIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEE 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1651 ALEEEQRARDEAREqyasaerrcnamhgeleesrqllassknshLRHIEQMEGEELLMQKKLRTEVIRLEDALVQVRKEY 1730
Cdd:PRK03918 593 RLKELEPFYNEYLE------------------------------LKDAEKELEREEKELKKLEEELDKAFEELAETEKRL 642
|
....*....
gi 556079866 1731 EMLRIEFEQ 1739
Cdd:PRK03918 643 EELRKELEE 651
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1192-1411 |
2.50e-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: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1192 NDTVAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDHSNKAQANAEKQVKQLEVQLADAQFKVDEMNRTLNDLDGG 1271
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1272 KKKLAVENSELQRQLEESESQVAQLNKIKASLATQLEEAKRMADEEARERAAILGKYRNLEHDLDNLRESVEEEQEAKAD 1351
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1352 FQRQLSKANAEAQLWRSKYEseglARLEELEEAKRKLHGKLQEAEEAMEQLNAKCSGLEK 1411
Cdd:COG4942 179 LLAELEEERAALEALKAERQ----KLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
826-1721 |
3.75e-08 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 59.29 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 826 KLYSKVKPLLSAVrVEDELKAMEEKLKKTEEALAKEEKLRKELEEHNV-KVLQEKNDLFLQLEAERMGAGDVEERLNKAL 904
Cdd:TIGR01612 707 KEYDKIQNMETAT-VELHLSNIENKKNELLDIIVEIKKHIHGEINKDLnKILEDFKNKEKELSNKINDYAKEKDELNKYK 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 905 TQKGDLESQLAD-LNDRLSHEEDAHASLSQSKKKL------EGEISGLKKDIEDM-ELALQKAEQDKATKDHQIRNLNDE 976
Cdd:TIGR01612 786 SKISEIKNHYNDqINIDNIKDEDAKQNYDKSKEYIktisikEDEIFKIINEMKFMkDDFLNKVDKFINFENNCKEKIDSE 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 977 IQHQDELINKLNKE---------KKHLQEASQKTSEDLQATEDKVNHLNKVKaKLEQTLDELEDSLEREKKARGDIEKNK 1047
Cdd:TIGR01612 866 HEQFAELTNKIKAEisddklndyEKKFNDSKSLINEINKSIEEEYQNINTLK-KVDEYIKICENTKESIEKFHNKQNILK 944
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1048 RKVEGDLKLAQEAVADLEKNKKEMEQNLQRKEKEMASL--AAKLEDEQALVAKLQKQIKELQARIEELEEELEAerQARA 1125
Cdd:TIGR01612 945 EILNKNIDTIKESNLIEKSYKDKFDNTLIDKINELDKAfkDASLNDYEAKNNELIKYFNDLKANLGKNKENMLY--HQFD 1022
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1126 KAEKQRADLAREIEELSERLEESGGATSSQIeLNKRREAElSKLRRDLEESNlqheqamSNLRKKHNDTVAEMSEQIDQL 1205
Cdd:TIGR01612 1023 EKEKATNDIEQKIEDANKNIPNIEIAIHTSI-YNIIDEIE-KEIGKNIELLN-------KEILEEAEINITNFNEIKEKL 1093
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1206 NKHKAK--VEKERATMSAEVSDLQSLLDHSNKaqaNAEKQVKQLEVQLADAQFKVDEMNRTLNDLDGGKKKlAVENSElq 1283
Cdd:TIGR01612 1094 KHYNFDdfGKEENIKYADEINKIKDDIKNLDQ---KIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADK-AISNDD-- 1167
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1284 rqleesesqVAQLNKIKASLATQLEEAKRMADEEAReraaILGKYRNLEHDldnlRESVEEEQEAKADFQRQLSKANAEa 1363
Cdd:TIGR01612 1168 ---------PEEIEKKIENIVTKIDKKKNIYDEIKK----LLNEIAEIEKD----KTSLEEVKGINLSYGKNLGKLFLE- 1229
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1364 QLWRSKYESEGL-----ARLEELEEAKRK------LHGKLQEAEEAMEQLNakCSGLEKTKSHLQGELEDMSIEvdkana 1432
Cdd:TIGR01612 1230 KIDEEKKKSEHMikameAYIEDLDEIKEKspeienEMGIEMDIKAEMETFN--ISHDDDKDHHIISKKHDENIS------ 1301
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1433 lasslEKRQKSFdKVIAEW--KAKVDDLAAELDASQKECRNYSTEVfklRAAYEESQEHYESVKREN-KNLQDEVKDLMD 1509
Cdd:TIGR01612 1302 -----DIREKSL-KIIEDFseESDINDIKKELQKNLLDAQKHNSDI---NLYLNEIANIYNILKLNKiKKIIDEVKEYTK 1372
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1510 QLGEGGRSVH-ELEKSRKRLEMEKEELQAALEEAEAALEQEENKVLRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRA 1588
Cdd:TIGR01612 1373 EIEENNKNIKdELDKSEKLIKKIKDDINLEECKSKIESTLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENV 1452
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1589 LDSMQaSLEAEAKGKAEALRLKKK-----LESDINELEIALDHANKANAEAQKNLKKYQQNvKDLqgaLEEEQRARDEAR 1663
Cdd:TIGR01612 1453 LLLFK-NIEMADNKSQHILKIKKDnatndHDFNINELKEHIDKSKGCKDEADKNAKAIEKN-KEL---FEQYKKDVTELL 1527
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*...
gi 556079866 1664 EQYASAERRcNAMHGELEESRQLLASSKNSHLRHIEQMEGEELLMqKKLRTEVIRLED 1721
Cdd:TIGR01612 1528 NKYSALAIK-NKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKI-KEIKKEKFRIED 1583
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1871-2161 |
3.98e-08 |
|
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: 58.91 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1871 DIIRDLKAQLKK----SQEAQRELKLlldmykgapKEQRDKVQ--LMAAEKK-ARAEVEEHRQQLKKLAEHERKERRKLA 1943
Cdd:TIGR02168 193 DILNELERQLKSlerqAEKAERYKEL---------KAELRELElaLLVLRLEeLREELEELQEELKEAEEELEELTAELQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1944 DEDAmkKIRGLEETVASLHKSLTAQKQEVWEeallsemevTGQAFEDMqEQNLRLIQQLREKDDANFKLMSERIKSNQIH 2023
Cdd:TIGR02168 264 ELEE--KLEELRLEVSELEEEIEELQKELYA---------LANEISRL-EQQKQILRERLANLERQLEELEAQLEELESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 2024 KL-LQEEKAMLSEQGATLQAQVEAQNQvvrKLEEKERLLQNSLSTLEKelslRQQAAEMHRRKAVESAQSAADLKLHLEK 2102
Cdd:TIGR02168 332 LDeLAEELAELEEKLEELKEELESLEA---ELEELEAELEELESRLEE----LEEQLETLRSKVAQLELQIASLNNEIER 404
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 556079866 2103 YLAQLKDAQGivtdrtavlsqetfKTKRLQEEILSLRRKVERAKKFELATNTDEVLMEE 2161
Cdd:TIGR02168 405 LEARLERLED--------------RRERLQQEIEELLKKLEEAELKELQAELEELEEEL 449
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1149-1378 |
4.06e-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: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1149 GGATSSQIELNKRREAELSKLRRDLEESNlQHEQAMSNLRKKHNDTVAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQS 1228
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELE-KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1229 LLDHSNKAQANAEKQVKQL-----------EVQLADAQFKVDEMNRTLNDLDGGKKKLAVENSELQRQLEESESQVAQLN 1297
Cdd:COG4942 91 EIAELRAELEAQKEELAELlralyrlgrqpPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1298 KIKASLATQLEEAKRMADEEARERAAILGKYRNLEHDLDNLRESVEEEQEAKADFQRQLSKANAEAQLWRSKYESEGLAR 1377
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
.
gi 556079866 1378 L 1378
Cdd:COG4942 251 L 251
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1317-2203 |
4.36e-08 |
|
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: 58.83 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1317 EARERAAILGKYRNLEHDLDNLRESVEEEQEAKAdfQRQLSKANAEAqlwrsKYESEGLARLEELEEAKRKLHGKLQEAE 1396
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKL--QELKLKEQAKK-----ALEYYQLKEKLELEEEYLLYLDYLKLNE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1397 EAMEQLNAKCSGLEKTKSHLQGEL---EDMSIEVDKANALASSLEKRQKSFDKVIAEwkakvdDLAAELDASQKECRNYS 1473
Cdd:pfam02463 237 ERIDLLQELLRDEQEEIESSKQEIekeEEKLAQVLKENKEEEKEKKLQEEELKLLAK------EEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1474 TEVFKLRAAYEESQEHYESVKRENKNLQDEVKDLmdQLGEGGRSVHELEKSRKRLEMEKEELQAALEEAEAALEQEENKV 1553
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKEL--KELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1554 LRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRLKKKLESDINELEIALDHANKANAE 1633
Cdd:pfam02463 389 AAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELK 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1634 AQKNLKKYQQNVKDLQGALEEEQRARDEAREQYASAERRCNAMHgELEESRQLLASSKNSHLRHIEQMEGEELLMQKKLR 1713
Cdd:pfam02463 469 KSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVL-LALIKDGVGGRIISAHGRLGDLGVAVENYKVAIST 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1714 TEVIRLEDALVQVRKEYEMLRIEFEQNLAATEQTGPINREMRHLITSLQSHNRQLKGEVSRYKRKLREAAAEAARLKQTL 1793
Cdd:pfam02463 548 AVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEG 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1794 EMSNVAVSSTTVPSSASSTSSDNGSSRGEEGAPVScpqpgqggreeggtpSASSQRREEEAREEEPIPEREKGKSDLDII 1873
Cdd:pfam02463 628 ILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKS---------------EVKASLSELTKELLEIQELQEKAESELAKE 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1874 RDLKAQLKKSQEAQRELKLLLDMYKGAPKEQRDKVQlmaaEKKARAEVEEHRQQLKKLAEHERKERRKLADEDAMKKIRG 1953
Cdd:pfam02463 693 EILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQ----EAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1954 LEETVASLHKSLTAQKQEVWE----------EALLSEMEVTGQAFEDMQEQNLRLIQQLREKDDANFKLMSERIKSNQIH 2023
Cdd:pfam02463 769 LSLKEKELAEEREKTEKLKVEeekeeklkaqEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKL 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 2024 KLLQEEKAMLSEQGATLQAQVEAQNQVVRKLEEKERLLQNSLSTLEKELSLRQQAAEMHRRKAVESAQSAADLKLHLEKY 2103
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAE 928
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 2104 LAQLKDAQGIVTDRTAVLSQETFKTKRLQEEILSLRRKVERAKKFELATNTDEVLMEEIKEYKEQLTCPSCKVKRKDAVL 2183
Cdd:pfam02463 929 ILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLI 1008
|
890 900
....*....|....*....|
gi 556079866 2184 IKCFHVFCYDCLKTRYETRQ 2203
Cdd:pfam02463 1009 RAIIEETCQRLKEFLELFVS 1028
|
|
| RING |
smart00184 |
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ... |
2171-2209 |
5.33e-08 |
|
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)
Pssm-ID: 214546 [Multi-domain] Cd Length: 40 Bit Score: 50.59 E-value: 5.33e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 556079866 2171 CPSCK-VKRKDAVLIKCFHVFCYDCLKTRYETRQRKCPKC 2209
Cdd:smart00184 1 CPICLeEYLKDPVILPCGHTFCRSCIRKWLESGNNTCPIC 40
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1233-1468 |
6.07e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 6.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1233 SNKAQANAEKQVKQLEVQLADAQFKVDEMNRTLNDLDGGKKKLAVENSELQRQLEESESQVAQLNKIKASLATQLEEAKR 1312
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1313 MADEEARERAAILGK-YRNLEHDLDNLRESVEEEQEAKADFQ--RQLSKANAEaqlwrskyeseglaRLEELEEAKRKLH 1389
Cdd:COG4942 98 ELEAQKEELAELLRAlYRLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARRE--------------QAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556079866 1390 GKLQEAEEAMEQlnakcsgLEKTKSHLQGELEDMSIEVDKANALASSLEKRQKSFDKVIAEWKAKVDDLAAELDASQKE 1468
Cdd:COG4942 164 ALRAELEAERAE-------LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
895-1054 |
6.50e-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: 6.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 895 DVEERLNKALTQKGDLESQLADLNDRLSHEEDAHASLSQSKKKLEGEISGLKKDIEDMELALQKAE--QDKATKDHQIRN 972
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqLGNVRNNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 973 LNDEIQHQDELINKLNKEKKHLQEASQKTSEDLQATEDKVNHLNKVKAKLEQTLDELEDSLERE-KKARGDIEKNKRKVE 1051
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAElEELEAEREELAAKIP 173
|
...
gi 556079866 1052 GDL 1054
Cdd:COG1579 174 PEL 176
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
873-1669 |
6.73e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.43 E-value: 6.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 873 VKVLQEKNDLFLQL--EAERMGAGD---VEERLNKALTQKGDLESQLADLNDRLSHEEDAHASLSQSKKKLEGEISGLKK 947
Cdd:PRK04863 249 IRVTQSDRDLFKHLitESTNYVAADymrHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQ 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 948 DIEdmelalqkaeqdkATKDHQIRNLNDEIQHqdeliNKLNKEKKHLQEASQKTSEDLQATEDkvnhLNKVKAKLEQTLD 1027
Cdd:PRK04863 329 DYQ-------------AASDHLNLVQTALRQQ-----EKIERYQADLEELEERLEEQNEVVEE----ADEQQEENEARAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1028 ELEDSLEREKKARGD-----IEKNKRKVEgdlklAQEAVADLEK-------------NKKEMEQNLQRKEKEMA----SL 1085
Cdd:PRK04863 387 AAEEEVDELKSQLADyqqalDVQQTRAIQ-----YQQAVQALERakqlcglpdltadNAEDWLEEFQAKEQEATeellSL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1086 AAKLEDEQAlvAKLQ-KQIKELQARIEELEEELEAERQARAK---AEKQRADLAREIEELSERLEESGgatssqiELNKR 1161
Cdd:PRK04863 462 EQKLSVAQA--AHSQfEQAYQLVRKIAGEVSRSEAWDVARELlrrLREQRHLAEQLQQLRMRLSELEQ-------RLRQQ 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1162 REAElsKLRRDLE---ESNLQHEQAMSNLRKKHNDTVAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDHSNKAQA 1238
Cdd:PRK04863 533 QRAE--RLLAEFCkrlGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQD 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1239 NAEKQVKQLEVQLADAQFKVDEMNRTLNDLdggkKKLAVENSELQRQLEESESQVAQLNKIKASLATQLeeaKRMAD--- 1315
Cdd:PRK04863 611 ALARLREQSGEEFEDSQDVTEYMQQLLERE----RELTVERDELAARKQALDEEIERLSQPGGSEDPRL---NALAErfg 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1316 -------------EEARERAAILGKYRN--------------------------LEHDLDNLRESVEEEQEAKADFQRQL 1356
Cdd:PRK04863 684 gvllseiyddvslEDAPYFSALYGPARHaivvpdlsdaaeqlagledcpedlylIEGDPDSFDDSVFSVEELEKAVVVKI 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1357 SkanaEAQLWRSKYESEGL-------ARLEEL----EEAKRKLHG------KLQ--------------------EAEEAM 1399
Cdd:PRK04863 764 A----DRQWRYSRFPEVPLfgraareKRIEQLraerEELAERYATlsfdvqKLQrlhqafsrfigshlavafeaDPEAEL 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1400 EQLNAKCSGLEKTKSHLQGELEDMSIEVDKANALASSLEKRQKS----FDKVIAEwkaKVDDLAAELDASQKECR----- 1470
Cdd:PRK04863 840 RQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRlnllADETLAD---RVEEIREQLDEAEEAKRfvqqh 916
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1471 -NYSTEVFKLRAAYEESQEHYESVKRENKNLQDEVKDLMDQLgeggRSVHELEKSRKRLEMEKeelqaalEEAEAALEQE 1549
Cdd:PRK04863 917 gNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQA----FALTEVVQRRAHFSYED-------AAEMLAKNSD 985
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1550 ENKVLRAQLELSQV-RQEIDRRIQEKEEEFentRKNHQRaLDSMQASLEAEAKGKAEALR------------LKKKLESD 1616
Cdd:PRK04863 986 LNEKLRQRLEQAEQeRTRAREQLRQAQAQL---AQYNQV-LASLKSSYDAKRQMLQELKQelqdlgvpadsgAEERARAR 1061
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 556079866 1617 INELEIALDHANKANAEAQKNLKKYQQNVKDLQGALEEEQRARDEAREQYASA 1669
Cdd:PRK04863 1062 RDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNA 1114
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
909-1507 |
9.37e-08 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 57.75 E-value: 9.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 909 DLESQLADLNDRLSHEEDA-HASLSQSKKKLEGEISglkKDIEDMELALQKAEQDKATKDHQIR------NLND-----E 976
Cdd:TIGR01612 1030 DIEQKIEDANKNIPNIEIAiHTSIYNIIDEIEKEIG---KNIELLNKEILEEAEINITNFNEIKeklkhyNFDDfgkeeN 1106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 977 IQHQDElINKLNKEKKHLQEASQKTSEDLQATEDKV-NHLNKVKA---KLEQTLDEL---EDSLEREKKARG---DIEKN 1046
Cdd:TIGR01612 1107 IKYADE-INKIKDDIKNLDQKIDHHIKALEEIKKKSeNYIDEIKAqinDLEDVADKAisnDDPEEIEKKIENivtKIDKK 1185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1047 KRKVEGDLKLAQEaVADLEKNKKEMEQ----NLQRKEKEMASLAAKLEDEQA----LVAKLQKQIKEL-QARIEELEEEL 1117
Cdd:TIGR01612 1186 KNIYDEIKKLLNE-IAEIEKDKTSLEEvkgiNLSYGKNLGKLFLEKIDEEKKksehMIKAMEAYIEDLdEIKEKSPEIEN 1264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1118 EAERQARAKAEKQRADLAREIEELSERLEESGGATSSQIElNKR--------REAELSKLRRDLEESNLQHEQAMSNLRK 1189
Cdd:TIGR01612 1265 EMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIR-EKSlkiiedfsEESDINDIKKELQKNLLDAQKHNSDINL 1343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1190 KHND--------TVAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDhSNKAQANAEKQVKQLEVQLADaqfkvDEM 1261
Cdd:TIGR01612 1344 YLNEianiynilKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIK-KIKDDINLEECKSKIESTLDD-----KDI 1417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1262 NRTLNDLDGGKKKLAVENSELQ---RQLEESESQVAQL--------NKIKASLATQLEEAKRMADEEARERAAILGKYRN 1330
Cdd:TIGR01612 1418 DECIKKIKELKNHILSEESNIDtyfKNADENNENVLLLfkniemadNKSQHILKIKKDNATNDHDFNINELKEHIDKSKG 1497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1331 LEHDLDNLRESVEEEQEA----KADFQRQLSKANAEA---QLWRSKYESEGLarLEELEEAKRKLHGKLQEAEEAMEQLN 1403
Cdd:TIGR01612 1498 CKDEADKNAKAIEKNKELfeqyKKDVTELLNKYSALAiknKFAKTKKDSEII--IKEIKDAHKKFILEAEKSEQKIKEIK 1575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1404 AKcsglektkshlQGELEDMSIEVDKANALA----SSLEKRQKSFDKvIAEWKAKVDDLAAELDASQKECRNYS-----T 1474
Cdd:TIGR01612 1576 KE-----------KFRIEDDAAKNDKSNKAAidiqLSLENFENKFLK-ISDIKKKINDCLKETESIEKKISSFSidsqdT 1643
|
650 660 670
....*....|....*....|....*....|...
gi 556079866 1475 EVFKLRAAYEESQEHYESVKRENKNLQDEVKDL 1507
Cdd:TIGR01612 1644 ELKENGDNLNSLQEFLESLKDQKKNIEDKKKEL 1676
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1083-1350 |
1.06e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1083 ASLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLAREIeelserleesggatssqielnKRR 1162
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI---------------------RAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1163 EAELSKLRRDLEESNLQHEQamsnLRKKHNDTVAEMSEQIDQLNKhkakvekeratmSAEVSDLQSLLDHSNKAQAnaEK 1242
Cdd:COG4942 75 EQELAALEAELAELEKEIAE----LRAELEAQKEELAELLRALYR------------LGRQPPLALLLSPEDFLDA--VR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1243 QVKQLEVQLADAQFKVDEMNRTLNDLDGGKKKLAVENSELQRQLEESESQVAQLNKIKASLATQLEEAKRMADEEARERA 1322
Cdd:COG4942 137 RLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
|
250 260
....*....|....*....|....*...
gi 556079866 1323 AILGKYRNLEHDLDNLRESVEEEQEAKA 1350
Cdd:COG4942 217 ELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
954-1110 |
1.22e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.93 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 954 LALQKAEQDKATKDHQIRNLNDEIQHQDELINKLNKEKKHLQEASQKTSEDLQATEDKVNHLNKVKAKLEQTLDE----- 1028
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1029 ----LEDSLEREKKARGDIEKNKRKVEGDLKLAQEAVADLEKNKKEMEQNLQRKEKEMASLAAKLEDEQalvAKLQKQIK 1104
Cdd:COG1579 90 eyeaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL---EELEAERE 166
|
....*.
gi 556079866 1105 ELQARI 1110
Cdd:COG1579 167 ELAAKI 172
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
996-1134 |
1.30e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.93 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 996 EASQKTSEDLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKRKVEGDLKLAQEAVADLEKNKKEMEQNL 1075
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556079866 1076 Q--RKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADL 1134
Cdd:COG1579 83 GnvRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
947-1483 |
1.56e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 947 KDIEDMELALQKAEQDKAT-----KDHQ-IRNLNDEIQHQDELINKLN-----KEKKHLQEASQKTSEDLQATEDKVNHL 1015
Cdd:COG4913 235 DDLERAHEALEDAREQIELlepirELAErYAAARERLAELEYLRAALRlwfaqRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1016 NKVKAKLEQTLDELE-----------DSLEREKKARgdiEKNKRKVEGDLKLAQEAVADLEKNKKEMEQNLQRKEKEMAS 1084
Cdd:COG4913 315 EARLDALREELDELEaqirgnggdrlEQLEREIERL---ERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1085 LAAKLEDEQALV----AKLQKQIKELQARIEELEEELEAERQAR----AKAEKQRADLAReieelserleesggatssqi 1156
Cdd:COG4913 392 LLEALEEELEALeealAEAEAALRDLRRELRELEAEIASLERRKsnipARLLALRDALAE-------------------- 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1157 ELNKRRE-----AELSKLRRDLEESNLQHEQAMSNLR------KKHNDTVAEMseqIDQLNKHKA----KVEKERATMSA 1221
Cdd:COG4913 452 ALGLDEAelpfvGELIEVRPEEERWRGAIERVLGGFAltllvpPEHYAAALRW---VNRLHLRGRlvyeRVRTGLPDPER 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1222 EVSDLQSLLD----HSNKAQANAEKQVKQL--------EVQLADAQFKVDE-----MNRTLNDLDGGKKK-----LAVEN 1279
Cdd:COG4913 529 PRLDPDSLAGkldfKPHPFRAWLEAELGRRfdyvcvdsPEELRRHPRAITRagqvkGNGTRHEKDDRRRIrsryvLGFDN 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1280 selQRQLEESESQVAQLNKIKASLATQLEEAKRmADEEARERAAILGKYRNLEHDLDNLReSVEEEQEAKADFQRQLSKA 1359
Cdd:COG4913 609 ---RAKLAALEAELAELEEELAEAEERLEALEA-ELDALQERREALQRLAEYSWDEIDVA-SAEREIAELEAELERLDAS 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1360 NAEaqlwrskyeseglarLEELEEAKRKLHGKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEVDKANALASS--- 1436
Cdd:COG4913 684 SDD---------------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelr 748
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 556079866 1437 --LEKR--QKSFDKVIAEwkaKVDDLAAELDASQKECRNYSTEVFKLRAAY 1483
Cdd:COG4913 749 alLEERfaAALGDAVERE---LRENLEERIDALRARLNRAEEELERAMRAF 796
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1232-1468 |
1.93e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.61 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1232 HSNKAQANAEKQVKQLEVQLADAQFKVDEMNRTLNDLDGGKKKLAVENSELQRQLEESESQVAQLNKikaslatQLEEAK 1311
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA-------EIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1312 rmadEEARERAAILGKYRNLEHDLDNLRESveeeqeakADFQRQLSKANAEAQLwrSKYESEGLARL----EELEEAKRK 1387
Cdd:COG3883 86 ----EELGERARALYRSGGSVSYLDVLLGS--------ESFSDFLDRLSALSKI--ADADADLLEELkadkAELEAKKAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1388 LHGKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEVDKANALASSLEKRQKSFDKVIAEWKAKVDDLAAELDASQK 1467
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
.
gi 556079866 1468 E 1468
Cdd:COG3883 232 A 232
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1383-1669 |
2.45e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1383 EAKRKLHGKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEVDKANALASSLEKRQKSFDKVIAEWKAKVDDLAAEL 1462
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1463 DASQKECRNYstevfkLRAAYEESQEHYESVKRENKNLQDEVKDLMdqlgeggrSVHELEKSRKRLEMEkeelqaaleea 1542
Cdd:COG4942 100 EAQKEELAEL------LRALYRLGRQPPLALLLSPEDFLDAVRRLQ--------YLKYLAPARREQAEE----------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1543 eaaleqeenkvLRAQL-ELSQVRQEIDRRIQEKEEefentrknhqraldsmqasleaeakGKAEALRLKKKLESDINELE 1621
Cdd:COG4942 155 -----------LRADLaELAALRAELEAERAELEA-------------------------LLAELEEERAALEALKAERQ 198
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 556079866 1622 IALDHANKANAEAQKNLKKYQQNVKDLQGALEEEQRARDEAREQYASA 1669
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| RING-HC_COP1 |
cd16504 |
RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and ... |
2169-2212 |
2.50e-07 |
|
RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and similar proteins; COP1, also known as RING finger and WD repeat domain protein 2 (RFWD2) or RING finger protein 200 (RNF200), is a central regulator of photomorphogenic development in plants, which targets key transcription factors for proteasome-dependent degradation. It is localized predominantly in the nucleus, but may also be present in the cytosol. Mammalian COP1 functions as an E3 ubiquitin-protein ligase that interacts with Jun transcription factors and modulates their transcriptional activity. It also interacts with and negatively regulates the tumor-suppressor protein p53. Moreover, COP1 associates with COP9 signalosome subunit 6 (CSN6), and is involved in 14-3-3sigma ubiquitin-mediated degradation. The CSN6-COP1 link enhances ubiquitin-mediated degradation of p27(Kip1), a critical CDK inhibitor involved in cell cycle regulation, to promote cancer cell growth. Furthermore, COP1 functions as the negative regulator of ETV1 and influences prognosis in triple-negative breast cancer. COP1 contains an N-terminal extension, a C3HC4-type RING-HC finger, a coiled coil domain, and seven WD40 repeats. In human COP1, a classic leucine-rich NES, and a novel bipartite NLS is bridged by the RING-HC finger.
Pssm-ID: 438167 [Multi-domain] Cd Length: 47 Bit Score: 49.16 E-value: 2.50e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 556079866 2169 LTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYETRQRkCPKCNAP 2212
Cdd:cd16504 3 FLCPICFDIIKEAFVTKCGHSFCYKCIVKHLEQKNR-CPKCNFY 45
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
895-1267 |
2.52e-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: 56.18 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 895 DVEERLNKALTQKGDLESQLADLNDRLSHEEDAHASLSQSKKKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLN 974
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 975 DEIQHQDELINKLNKEKKHLQEASQKTSEDLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKRKVEGDL 1054
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1055 KLAQEAVADLEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEE----LEEELEAERQARAKAEKQ 1130
Cdd:TIGR04523 471 KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKleseKKEKESKISDLEDELNKD 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1131 RADLAREIEELSERLEESggatssQIELNKRREAELSKLRRDLEESNLQHEQAMSNLRKKhndtVAEMSEQIDQLNKHKA 1210
Cdd:TIGR04523 551 DFELKKENLEKEIDEKNK------EIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE----IEEKEKKISSLEKELE 620
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 556079866 1211 KVEKERATMSAEVSDLQSLLDHSNKAQANAEKQVKQLEVQLADAQFKVDEMNRTLND 1267
Cdd:TIGR04523 621 KAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
997-1254 |
2.55e-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: 55.16 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 997 ASQKTSEDLQATEDKVNHLNKVKAKLEQTLDELedslerekkargdiEKNKRKVEGDLKLAQEAVADLEKNKKEMEQNLQ 1076
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAAL--------------KKEEKALLKQLAALERRIAALARRIRALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1077 RKEKEMASLAAKledEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLAREIEELSerleesggatssqi 1156
Cdd:COG4942 80 ALEAELAELEKE---IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLK-------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1157 ELNKRREAELSKLRRDLEESNLQhEQAMSNLRKKHNDTVAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDHSNKA 1236
Cdd:COG4942 143 YLAPARREQAEELRADLAELAAL-RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
250
....*....|....*...
gi 556079866 1237 QANAEKQVKQLEVQLADA 1254
Cdd:COG4942 222 AEELEALIARLEAEAAAA 239
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1370-2169 |
2.89e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1370 YESEGLARLEELEEAKRKlHGKLQEAEEAMEQLNAKCSGLEKTKSHL-QGELEDMSIEVDKANALASSLEKRQKSFDKVI 1448
Cdd:PTZ00121 1021 NQNFNIEKIEELTEYGNN-DDVLKEKDIIDEDIDGNHEGKAEAKAHVgQDEGLKPSYKDFDFDAKEDNRADEATEEAFGK 1099
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1449 AEWKAKVDDLAAELDASQKECRNYSTEVFKLraayeESQEHYESVKR--ENKNLQDEVKDLMDQLGEGGRSVHELEKSRK 1526
Cdd:PTZ00121 1100 AEEAKKTETGKAEEARKAEEAKKKAEDARKA-----EEARKAEDARKaeEARKAEDAKRVEIARKAEDARKAEEARKAED 1174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1527 RLEMEKEELQAALEEAEAALEQEENKVLRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEA 1606
Cdd:PTZ00121 1175 AKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEI 1254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1607 LRLKKKLESDINELEIALDHANKANAEAQKN---------LKKYQQNVK-DLQGALEEEQRARDEAREQYASAERRCNAM 1676
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARKADELKKaeekkkadeAKKAEEKKKaDEAKKKAEEAKKADEAKKKAEEAKKKADAA 1334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1677 HGELEESRQLLASSKNSHLRHIEQMEGEEllmqKKLRTEVIRLEDAlvqvRKEYEMLRIEFEQNLAATEqtgpinremrh 1756
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAE----EKAEAAEKKKEEA----KKKADAAKKKAEEKKKADE----------- 1395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1757 liTSLQSHNRQLKGEVSRYKRKLREAAAEAARLKQTLEMSNVAVSSTTVPSSASSTSSDNGSSRGEEGAPVSCpqpgqgg 1836
Cdd:PTZ00121 1396 --AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKA------- 1466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1837 rEEGGTPSASSQRREEEAREEEPIPEREKGKSDLDIIRDLKAQLKKSQEAQR-ELKLLLDMYKGApKEQRDKVQLMAAEK 1915
Cdd:PTZ00121 1467 -EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKaEEAKKADEAKKA-EEAKKADEAKKAEE 1544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1916 KARAEVEEHRQQLKKLAEHERKERRKLADEDAMKKIRGLEETVASLHKSLTAQKQEVWEEALLSEMEVTGQAFEDMQEQN 1995
Cdd:PTZ00121 1545 KKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1996 LRLIQQLREKDDANFKLMSERIKSNQIHKLLQEEKAMLSEQGATLQAQVEAQNQVVRKLEEKERLLQNSLSTLEKElslr 2075
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE---- 1700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 2076 QQAAEMHRRKAVESAQSAadlklhlekylAQLKDAQGIVTDRTAVLSQETFKTKRLQEEilsLRRKVERAKKFELATNTD 2155
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKA-----------EELKKAEEENKIKAEEAKKEAEEDKKKAEE---AKKDEEEKKKIAHLKKEE 1766
|
810
....*....|....
gi 556079866 2156 EVLMEEIKEYKEQL 2169
Cdd:PTZ00121 1767 EKKAEEIRKEKEAV 1780
|
|
| RING-HC_TRIM77_C-IV |
cd16543 |
RING finger, HC subclass, found in tripartite motif-containing protein 77 (TRIM77) and similar ... |
2167-2213 |
5.13e-07 |
|
RING finger, HC subclass, found in tripartite motif-containing protein 77 (TRIM77) and similar proteins; TRIM77 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including two consecutive zinc-binding domains, a C3HC4-type RING-HC finger and Bbox2, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain.
Pssm-ID: 438205 [Multi-domain] Cd Length: 54 Bit Score: 48.54 E-value: 5.13e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 556079866 2167 EQLTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYETRQ--RKCPKCNAPF 2213
Cdd:cd16543 2 DQLTCSICLDLLKDPVTIPCGHSFCMNCITLLWDRKQgvPSCPQCRESF 50
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
843-1509 |
5.33e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 55.23 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 843 ELKAMEEKLKKTEEALAKEEKLRKELEEHNVKVLQEKNDLFLQLEAErmgAGDVEERLNKALTQKGDLESQLADLndRLS 922
Cdd:pfam12128 309 ELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSE---LENLEERLKALTGKHQDVTAKYNRR--RSK 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 923 HEEDAHASLSQSKKKLEGEISGLKKDIEDMELALQKAEQD-KATKDHQIRNLNDEiqhQDELINKLNkEKKHLQEASQKT 1001
Cdd:pfam12128 384 IKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESElREQLEAGKLEFNEE---EYRLKSRLG-ELKLRLNQATAT 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1002 SEDLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKRKVegdlklaQEAVADLEKNKKEMEQNLQRKEKE 1081
Cdd:pfam12128 460 PELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEAL-------RQASRRLEERQSALDELELQLFPQ 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1082 MASLAAKLEDEQALvaklqkqIKELQARIEeleeeleaerqarAKAEKQRADLareiEELSERLEESGGATSSQIELNKR 1161
Cdd:pfam12128 533 AGTLLHFLRKEAPD-------WEQSIGKVI-------------SPELLHRTDL----DPEVWDGSVGGELNLYGVKLDLK 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1162 R---------EAELsKLRRDLEESNLQHEQamsnlrkkhnDTVAEMSEQIDQLNKH--KAKVEKERATMSAEVSDLqsll 1230
Cdd:pfam12128 589 RidvpewaasEEEL-RERLDKAEEALQSAR----------EKQAAAEEQLVQANGEleKASREETFARTALKNARL---- 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1231 dhsNKAQANAEKQVKQLEVQLADAQFKvDEMNRTLNDLDGGKKKLaveNSELQRQLEESESQVAQLNKIKASLATQLEEA 1310
Cdd:pfam12128 654 ---DLRRLFDEKQSEKDKKNKALAERK-DSANERLNSLEAQLKQL---DKKHQAWLEEQKEQKREARTEKQAYWQVVEGA 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1311 KRmaDEEARERAAILGKYRNLEHDLDNLRE---------SVEEEQEAK-----ADFQRQLSKA---NAEAQLWRSKYESE 1373
Cdd:pfam12128 727 LD--AQLALLKAAIAARRSGAKAELKALETwykrdlaslGVDPDVIAKlkreiRTLERKIERIavrRQEVLRYFDWYQET 804
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1374 GL-------ARLEELEEAKRKLHGKL----QEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEVDKANALAssLEKRQK 1442
Cdd:pfam12128 805 WLqrrprlaTQLSNIERAISELQQQLarliADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLK--EDANSE 882
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556079866 1443 SFDKVIAEWKAKVDDL----AAELDASQKECRNYSTEVFKLRAAyeESQEHYESVKRENKNLQDEVKDLMD 1509
Cdd:pfam12128 883 QAQGSIGERLAQLEDLklkrDYLSESVKKYVEHFKNVIADHSGS--GLAETWESLREEDHYQNDKGIRLLD 951
|
|
| RING-HC_Topors |
cd16574 |
RING finger, HC subclass, found in topoisomerase I-binding arginine/serine-rich protein ... |
2170-2213 |
5.42e-07 |
|
RING finger, HC subclass, found in topoisomerase I-binding arginine/serine-rich protein (Topors) and similar proteins; Topors, also known as topoisomerase I-binding RING finger protein, tumor suppressor p53- binding protein 3, or p53-binding protein 3 (p53BP3), is a ubiquitously expressed nuclear E3 ubiquitin-protein ligase that can ligate both ubiquitin and small ubiquitin-like modifier (SUMO) to substrate proteins in the nucleus. It contains an N-terminal C3HC4-type RING-HC finger which ligates ubiquitin to its target proteins including DNA topoisomerase I, p53, NKX3.1, H2AX, and the AAV-2 Rep78/68 proteins. As a RING-dependent E3 ubiquitin ligase, Topors works with the E2 enzymes UbcH5a, UbcH5c, and UbcH6, but not with UbcH7, CDC34, or UbcH2b. Topors acts as a tumor suppressor in various malignancies. It regulates p53 modification, suggesting it may be responsible for astrocyte elevated gene-1 (AEG-1, also known as metadherin, or LYRIC) ubiquitin modification. Plk1-mediated phosphorylation of Topors inhibits Topors-mediated sumoylation of p53, whereas p53 ubiquitination is enhanced, leading to p53 degradation. It also functions as a negative regulator of the prostate tumor suppressor NKX3.1. Moreover, Topors is associated with promyelocytic leukemia nuclear bodies, and may be involved in the cellular response to camptothecin. It also plays a key role in the turnover of H2AX protein, discriminating the type of DNA damaging stress. Furthermore, Topors is a cilia-centrosomal protein associated with autosomal dominant retinal degeneration. Mutations in TOPORS cause autosomal dominant retinitis pigmentosa (adRP).
Pssm-ID: 438236 [Multi-domain] Cd Length: 47 Bit Score: 48.05 E-value: 5.42e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 556079866 2170 TCPSC--KVKRKDAVLIKCFHVFCYDCLKtRYETRQRKCPKCNAPF 2213
Cdd:cd16574 3 SCPICldRFENEKAFLDGCFHAFCFTCIL-EWSKVKNECPLCKQPF 47
|
|
| RING-HC_TRIM65_C-IV |
cd16609 |
RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar ... |
2167-2213 |
6.13e-07 |
|
RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar proteins; TRIM65 is an E3 ubiquitin-protein ligase that interacts with the innate immune receptor MDA5, enhancing its ability to stimulate interferon-beta signaling. It functions as a potential oncogenic protein that negatively regulates p53 through ubiquitination, providing insight into the development of novel approaches targeting TRIM65 for non-small cell lung carcinoma (NSCLC) treatment, and also overcoming chemotherapy resistance. Moreover, TRIM65 negatively regulates microRNA-driven suppression of mRNA translation by targeting TNRC6 proteins for ubiquitination and degradation. TRIM65 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.
Pssm-ID: 438271 [Multi-domain] Cd Length: 58 Bit Score: 48.14 E-value: 6.13e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 556079866 2167 EQLTCPSCKVKRKDAVLIKCFHVFCYDCLK---TRYETRQRKCPKCNAPF 2213
Cdd:cd16609 2 EELTCSICLGLYQDPVTLPCQHSFCRACIEdhwRQKDEGSFSCPECRAPF 51
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
941-1389 |
6.43e-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: 54.96 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 941 EISGLKKDIEDMELALQK------AEQDKATKDHQIRNLNDEIQH---QDELINKlnKEKKHLQEASQKTSEDLQATEDK 1011
Cdd:COG3096 223 ENSGVRKAFQDMEAALREnrmtleAIRVTQSDRDLFKHLITEATNyvaADYMRHA--NERRELSERALELRRELFGARRQ 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1012 vnhLNKVKAKLEQTLDELEDSLEREKkargDIEKNKRKVEGDLKLAQEAVADLEKnkkemeqnLQRKEKEMASLAAKLED 1091
Cdd:COG3096 301 ---LAEEQYRLVEMARELEELSARES----DLEQDYQAASDHLNLVQTALRQQEK--------IERYQEDLEELTERLEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1092 EQALVAKLQKQIKELQARIEELEEELEAER-------------QARAKAEKQ-RADLAREIEELSERLEESGGATSSQIE 1157
Cdd:COG3096 366 QEEVVEEAAEQLAEAEARLEAAEEEVDSLKsqladyqqaldvqQTRAIQYQQaVQALEKARALCGLPDLTPENAEDYLAA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1158 LnKRREAELSKLRRDLE-------ESNLQHEQAMSNLRKKHNDTVAEMS-----EQIDQLNKHKAKVEKErATMSAEVSD 1225
Cdd:COG3096 446 F-RAKEQQATEEVLELEqklsvadAARRQFEKAYELVCKIAGEVERSQAwqtarELLRRYRSQQALAQRL-QQLRAQLAE 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1226 LQSLLDhsnkAQANAEKQVKQLEVQLadaqfkvdemNRTLNDLDggkkKLAVENSELQRQLEESESQVAQLNKIKASLAT 1305
Cdd:COG3096 524 LEQRLR----QQQNAERLLEEFCQRI----------GQQLDAAE----ELEELLAELEAQLEELEEQAAEAVEQRSELRQ 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1306 QLEEAKRMADEEARERAAILGKYRNLEHDLDNLRESVEEEQEAKADFQRQLSKanaEAQLWRSKyeSEGLARLEELEEAK 1385
Cdd:COG3096 586 QLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLER---EREATVER--DELAARKQALESQI 660
|
....
gi 556079866 1386 RKLH 1389
Cdd:COG3096 661 ERLS 664
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1482-2164 |
8.14e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.59 E-value: 8.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1482 AYEESQEHYESVKRENKNLQDEVKDLMDQLGEGGRSVHELEKSRKRLEmEKEELQAALEEAEAALEQEENKVLRAQLELS 1561
Cdd:TIGR00618 185 EFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLR-EALQQTQQSHAYLTQKREAQEEQLKKQQLLK 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1562 QVRQEIDR-RIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRLKKKLESDINELEIALDHankaNAEAQKNLKK 1640
Cdd:TIGR00618 264 QLRARIEElRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMK----RAAHVKQQSS 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1641 YQQNVKDLQGALEEEQRARDEAREQYASAERRCNAmHGELEESRQL------------LASSKNSHLRHIEQMEGEELLM 1708
Cdd:TIGR00618 340 IEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQ-HTLTQHIHTLqqqkttltqklqSLCKELDILQREQATIDTRTSA 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1709 QKKLRTEVIRLEDALVQVRKEYEMLRIEFEQNLAATEQTGPINREMRHLITSLQSHNRQLKGEVSRYKRKLREAAAEAAR 1788
Cdd:TIGR00618 419 FRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLE 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1789 LKQT----------LEMSNVAVSSTTVPSSASSTSSDNGSSRGEEGAPVScpqpGQGGREEGGTPSASSQRREEEAREEE 1858
Cdd:TIGR00618 499 LQEEpcplcgscihPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVY----HQLTSERKQRASLKEQMQEIQQSFSI 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1859 PIPEREKGKSDLDIIRDLKAQLKKSQEAQRELKlllDMYKGAPKEQRDKVQLMAAEKKARAEVEEHRQQLKKLAEHERKE 1938
Cdd:TIGR00618 575 LTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE---DMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHAL 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1939 RRKLADEDAMKKIRgleetvaslhkSLTAQKQEVWEEALLSEMEvtgqafedMQEQNLRLIQQLREKDDANFKLMSERIK 2018
Cdd:TIGR00618 652 QLTLTQERVREHAL-----------SIRVLPKELLASRQLALQK--------MQSEKEQLTYWKEMLAQCQTLLRELETH 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 2019 SNQIHKLLQEEKAMLSEQGATLQAQVEAQNQVVRKLEE------KERLLQNSLSTLE--------KELSLRQQAAEMHRR 2084
Cdd:TIGR00618 713 IEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHqartvlKARTEAHFNNNEEvtaalqtgAELSHLAAEIQFFNR 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 2085 KAVESAQSAADLKLHLEKYLAQLKDA-----QGIVTDRTAVLSQETFKTKRLQEEILSLRRKVERAKKFELATNTDEVLM 2159
Cdd:TIGR00618 793 LREEDTHLLKTLEAEIGQEIPSDEDIlnlqcETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKII 872
|
....*
gi 556079866 2160 EEIKE 2164
Cdd:TIGR00618 873 QLSDK 877
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1093-1404 |
1.05e-06 |
|
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: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1093 QALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLAREIEElserleesggaTSSQIELN--KRREAELSKLR 1170
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEY-----------SWDEIDVAsaEREIAELEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1171 RDLEESnlqheqamsnlrkkhNDTVAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQslldhsnKAQANAEKQVKQLEVQ 1250
Cdd:COG4913 678 ERLDAS---------------SDDLAALEEQLEELEAELEELEEELDELKGEIGRLE-------KELEQAEEELDELQDR 735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1251 LADAQFKVDEmnRTLNDLDGGKKKLAVENSElQRQLEESESQVAQLNKIKASLATQLEEAKR-------MADEEARERAA 1323
Cdd:COG4913 736 LEAAEDLARL--ELRALLEERFAAALGDAVE-RELRENLEERIDALRARLNRAEEELERAMRafnrewpAETADLDADLE 812
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1324 ILGKYRNLehdLDNLRESVEEEQEAKadFQRQLSKANaeaqlwrskyeseglarLEELEEAKRKLHGKLQEAEEAMEQLN 1403
Cdd:COG4913 813 SLPEYLAL---LDRLEEDGLPEYEER--FKELLNENS-----------------IEFVADLLSKLRRAIREIKERIDPLN 870
|
.
gi 556079866 1404 A 1404
Cdd:COG4913 871 D 871
|
|
| RING-HC_RNF39 |
cd16592 |
RING finger, HC subclass, found in RING finger protein 39 (RNF39) and similar proteins; RNF39, ... |
2167-2213 |
1.31e-06 |
|
RING finger, HC subclass, found in RING finger protein 39 (RNF39) and similar proteins; RNF39, also called protein HZFw, may play a role in prolonged long term-potentiation (LTP) maintenance. It is involved in the etiology of Behcet's disease (BD). It may also be involved in HIV-1 replication. RNF39 acts as an E3 ubiquitin ligase that inhibits retinoic acid-inducible gene-I (RIG-I)-like receptor (RLR) pathways by mediating K48-linked ubiquitination and proteasomal degradation of DDX3X (DEAD-box RNA helicase 3, X-linked). RNF39 contains a typical C3HC4-type RING-HC finger.
Pssm-ID: 438254 [Multi-domain] Cd Length: 58 Bit Score: 47.44 E-value: 1.31e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 556079866 2167 EQLTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYETRQRK--------CPKCNAPF 2213
Cdd:cd16592 3 EETTCPICLGYFKDPVILDCEHSFCRACIARHWGQEAMEgngaegvfCPQCGEPC 57
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1193-1385 |
1.41e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1193 DTVAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDHSNKAQANAEKQVKQLEVQLADAQFKVDEMNRTLNDL---- 1268
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaral 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1269 ---DGGKKKLAV--------------------------ENSELQRQLEESESQVAQLNKIKASLATQLEEAKRMADEEAR 1319
Cdd:COG3883 96 yrsGGSVSYLDVllgsesfsdfldrlsalskiadadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556079866 1320 ERAAILGKYRNLEHDLDNLRESVEEEQEAKADFQRQLSKANAEAQLWRSKYESEGLARLEELEEAK 1385
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| vRING-HC-C4C4_RBBP6 |
cd16620 |
Variant RING finger, HC subclass (C4C4-type), found in retinoblastoma-binding protein 6 (RBBP6) ... |
2167-2213 |
1.45e-06 |
|
Variant RING finger, HC subclass (C4C4-type), found in retinoblastoma-binding protein 6 (RBBP6) and similar proteins; RBBP6, also known as proliferation potential-related protein, protein P2P-R, retinoblastoma-binding Q protein 1 (RBQ-1), or p53-associated cellular protein of testis (PACT), is a nuclear E3 ubiquitin-protein ligase involved in multiple processes, such as the control of gene expression, mitosis, cell differentiation, and cell apoptosis. It plays a role in both promoting and inhibiting apoptosis in many human cancers, including esophageal, lung, hepatocellular, and colon cancers, familial myeloproliferative neoplasms, as well as in human immunodeficiency virus-associated nephropathy (HIVAN). It functions as an Rb- and p53-binding protein that plays an important role in chaperone-mediated ubiquitination and possibly in protein quality control. It acts as a scaffold protein to promote the assembly of the p53/TP53-MDM2 complex, resulting in an increase of MDM2-mediated ubiquitination and degradation of p53/TP53, and leading to both apoptosis and cell growth. It is also a double-stranded RNA-binding protein that plays a role in mRNA processing by regulating the human polyadenylation machinery and modulating expression of mRNAs with AU-rich 3' untranslated regions (UTRs). Moreover, RBBP6 ubiquitinates and destabilizes the transcriptional repressor ZBTB38 that negatively regulates transcription and levels of the MCM10 replication factor on chromatin. Furthermore, RBBP6 is involved in tunicamycin-induced apoptosis by mediating protein kinase (PKR) activation. RBBP6 contains an N-terminal ubiquitin-like domain and a C4C4-type RING finger, whose overall folding is similar to that of the typical C3HC4-type RING-HC finger. RBBP6 interacts with chaperones Hsp70 and Hsp40 through its N-terminal ubiquitin-like domain. It promotes the ubiquitination of p53 by Hdm2 in an E4-like manner through its RING finger. It also interacts directly with the pro-proliferative transcription factor Y-box-binding protein-1 (YB-1) via its RING finger.
Pssm-ID: 438282 [Multi-domain] Cd Length: 55 Bit Score: 47.01 E-value: 1.45e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 556079866 2167 EQLTCPSCKVKRKDAVLIKC-FHVFCYDCLKTRYETRQRKCPKCNAPF 2213
Cdd:cd16620 2 DELKCPICKDLMKDAVLTPCcGNSFCDECIRTALLEEDFTCPTCKEPD 49
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
933-1317 |
1.50e-06 |
|
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: 53.48 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 933 QSKKKLEGEI-SGLKKDIEDMELALQKaeqdkaTKDHQIRNLNDEIQH-QDELINKLNK-EKKHLQEASQKTSEDLQATE 1009
Cdd:NF033838 54 ESQKEHAKEVeSHLEKILSEIQKSLDK------RKHTQNVALNKKLSDiKTEYLYELNVlKEKSEAELTSKTKKELDAAF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1010 DKvnhLNKVKAKLEQTLDELEDSL-EREKKARGDIEKNKRK-------------VEGDLKLAQeavADLEKNKKEMEQNl 1075
Cdd:NF033838 128 EQ---FKKDTLEPGKKVAEATKKVeEAEKKAKDQKEEDRRNyptntyktleleiAESDVEVKK---AELELVKEEAKEP- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1076 qRKEKEMASLAAKLEDEQALVAKLQKqIKELQARieeleEELEAERQARAKAEKQRADLAREIEELSERLEESGGATSSQ 1155
Cdd:NF033838 201 -RDEEKIKQAKAKVESKKAEATRLEK-IKTDREK-----AEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1156 IELNKRREaelsklrrDLEESNLQ-HEQAMSNLRKKHNDTVAEMSEQIDQLNKhKAKVEKERatmsaevsdlqsllDHSN 1234
Cdd:NF033838 274 ATPDKKEN--------DAKSSDSSvGEETLPSPSLKPEKKVAEAEKKVEEAKK-KAKDQKEE--------------DRRN 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1235 KAQANaekqVKQLEVQLADAQFKVDEMNRTLNDLDGGKKKLAVENSELQRQLEESESQVAQLNKIKASLATQLEEAKRMA 1314
Cdd:NF033838 331 YPTNT----YKTLELEIAESDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEEEAKRKA 406
|
...
gi 556079866 1315 DEE 1317
Cdd:NF033838 407 AEE 409
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
647-671 |
1.78e-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: 50.04 E-value: 1.78e-06
10 20
....*....|....*....|....*
gi 556079866 647 YREQLNKLMATLNSTSPHFVRCIIP 671
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
842-1312 |
1.99e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 842 DELKAMEEKLKKteealakeeklrkeleehnvkvLQEKNDLFLQLEAERMGAgdvEERLNKALTQKGDLESQLADLNDRL 921
Cdd:COG4717 71 KELKELEEELKE----------------------AEEKEEEYAELQEELEEL---EEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 922 SHEEDAhaslsQSKKKLEGEISGLKKDIEdmelALQKAEQDKATKDHQIRNLNDEI-QHQDELINKLNKEKKHLQEASQK 1000
Cdd:COG4717 126 QLLPLY-----QELEALEAELAELPERLE----ELEERLEELRELEEELEELEAELaELQEELEELLEQLSLATEEELQD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1001 TSEDLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKRKVEGDLKLAQEA-VADLEKNKKEMEQNLQRKE 1079
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAaLLALLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1080 KEMASLAAkledeqALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLAREIEELSERLEESGGATSSQIELn 1159
Cdd:COG4717 277 GVLFLVLG------LLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL- 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1160 KRREAELSKLRRDLEESNLQHEQA--MSNLRKKHNDTVAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDHSNKAQ 1237
Cdd:COG4717 350 QELLREAEELEEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1238 ANAEKQvkQLEVQLADAQFKVDEMNRTLNDLDGGKKKLAVEN--SELQRQLEESESQVAQLNKIKASL---ATQLEEAKR 1312
Cdd:COG4717 430 LEEELE--ELEEELEELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRELAEEWAALklaLELLEEARE 507
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1391-2108 |
2.29e-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: 53.30 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1391 KLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEVDKANAlasslEKRQKsFDKVIAEWKAKVDDLAAELDAsqkecr 1470
Cdd:pfam12128 245 KLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSA-----ELNQL-LRTLDDQWKEKRDELNGELSA------ 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1471 nystevfkLRAAYEESQEHYESVKRENKNLQDE----VKDLMDQLGEGGRSVHELEKSRKRLEMEKEELQAALEEAEAAL 1546
Cdd:pfam12128 313 --------ADAAVAKDRSELEALEDQHGAFLDAdietAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKI 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1547 EQEENKVL-RAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEAL-RLKKKLESDINELEIAL 1624
Cdd:pfam12128 385 KEQNNRDIaGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLgELKLRLNQATATPELLL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1625 DHANKANA--EAQKNLKKYQQNVKDLQGALEEEQRARDEAREQYASAERRCNAMHGELEESRQLLASSKNSHLRHieqme 1702
Cdd:pfam12128 465 QLENFDERieRAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHF----- 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1703 geellmqkkLRTEVIRLEDALVQVRKEYEMLRIEFEQNLAATEQTGPIN------REMRHLITSLQSHNRQLKGEVSRYK 1776
Cdd:pfam12128 540 ---------LRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNlygvklDLKRIDVPEWAASEEELRERLDKAE 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1777 RKLREAAAEAARLKQTLEMSNVAVssttvpssasstssdNGSSRGEEGApvscPQPGQGGREEGGTPSASSQRREEEARE 1856
Cdd:pfam12128 611 EALQSAREKQAAAEEQLVQANGEL---------------EKASREETFA----RTALKNARLDLRRLFDEKQSEKDKKNK 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1857 EEPIPEREKGKSDLDIIRDLKAQLKKSQ---EAQRELKLLLDMYKGAPK---EQRDKVQLMAAEKKARAEVEEHRQQLKK 1930
Cdd:pfam12128 672 ALAERKDSANERLNSLEAQLKQLDKKHQawlEEQKEQKREARTEKQAYWqvvEGALDAQLALLKAAIAARRSGAKAELKA 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1931 LAEHERKERRKLA-DEDamkKIRGLEETVASLHKSLtaqkqevwEEALLSEMEVTgQAFEDMQE----QNLRLIQQLREK 2005
Cdd:pfam12128 752 LETWYKRDLASLGvDPD---VIAKLKREIRTLERKI--------ERIAVRRQEVL-RYFDWYQEtwlqRRPRLATQLSNI 819
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 2006 DDANFKLMSERIKSNQIHKLlqEEKAMLSEQGATLQAQVEAqNQVVRKLeekeRLLQNSLSTLEKELSLRQQAAEM-HRR 2084
Cdd:pfam12128 820 ERAISELQQQLARLIADTKL--RRAKLEMERKASEKQQVRL-SENLRGL----RCEMSKLATLKEDANSEQAQGSIgERL 892
|
730 740
....*....|....*....|....*
gi 556079866 2085 KAVESAQSAAD-LKLHLEKYLAQLK 2108
Cdd:pfam12128 893 AQLEDLKLKRDyLSESVKKYVEHFK 917
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
793-1316 |
2.57e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 793 KKHFQKLKEQRVALLVIQRNLRKFLQLRnwlwwKLYSKVKPLLSAV-----RVEDELKAMEEKLKKTEEALAKEEKLRKE 867
Cdd:PRK03918 272 KKEIEELEEKVKELKELKEKAEEYIKLS-----EFYEEYLDELREIekrlsRLEEEINGIEERIKELEEKEERLEELKKK 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 868 LeehnVKVLQEKNDLFLQLEAERMgAGDVEERLNKALTQKGDLEsqLADLNDRLSHEEDAHASLSQSKKKLEGEISGLKK 947
Cdd:PRK03918 347 L----KELEKRLEELEERHELYEE-AKAKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 948 DIEDMELALQKAEQDKATKDHQIRNLNDEiqHQDELINKLNKEKKhlqeasqKTSEDLQATEDKVNHLNKVKAKLEQTLD 1027
Cdd:PRK03918 420 EIKELKKAIEELKKAKGKCPVCGRELTEE--HRKELLEEYTAELK-------RIEKELKEIEEKERKLRKELRELEKVLK 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1028 ElEDSLEREKKARGDIEKNKRKVEG-DLKLAQEAVADLEKNKKEmeqnLQRKEKEMASLAAKLEDEQALVAKLQKQIKEL 1106
Cdd:PRK03918 491 K-ESELIKLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEK----LIKLKGEIKSLKKELEKLEELKKKLAELEKKL 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1107 QarieeleeeleaerqaraKAEKQRADLAREIEELSERLEESGGATSSQIELNKRREAELSKLRRDLEEsnlqheqamsn 1186
Cdd:PRK03918 566 D------------------ELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELER----------- 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1187 LRKKHNDTVAEMSEQIDQLNKHKAKVEKERATMSaEVSDLQSLLDHSNKAQANAE--KQVKQLEVQLADAQFKVDEMNRT 1264
Cdd:PRK03918 617 EEKELKKLEEELDKAFEELAETEKRLEELRKELE-ELEKKYSEEEYEELREEYLElsRELAGLRAELEELEKRREEIKKT 695
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 556079866 1265 LNDLDGGKKKL---AVENSELQRQLEESESQVAQLNKIKASLATQ-LEEAKRMADE 1316
Cdd:PRK03918 696 LEKLKEELEERekaKKELEKLEKALERVEELREKVKKYKALLKERaLSKVGEIASE 751
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
843-1304 |
2.88e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.60 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 843 ELKAMEEKLKKTEEALAKEEKLRKELEEHNVKvLQEKNDLFLQLEAERMGAGdvEERLNKALTQKGDLESQ---LADLND 919
Cdd:PRK01156 243 ELSSLEDMKNRYESEIKTAESDLSMELEKNNY-YKELEERHMKIINDPVYKN--RNYINDYFKYKNDIENKkqiLSNIDA 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 920 RLSHEEDAHASLSQ---------SKKKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLNDEIQHQDELINKLNKE 990
Cdd:PRK01156 320 EINKYHAIIKKLSVlqkdyndyiKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKI 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 991 KKHLQEASQKTSE----DLQATEDKVNHLNKVKAKLEQTLDELEDSL------------------EREKKARGDIEKNKR 1048
Cdd:PRK01156 400 QEIDPDAIKKELNeinvKLQDISSKVSSLNQRIRALRENLDELSRNMemlngqsvcpvcgttlgeEKSNHIINHYNEKKS 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1049 KVEGDLKLAQEAVADLEKNKKEMEQNLQRKEKEMASlaaKLEDEQALVAKLQKQIKELQARIEELEEELEAERQAraKAE 1128
Cdd:PRK01156 480 RLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEIN---KSINEYNKIESARADLEDIKIKINELKDKHDKYEEI--KNR 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1129 KQRADLAREIEELSERLEESGGATSSQIELNKRREAELSKLRRDLEESNLQHEQAMSNLRKKHNDTVAEMSEQIDQLNKH 1208
Cdd:PRK01156 555 YKSLKLEDLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNK 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1209 KAKVEKERA---TMSAEVSDLQSL---LDHSNKAQANAEKQVKQLEVQLADAQFKVDEMNRTLNDLDGGKKKLAVENSEL 1282
Cdd:PRK01156 635 YNEIQENKIlieKLRGKIDNYKKQiaeIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINEL 714
|
490 500
....*....|....*....|..
gi 556079866 1283 QRQLEESESQVAQLNKIKASLA 1304
Cdd:PRK01156 715 SDRINDINETLESMKKIKKAIG 736
|
|
| RING-HC_RNF166 |
cd16549 |
RING finger, HC subclass, found in RING finger protein 166 (RNF166) and similar proteins; ... |
2168-2213 |
3.24e-06 |
|
RING finger, HC subclass, found in RING finger protein 166 (RNF166) and similar proteins; RNF166 is encoded by the gene RNF166 targeted by thyroid hormone receptor alpha1 (TRalpha1), which is important in brain development. It plays an important role in RNA virus-induced interferon-beta production by enhancing the ubiquitination of TRAF3 and TRAF6. RNF166, together with three closely related proteins: RNF114, RNF125 and RNF138, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM).
Pssm-ID: 438211 [Multi-domain] Cd Length: 47 Bit Score: 45.96 E-value: 3.24e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 556079866 2168 QLTCPSC-KVKRKDAVLIKCFHVFCYDCLKTRYETRQRKCPKCNAPF 2213
Cdd:cd16549 1 QFSCPIClEVYHKPVVITSCGHTFCGECLQPCLQVASPLCPLCRMPF 47
|
|
| RING-HC_TRIM69_C-IV |
cd16611 |
RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar ... |
2167-2217 |
3.28e-06 |
|
RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar proteins; TRIM69, also known as RFP-like domain-containing protein trimless or RING finger protein 36 (RNF36), is a testis E3 ubiquitin-protein ligase that plays a specific role in apoptosis and may also play an important role in germ cell homeostasis during spermatogenesis. TRIM69 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.
Pssm-ID: 438273 [Multi-domain] Cd Length: 59 Bit Score: 46.29 E-value: 3.28e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 556079866 2167 EQLTCPSCKVKRKDAVLIKCFHVFCYDCLkTRYETRQRK---CPKCNAPFGTND 2217
Cdd:cd16611 3 EELHCPLCLDFFRDPVMLSCGHNFCQSCI-TGFWELQAEdttCPECRELCQYRN 55
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1278-1522 |
3.33e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 51.46 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1278 ENSELQRQLEESESQV-AQLNKIKASLATQLEEAKRMADEEARERAAILGKYRNLEHDLDNLRESVEEE----QEAKADF 1352
Cdd:pfam00038 26 QNKLLETKISELRQKKgAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDElnlrTSAENDL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1353 QrQLSKANAEAQLWRSKYESEGLARLEEL-------EEAKRKLHGKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSi 1425
Cdd:pfam00038 106 V-GLRKDLDEATLARVDLEAKIESLKEELaflkknhEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIA- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1426 evdkanalasslekrQKSFDKVIAEWKAKVDDLAAELDASQKECRNYSTEVFKLRAAYEESQEHYESVKRENKNLQDEVK 1505
Cdd:pfam00038 184 ---------------AKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLA 248
|
250 260
....*....|....*....|.
gi 556079866 1506 DLMD----QLGEGGRSVHELE 1522
Cdd:pfam00038 249 ETEEryelQLADYQELISELE 269
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
975-1250 |
3.70e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.61 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 975 DEIQHQdelINKLNKEKkhLQEASQKTS-EDLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKRKVEGD 1053
Cdd:PRK11281 39 ADVQAQ---LDALNKQK--LLEAEDKLVqQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1054 LK--LAQEAVADLEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEeleeeleaerQARAKAEKQR 1131
Cdd:PRK11281 114 TRetLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQ----------QIRNLLKGGK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1132 AdlareieelserleesGGATSSQIELNKrREAELSKL--RRDLEESNLQHEQAMSNLRKKHNDtvaEMSEQIDQLNKhk 1209
Cdd:PRK11281 184 V----------------GGKALRPSQRVL-LQAEQALLnaQNDLQRKSLEGNTQLQDLLQKQRD---YLTARIQRLEH-- 241
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 556079866 1210 akvekeratmsaEVSDLQSLLDHSNKAQanAEKQVKQLEVQ 1250
Cdd:PRK11281 242 ------------QLQLLQEAINSKRLTL--SEKTVQEAQSQ 268
|
|
| mRING_PEX12 |
cd16451 |
Modified RING finger found in peroxin-12 (PEX12) and similar proteins; PEX12, also known as ... |
2170-2222 |
3.71e-06 |
|
Modified RING finger found in peroxin-12 (PEX12) and similar proteins; PEX12, also known as peroxisome assembly protein 12 or peroxisome assembly factor 3 (PAF-3), is a RING finger domain-containing integral membrane peroxin required for protein import into peroxisomes. Mutations in human PEX12 result in the peroxisome deficiency Zellweger syndrome of complementation group III (CG-III), a lethal neurological disorder. PEX12 also functions as an E3-ubiquitin ligase that facilitates the PEX4-dependent monoubiquitination of PEX5, a key player in peroxisomal matrix protein import, to control PEX5 receptor recycling or degradation. PEX12 contains a modified RING finger that lacks the third, fourth, and eighth zinc-binding residues of the consensus RING finger motif, suggesting PEX12 may only bind one zinc ion.
Pssm-ID: 438115 [Multi-domain] Cd Length: 54 Bit Score: 46.08 E-value: 3.71e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 556079866 2170 TCPSCKVKRK-DAVLIKCFHVFCYDCLkTRYETRQRKCPKCNAPFGTNDYHRLY 2222
Cdd:cd16451 2 ICPLCRKKRTnPTALATSGYVFCYPCI-YRYVKEHGRCPVTGYPASLDHLIKLY 54
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1157-1582 |
4.03e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1157 ELNKRREaELSKLRRDLEESNLQHEQAMSNLRKKHNDTVAEMSEQIDQLnkhkAKVEKERATMSAEVSDLQSLLDHSNKA 1236
Cdd:COG4717 50 RLEKEAD-ELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEEL----EELEEELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1237 QANAE--KQVKQLEVQLADAQFKVDEMNRTLNDLdggkkklavenSELQRQLEESESQVAQLNKIKASLATQLEEAKRMA 1314
Cdd:COG4717 125 LQLLPlyQELEALEAELAELPERLEELEERLEEL-----------RELEEELEELEAELAELQEELEELLEQLSLATEEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1315 DEE-ARERAAILGKYRNLEHDLDNLRESVEEEQEAKADFQRQLSKANAEAQLWRSKYESEGLARLEELE----------- 1382
Cdd:COG4717 194 LQDlAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLglggsllslil 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1383 ------------------EAKRKLHGKLQEAEEAmeQLNAKCSGLEKTKshLQGELEDMSIEVDKANALASSLEKRQKSF 1444
Cdd:COG4717 274 tiagvlflvlgllallflLLAREKASLGKEAEEL--QALPALEELEEEE--LEELLAALGLPPDLSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1445 DKVIAEWKAKVDDLaaELDASQKECRNYSTEV-FKLRAAYEESQEHYEsvkrENKNLQDEVKDLMDQLGEGGRSVHELEK 1523
Cdd:COG4717 350 QELLREAEELEEEL--QLEELEQEIAALLAEAgVEDEEELRAALEQAE----EYQELKEELEELEEQLEELLGELEELLE 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556079866 1524 SRKRLEMEKEELQAALEEAEAAleqeeNKVLRAQLELSQVRQEI-----DRRIQEKEEEFENTR 1582
Cdd:COG4717 424 ALDEEELEEELEELEEELEELE-----EELEELREELAELEAELeqleeDGELAELLQELEELK 482
|
|
| RING-HC_RNF138 |
cd16544 |
RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins; ... |
2167-2214 |
4.42e-06 |
|
RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins; RNF138, also known as Nemo-like kinase-associated RING finger protein (NARF) or NLK-associated RING finger protein, is an E3 ubiquitin-protein ligase that plays an important role in glioma cell proliferation, apoptosis, and cell cycle. It specifically cooperates with the E2 conjugating enzyme E2-25K (Hip-2/UbcH1), regulates the ubiquitylation and degradation of T cell factor/lymphoid enhancer factor (TCF/LEF), and further suppresses Wnt-beta-catenin signaling. RNF138, together with three closely related proteins: RNF114, RNF125 and RNF166, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM).
Pssm-ID: 438206 [Multi-domain] Cd Length: 53 Bit Score: 45.86 E-value: 4.42e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 556079866 2167 EQLTCPSCKVKRKDAV-LIKCFHVFCYDCLKTRYETRQRKCPKCNAPFG 2214
Cdd:cd16544 1 AELTCPVCQEVLKDPVeLPPCRHIFCKACILLALRSSGARCPLCRGPVG 49
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1020-1370 |
5.02e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1020 AKLEQTLDELEDSLEREKKARGDIEKNKRKVEgDLKLAQEAVADL---EKNKKEMEQNLQRKEKEMASLaaklEDEQALV 1096
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQ-ERREALQRLAEYswdEIDVASAEREIAELEAELERL----DASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1097 AKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLAREIEELSERLEESGGATSSQI--ELNKRREAELSKLRRDLE 1174
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELraLLEERFAAALGDAVEREL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1175 ESNLQHEQAmsNLRKKHNDTVAEMseqIDQLNKHKAKVEKERATMSAEVSDLQSLLDHSNKAQANAekqVKQLEVQLADA 1254
Cdd:COG4913 768 RENLEERID--ALRARLNRAEEEL---ERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDG---LPEYEERFKEL 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1255 qfKVDEMNRTLNDLdggkkklaveNSELQRQLEESESQVAQLNKIKASLA----TQLE-EAKRMADEEARERaailgkYR 1329
Cdd:COG4913 840 --LNENSIEFVADL----------LSKLRRAIREIKERIDPLNDSLKRIPfgpgRYLRlEARPRPDPEVREF------RQ 901
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 556079866 1330 NLEHDLDNLRESVEEEQEAKAD-----FQRQLSKANAEAQLWRSKY 1370
Cdd:COG4913 902 ELRAVTSGASLFDEELSEARFAalkrlIERLRSEEEESDRRWRARV 947
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
840-1110 |
5.04e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 840 VEDELKAMEEKLKKTEEALAKeeklrkeleehnvkvLQEKNDLFlqleaermgagDVEERLNKALTQKGDLESQLADLND 919
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEE---------------FRQKNGLV-----------DLSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 920 RLSHEEDAHASLSQSKKKLEGEISGLKKD--IEDMELALQKAEQDKA------TKDH-QIRNLNDEIQhqdELINKLNKE 990
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAelsaryTPNHpDVIALRAQIA---ALRAQLQQE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 991 KKHLQEASQKTSEDLQATEdkvnhlnkvkAKLEQTLDELEDSLERekkargdieknkrkvegdlklaqeaVADLEKNKKE 1070
Cdd:COG3206 311 AQRILASLEAELEALQARE----------ASLQAQLAQLEARLAE-------------------------LPELEAELRR 355
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 556079866 1071 MEQNLQRKEKEMASLAAKLEDeqalvAKLQKQIKELQARI 1110
Cdd:COG3206 356 LEREVEVARELYESLLQRLEE-----ARLAEALTVGNVRV 390
|
|
| RING-HC_TRIM7-like_C-IV |
cd16594 |
RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM7, TRIM11 and ... |
2166-2214 |
7.25e-06 |
|
RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM7, TRIM11 and TRIM27, and similar proteins; TRIM7, TRIM11 and TRIM27, closely related tripartite motif-containing proteins, belong to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. TRIM7, also known as glycogenin-interacting protein (GNIP) or RING finger protein 90 (RNF90), is an E3 ubiquitin-protein ligase that mediates c-Jun/AP-1 activation by Ras signalling. Its phosphorylation and activation by MSK1 in response to direct activation by the Ras-Raf-MEK-ERK pathway can stimulate TRIM7 E3 ubiquitin ligase activity in mediating Lys63-linked ubiquitination of the AP-1 coactivator RACO-1, leading to RACO-1 protein stabilization. Moreover, TRIM7 binds and activates glycogenin, the self-glucosylating initiator of glycogen biosynthesis. TRIM11, also known as protein BIA1, or RING finger protein 92 (RNF92), is an E3 ubiquitin-protein ligase involved in the development of the central nervous system. It is overexpressed in high-grade gliomas and promotes proliferation, invasion, migration and glial tumor growth. TRIM11 acts as a potential therapeutic target for congenital central hypoventilation syndrome (CCHS) by mediating the degradation of CCHS-associated polyalanine-expanded Phox2b. TRIM11 modulates the function of neurogenic transcription factor Pax6 through the ubiquitin-proteosome system, and thus plays an essential role for Pax6-dependent neurogenesis. It also binds to and destabilizes a key component of the activator-mediated cofactor complex (ARC105), humanin, a neuroprotective peptide against Alzheimer's disease-relevant insults, and further regulates ARC105 function in transforming growth factor beta (TGFbeta) signaling. Moreover, TRIM11 negatively regulates retinoic acid-inducible gene-I (RIG-I)-mediated interferon-beta (IFNbeta) production and antiviral activity by targeting TANK-binding kinase-1 (TBK1). It may contribute to the endogenous restriction of retroviruses in cells. It enhances N-tropic murine leukemia virus (N-MLV) entry by interfering with Ref1 restriction. It also suppresses the early steps of human immunodeficiency virus HIV-1 transduction, resulting in decreased reverse transcripts. TRIM27, also known as RING finger protein 76 (RNF76), RET finger protein (RFP), or zinc finger protein RFP, is a nuclear E3 ubiquitin-protein ligase that is highly expressed in testis and in various tumor cell lines. Expression of TRIM27 is associated with prognosis of colon and endometrial cancers. TRIM27 was first identified as a fusion partner of the RET receptor tyrosine kinase. It functions as a transcriptional repressor and associates with several proteins involved in transcriptional activity, such as enhancer of polycomb 1 (Epc1), a member of the Polycomb group proteins, and Mi-2beta, a main component of the nucleosome remodeling and deacetylase (NuRD) complex, and the cell cycle regulator retinoblastoma protein (RB1). It also interacts with HDAC1, leading to downregulation of thioredoxin binding protein 2 (TBP-2), which inhibits the function of thioredoxin. Moreover, TRIM27 mediates Pax7-induced ubiquitination of MyoD in skeletal muscle atrophy. In addition, it inhibits muscle differentiation by modulating serum response factor (SRF) and Epc1. TRIM27 promotes a non-canonical polyubiquitination of PTEN, a lipid phosphatase that catalyzes PtdIns(3,4,5)P3 (PIP3) to PtdIns(4,5)P2 (PIP2). It is an IKKepsilon-interacting protein that regulates IkappaB kinase (IKK) function and negatively regulates signaling involved in the antiviral response and inflammation. TRIM27 also forms a protein complex with MBD4 or MBD2 or MBD3, and thus plays an important role in the enhancement of transcriptional repression through MBD proteins in tumorigenesis, spermatogenesis, and embryogenesis. It is a component of an estrogen receptor 1 (ESR1) regulatory complex that is involved in estrogen receptor-mediated transcription in MCF-7 cells.
Pssm-ID: 438256 [Multi-domain] Cd Length: 61 Bit Score: 45.37 E-value: 7.25e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 556079866 2166 KEQLTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYETRQRK--CPKCNAPFG 2214
Cdd:cd16594 3 QEELTCPICLDYFTDPVTLDCGHSFCRACIARCWEEPETSasCPQCRETCP 53
|
|
| RING-HC_RNFT1-like |
cd16532 |
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein ... |
2170-2209 |
8.46e-06 |
|
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein RNFT1, RNFT2, and similar proteins; Both RNFT1 and RNFT2 are multi-pass membrane proteins containing a C3HC4-type RING-HC finger. Their biological roles remain unclear.
Pssm-ID: 438194 [Multi-domain] Cd Length: 41 Bit Score: 44.60 E-value: 8.46e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 556079866 2170 TCPSCKVKRKDAVLIKCFHVFCYDCLKTRYEtRQRKCPKC 2209
Cdd:cd16532 2 ICPICQDEFKDPVVLRCKHIFCEDCVSEWFE-RERTCPLC 40
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1878-2095 |
1.16e-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: 50.15 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1878 AQLKKSQEAQRELKLLLDMYKGAPKEQRdkvQLMAAEKKARAEVEEHRQQLKKLAEHERKERRKLADEDamKKIRGLEET 1957
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELA---ALKKEEKALLKQLAALERRIAALARRIRALEQELAALE--AELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1958 VASLHKSLTAQKQEVWE--------------EALLS-----EMEVTGQAFEDMQEQNLRLIQQLREK----DDANFKLMS 2014
Cdd:COG4942 92 IAELRAELEAQKEELAEllralyrlgrqpplALLLSpedflDAVRRLQYLKYLAPARREQAEELRADlaelAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 2015 ERIKSNQIHKLLQEEKAmlseqgaTLQAQVEAQNQVVRKLEEKERLLQNSLSTLEK-ELSLRQQAAEMHRRKAVESAQSA 2093
Cdd:COG4942 172 ERAELEALLAELEEERA-------ALEALKAERQKLLARLEKELAELAAELAELQQeAEELEALIARLEAEAAAAAERTP 244
|
..
gi 556079866 2094 AD 2095
Cdd:COG4942 245 AA 246
|
|
| RING-HC_TRIM62_C-IV |
cd16608 |
RING finger, HC subclass, found in tripartite motif-containing protein 62 (TRIM62) and similar ... |
2166-2213 |
1.44e-05 |
|
RING finger, HC subclass, found in tripartite motif-containing protein 62 (TRIM62) and similar proteins; TRIM62, also known as Ductal Epithelium Associated Ring Chromosome 1 (DEAR1), is a cytoplasmic E3 ubiquitin-protein ligase that was identified as a dominant regulator of acinar morphogenesis in the mammary gland. It is implicated in the inflammatory response of immune cells by regulating the Toll-like receptor 4 (TLR4) signaling pathway, leading to increased activity of the activator protein 1 (AP-1) transcription factor in primary macrophages. It is also involved in muscular protein homeostasis, especially during inflammation-induced atrophy, and may play a role in the pathogenesis of ICU-acquired weakness (ICUAW) by activating and maintaining inflammation in myocytes. Moreover, TRIM62 facilitates K27-linked poly-ubiquitination of CARD9 and also regulates CARD9-mediated anti-fungal immunity and intestinal inflammation. It also functions as a chromosome 1p35 tumor suppressor and negatively regulates transforming growth factor beta (TGFbeta)-driven epithelial-mesenchymal transition (EMT) by binding to and promoting the ubiquitination of SMAD3, a major effector of TGFbeta-mediated EMT. TRIM62 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.
Pssm-ID: 438270 [Multi-domain] Cd Length: 52 Bit Score: 44.03 E-value: 1.44e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 556079866 2166 KEQLTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYET-RQRKCPKCNAPF 2213
Cdd:cd16608 4 KDELLCSICLSIYQDPVSLGCEHYFCRQCITEHWSRsEHRDCPECRRTF 52
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
925-1287 |
1.68e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 925 EDAHASLSQSKKKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLNDEIQHQDELINKLNKEKKHLQEASQKTSED 1004
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1005 LQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKRKVEGDLKLAQEAVADLEKNKKEMEQNLQRKEKEMAS 1084
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1085 LAAKLedEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLAREIEELSERLEESGGATSSQIELNKRREA 1164
Cdd:COG4372 169 LEQEL--QALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1165 ELSK-LRRDLEESNLQHEQAMSNLRKKHNDTVAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDHSNKAQANAEKQ 1243
Cdd:COG4372 247 DKEElLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 556079866 1244 VKQLEVQLADAQFKVDEMNRTLNDLDGGKKKLAVENSELQRQLE 1287
Cdd:COG4372 327 KLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
839-1231 |
1.75e-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: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 839 RVEDELKAMEEKLKKTEEALAKEEKLRKELEEhnvKVLQEKNDLFLQLEAERMGAGDVEERLNKALTQKGDLESQLADLN 918
Cdd:COG5185 176 LKKLEIFGLTLGLLKGISELKKAEPSGTVNSI---KESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTS 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 919 DRLSHEEDAHASLSQSK--------KKLEGEISGLKKDIEDMELALQKAEQDKATKDHQirNLNDEIQHQDELINKLNKE 990
Cdd:COG5185 253 DKLEKLVEQNTDLRLEKlgenaessKRLNENANNLIKQFENTKEKIAEYTKSIDIKKAT--ESLEEQLAAAEAEQELEES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 991 KKHLQEASQKTSEDL-QATEDKVNHLNKVKAKLEQ--TLDELEDSLEREKKARGDIEKNKRKVEGD----LKLAQEAVAD 1063
Cdd:COG5185 331 KRETETGIQNLTAEIeQGQESLTENLEAIKEEIENivGEVELSKSSEELDSFKDTIESTKESLDEIpqnqRGYAQEILAT 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1064 LEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKqRADLAREIEELSE 1143
Cdd:COG5185 411 LEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSV-RSKKEDLNEELTQ 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1144 RLEESGGATSSQIELNKRREAELSKLRRDLEESNLQHEQAMS----NLRKKHNDTVAEMSEQIDQLNKHKAKVEKERATM 1219
Cdd:COG5185 490 IESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRargyAHILALENLIPASELIQASNAKTDGQAANLRTAV 569
|
410
....*....|..
gi 556079866 1220 SAEVSDLQSLLD 1231
Cdd:COG5185 570 IDELTQYLSTIE 581
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1248-1358 |
3.03e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.09 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1248 EVQLADAQFKVDEMNRTLNDLDGGKKKLAVENSELQRQLEESESQVAQLNKikaslatQLEEAKRMADEEARERAAIlgk 1327
Cdd:COG2433 398 EREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLER-------ELSEARSEERREIRKDREI--- 467
|
90 100 110
....*....|....*....|....*....|.
gi 556079866 1328 yRNLEHDLDNLRESVEEEQEAKADFQRQLSK 1358
Cdd:COG2433 468 -SRLDREIERLERELEEERERIEELKRKLER 497
|
|
| RING-HC_TRIM39_C-IV |
cd16601 |
RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar ... |
2168-2209 |
3.10e-05 |
|
RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar proteins; TRIM39, also known as RING finger protein 23 (RNF23) or testis-abundant finger protein, is an E3 ubiquitin-protein ligase that plays a role in controlling DNA damage-induced apoptosis through inhibition of the anaphase promoting complex (APC/C), a multiprotein ubiquitin ligase that controls multiple cell cycle regulators, including cyclins, geminin, and others. TRIM39 also functions as a regulator of several key processes in the proliferative cycle. It directly regulates p53 stability. It modulates cell cycle progression and DNA damage responses via stabilizing p21. Moreover, TRIM39 negatively regulates the nuclear factor kappaB (NFkappaB)-mediated signaling pathway through stabilization of Cactin, an inhibitor of NFkappaB- and Toll-like receptor (TLR)-mediated transcription, which is induced by inflammatory stimulants such as tumor necrosis factor alpha. Furthermore, TRIM39 is a MOAP-1-binding protein that can promote apoptosis signaling through stabilization of MOAP-1 via the inhibition of its poly-ubiquitination process. TRIM39 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.
Pssm-ID: 438263 [Multi-domain] Cd Length: 44 Bit Score: 42.86 E-value: 3.10e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 556079866 2168 QLTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYETRQRK--CPKC 2209
Cdd:cd16601 1 EASCSLCKEYLKDPVIIECGHNFCRACITRFWEELDGDfpCPQC 44
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
895-1207 |
3.13e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.52 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 895 DVEERLNKALTQKGDLESQLADLNDRL----SHEEDAHASLSQSKKKLEgEISGLKKDIEDMELALQKAEQDK-----AT 965
Cdd:PRK11281 125 QLESRLAQTLDQLQNAQNDLAEYNSQLvslqTQPERAQAALYANSQRLQ-QIRNLLKGGKVGGKALRPSQRVLlqaeqAL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 966 KDHQIRNLNDEIQHQDELINKLNKEKKHLQEASQKTSEDLQATEDKVNhlNKVKAKLEQTLDELEdslEREKKARgdIEK 1045
Cdd:PRK11281 204 LNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAIN--SKRLTLSEKTVQEAQ---SQDEAAR--IQA 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1046 N---KRKVEGDLKLAQEAVADLEKNKKEMEQNLQRKEKemasLAAKLEDEQAlvakLQKQIKELQ-----ARIEELEEEL 1117
Cdd:PRK11281 277 NplvAQELEINLQLSQRLLKATEKLNTLTQQNLRVKNW----LDRLTQSERN----IKEQISVLKgslllSRILYQQQQA 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1118 EAERQARAKAEKQRADLaREIeelserleesggatssQIELNKRREaELSKLR---RDLEESnlQHEQAMSNLRKKHNDT 1194
Cdd:PRK11281 349 LPSADLIEGLADRIADL-RLE----------------QFEINQQRD-ALFQPDayiDKLEAG--HKSEVTDEVRDALLQL 408
|
330
....*....|...
gi 556079866 1195 VAEMSEQIDQLNK 1207
Cdd:PRK11281 409 LDERRELLDQLNK 421
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
978-1110 |
3.27e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 48.48 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 978 QHQDELINKLNKEKKHLQEasqktseDLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKrkvEGDLKLA 1057
Cdd:smart00787 140 KLLEGLKEGLDENLEGLKE-------DYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCD---PTELDRA 209
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 556079866 1058 QEAVADLEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARI 1110
Cdd:smart00787 210 KEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKL 262
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
839-1218 |
3.38e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 839 RVEDELKAMEEKLKKTEEALAKEEklrkeleehnvkvlQEKNDLFLQLEAERMGAGDVEERLNKAltqkgDLESQLADLN 918
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALE--------------AELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 919 DRLSHEEDAHASLSQskkkLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLNDEIQHQDELINKLNKEKKHLQEAS 998
Cdd:COG4913 675 AELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 999 qktSEDLQATEDKVNHLNKVKAKLEQTLDELEDSLER-EKKARGDIEKNKRKVEGDLKLAQEAVADLEKNKKEMEQ---- 1073
Cdd:COG4913 751 ---LEERFAAALGDAVERELRENLEERIDALRARLNRaEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRleed 827
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1074 NLQRKEKEMASLAAKLEDEQ--ALVAKLQKQIKELQARIeeleeeleaerqARAKAEKQRADLareieelserleesGGA 1151
Cdd:COG4913 828 GLPEYEERFKELLNENSIEFvaDLLSKLRRAIREIKERI------------DPLNDSLKRIPF--------------GPG 881
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556079866 1152 TSSQIELNKRREAELSKLRRDLEESNLQHEQAMSNLRKKHNDTVAEMSEQIDQLNKHKAKVEKERAT 1218
Cdd:COG4913 882 RYLRLEARPRPDPEVREFRQELRAVTSGASLFDEELSEARFAALKRLIERLRSEEEESDRRWRARVL 948
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1433-1993 |
3.82e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1433 LASSLEKRQKSFDKVIAEWKAKVDDLAAELDASQKECRnystEVFKLRAAYEESQEHYESVKRENKNLQDEVKDLMDQLG 1512
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVK----ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1513 EGGRSVHELEKSRKRLE--MEKEELQAALEEAEAALEQEENKVLRAQLELSQVRQEIDRRIQEKE------EEFENTRKN 1584
Cdd:PRK03918 270 ELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEekeerlEELKKKLKE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1585 HQRALDSMQASLEA--EAKGKAEAL-RLKKKLES-DINELEIALDHANKANAEAQKNLKKyqqnVKDLQGALEEEQRARD 1660
Cdd:PRK03918 350 LEKRLEELEERHELyeEAKAKKEELeRLKKRLTGlTPEKLEKELEELEKAKEEIEEEISK----ITARIGELKKEIKELK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1661 EAREQYASAERRCNAMHGEL-EESRQLLASSKNSHLRHIEQMEGEELLMQKKLRTEVIRLEDALVQVRKEYEMLRIeFEQ 1739
Cdd:PRK03918 426 KAIEELKKAKGKCPVCGRELtEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKEL-AEQ 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1740 NLAATEQTGPINRE----MRHLITSLQSHNRQLKGEVSRYKRKLREAAAEAARlkqtLEMSNVAVSSTTVPSSASSTSSD 1815
Cdd:PRK03918 505 LKELEEKLKKYNLEelekKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKK----LAELEKKLDELEEELAELLKELE 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1816 NGSSRGEEGAPVSCPQPGQGGREEGGTPSASSQRREEEAREEEPIPEREKGKSDLDiirDLKAQLKKSQEAQRELKLLLD 1895
Cdd:PRK03918 581 ELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELA---ETEKRLEELRKELEELEKKYS 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1896 M--YKGAPKEQRDKVQLMAAEKKARAEVEEHRQQLKKLAE---HERKERRKLADEdaMKKIRGLEETVASLHKSLTAQKQ 1970
Cdd:PRK03918 658 EeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEklkEELEEREKAKKE--LEKLEKALERVEELREKVKKYKA 735
|
570 580
....*....|....*....|...
gi 556079866 1971 EVWEEALLSEMEVTGQAFEDMQE 1993
Cdd:PRK03918 736 LLKERALSKVGEIASEIFEELTE 758
|
|
| RING-HC_RNF10 |
cd16536 |
RING finger, HC subclass, found in RING finger protein 10 (RNF10) and similar proteins; RNF10 ... |
2170-2217 |
4.37e-05 |
|
RING finger, HC subclass, found in RING finger protein 10 (RNF10) and similar proteins; RNF10 is an E3 ubiquitin-protein ligase that interacts with mesenchyme Homeobox 2 (MEOX2) transcription factor, a regulator of the proliferation, differentiation and migration of vascular smooth muscle cells and cardiomyocytes; it enhances Meox2 activation of the p21 promoter. It also regulates the expression of myelin-associated glycoprotein (MAG) genes and is required for myelin production in Schwann cells of the peripheral nervous system. Moreover, RNF10 regulates retinoic acid-induced neuronal differentiation and the cell cycle exit of P19 embryonic carcinoma cells. RNF10 contains a C3HC4-type RING-HC finger and three putative nuclear localization signals.
Pssm-ID: 438198 [Multi-domain] Cd Length: 54 Bit Score: 43.00 E-value: 4.37e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 556079866 2170 TCPSCKVKRKDAVLIKCFHVFCYDCLKtRY----ETRQRKCPKCNAPFGTND 2217
Cdd:cd16536 2 QCPICLEPPVAPRITRCGHIFCWPCIL-RYlslsEKKWRKCPICFESIHKKD 52
|
|
| RING-HC_HLTF |
cd16509 |
RING finger, HC subclass, found in helicase-like transcription factor (HLTF) and similar ... |
2171-2212 |
4.40e-05 |
|
RING finger, HC subclass, found in helicase-like transcription factor (HLTF) and similar proteins; HLTF, also known as DNA-binding protein/plasminogen activator inhibitor 1 regulator, HIP116, RING finger protein 80, SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3, or sucrose nonfermenting protein 2-like 3, is a yeast RAD5 homolog found in mammals. It has both E3 ubiquitin ligase and DNA helicase activities, and plays a pivotal role in the template-switching pathway of DNA damage tolerance. It is involved in Lys-63-linked poly-ubiquitination of proliferating cell nuclear antigen (PCNA) at Lys-164 and in the regulation of DNA damage tolerance. It shows double-stranded DNA translocase activity with 3'-5' polarity, thereby facilitating regression of the replication fork. HLTF contains an N-terminal HIRAN (HIP116 and RAD5 N-terminal) domain, a SWI/SNF helicase domain that is divided into N- and C-terminal parts by an insertion of a C3HC4-type RING-HC finger involved in the poly-ubiquitination of PCNA.
Pssm-ID: 438172 [Multi-domain] Cd Length: 53 Bit Score: 42.68 E-value: 4.40e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 556079866 2171 CPSCKVKRKDAVLIKCFHVFCYDCLKTRYETRQRKCPKCNAP 2212
Cdd:cd16509 6 CAICLDSLTNPVITPCAHVFCRRCICEVIQREKAKCPMCRAP 47
|
|
| zf-C3HC4_2 |
pfam13923 |
Zinc finger, C3HC4 type (RING finger); |
2171-2209 |
4.59e-05 |
|
Zinc finger, C3HC4 type (RING finger);
Pssm-ID: 404756 [Multi-domain] Cd Length: 40 Bit Score: 42.42 E-value: 4.59e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 556079866 2171 CPSCKVKRKDAVLIK-CFHVFCYDCLKtRYETRQRKCPKC 2209
Cdd:pfam13923 2 CPICMDMLKDPSTTTpCGHVFCQDCIL-RALEASNECPLC 40
|
|
| RING-HC_TRIM25_C-IV |
cd16597 |
RING finger, HC subclass, found in tripartite motif-containing protein TRIM25 and similar ... |
2166-2213 |
4.70e-05 |
|
RING finger, HC subclass, found in tripartite motif-containing protein TRIM25 and similar proteins; TRIM25, also known as estrogen-responsive finger protein (EFP), RING finger protein 147 (RNF147), or RING-type E3 ubiquitin transferase, is an E3 ubiquitin/ISG15 ligase that is induced by estrogen and is therefore particularly abundant in placenta and uterus. TRIM25 regulates various cellular processes through E3 ubiquitin ligase activity, transferring ubiquitin and ISG15 to target proteins. It mediates K63-linked polyubiquitination of retinoic acid inducible gene I (RIG-I) that is crucial for downstream antiviral interferon signaling. It is also required for melanoma differentiation-associated gene 5 (MDA5) and mitochondrial antiviral signaling (MAVS, also known as IPS-1, VISA, Cardiff) mediated activation of nuclear factor-kappaB (NF-kappaB) and interferon production. Upon UV irradiation, TRIM25 interacts with mono-ubiquitinated PCNA and promotes its ISG15 modification (ISGylation), suggesting a crucial role in termination of error-prone translesion DNA synthesis. TRIM25 also functions as a novel regulator of p53 and Mdm2. It enhances p53 and Mdm2 abundance by inhibiting their ubiquitination and degradation in 26S proteasomes. Meanwhile, it inhibits p53's transcriptional activity and dampens the response to DNA damage, and is essential for medaka development and this dependence is rescued by silencing of p53. Moreover, TRIM25 is involved in the host cellular innate immune response against retroviral infection. It interferes with the late stage of feline leukemia virus (FeLV) replication. Furthermore, TRIM25 acts as an oncogene in gastric cancer. Its blockade by RNA interference inhibits migration and invasion of gastric cancer cells through transforming growth factor-beta (TGF-beta) signaling, suggesting it presents a novel target for the detection and treatment of gastric cancer. In addition, TRIM25 acts as an RNA-specific activator for Lin28a/TuT4-mediated uridylation. TRIM25 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.
Pssm-ID: 438259 [Multi-domain] Cd Length: 71 Bit Score: 43.45 E-value: 4.70e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 556079866 2166 KEQLTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYET---RQRKCPKCNAPF 2213
Cdd:cd16597 3 EEELTCSICLELFKDPVTLPCGHNFCGVCIEKTWDSqhgSEYSCPQCRATF 53
|
|
| RING-HC_MmTRIM43-like |
cd23133 |
RING finger, HC subclass, found in Mus musculus tripartite motif-containing protein 43 (TRIM43) ... |
2166-2213 |
5.38e-05 |
|
RING finger, HC subclass, found in Mus musculus tripartite motif-containing protein 43 (TRIM43) and similar propteins; This subfamily includes TRIM43A, TRIM43B and TRIM43C, which are expressed specifically in mouse preimplantation embryos. They contain a typical C3HC4-type RING-HC finger.
Pssm-ID: 438495 [Multi-domain] Cd Length: 57 Bit Score: 42.59 E-value: 5.38e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 556079866 2166 KEQLTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYE--TRQRKCPKCNAPF 2213
Cdd:cd23133 1 EETLTCSICQGIFMNPVYLRCGHKFCEACLLLFQEdiKFPAYCPMCRQPF 50
|
|
| RING-HC_NHL-1-like |
cd16524 |
RING finger, HC subclass, found in Caenorhabditis elegans RING finger protein NHL-1 and ... |
2166-2211 |
6.11e-05 |
|
RING finger, HC subclass, found in Caenorhabditis elegans RING finger protein NHL-1 and similar proteins; NHL-1 functions as an E3 ubiquitin-protein ligase in the presence of both UBC-13 and UBC-1 within the ubiquitin pathway of Caenorhabditis elegans. It acts in chemosensory neurons to promote stress resistance in distal tissues by the transcription factor DAF-16 activation but is dispensable for the activation of heat shock factor 1 (HSF-1). NHL-1 belongs to the TRIM (tripartite motif)-NHL family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as an NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain.
Pssm-ID: 438187 [Multi-domain] Cd Length: 53 Bit Score: 42.41 E-value: 6.11e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 556079866 2166 KEQLTCPSCKVKRKDAVLIKCFHVFCYD-CLK--TRYETRQRKCPKCNA 2211
Cdd:cd16524 3 EQLLTCPICLDRYRRPKLLPCQHTFCLSpCLEglVDYVTRKLKCPECRA 51
|
|
| RING-HC_RNF207 |
cd16558 |
RING finger, HC subclass, found in RING finger protein 207 (RNF207) and similar proteins; ... |
2169-2209 |
6.45e-05 |
|
RING finger, HC subclass, found in RING finger protein 207 (RNF207) and similar proteins; RNF207 is a cardiac-specific E3 ubiquitin-protein ligase that plays an important role in the regulation of cardiac repolarization. It regulates action potential duration, likely via effects on human ether-a-go-go-related gene (HERG) trafficking and localization in a heat shock protein-dependent manner. RNF207 contains a C3HC4-type RING-HC finger, Bbox 1 and Bbox C-terminal (BBC) domain, as well as a C-terminal non-homologous region (CNHR).
Pssm-ID: 438220 [Multi-domain] Cd Length: 43 Bit Score: 41.96 E-value: 6.45e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 556079866 2169 LTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYETRQRKCPKC 2209
Cdd:cd16558 2 LVCYLCHEQYEHPCLLDCYHTFCASCLRGRAADGRLTCPLC 42
|
|
| RING-HC_PEX2 |
cd16526 |
RING finger, HC subclass, found in peroxin-2 (PEX2) and similar proteins; PEX2, also known as ... |
2186-2213 |
7.05e-05 |
|
RING finger, HC subclass, found in peroxin-2 (PEX2) and similar proteins; PEX2, also known as peroxisome biogenesis factor 2, 35 kDa peroxisomal membrane protein, peroxisomal membrane protein 3, peroxisome assembly factor 1 (PAF-1), or RING finger protein 72 (RNF72), is an integral peroxisomal membrane protein with two transmembrane regions and a C3HC4-type RING-HC finger within its cytoplasmically exposed C-terminus. It may be involved in the biogenesis of peroxisomes, as well as in peroxisomal matrix protein import. Mutations in the PEX2 gene are the primary defect in a subset of patients with Zellweger syndrome and related peroxisome biogenesis disorders. Moreover, PEX2 functions as an E3-ubiquitin ligase that mediates the UBC4-dependent polyubiquitination of PEX5, a key player in peroxisomal matrix protein import, to control PEX5 receptor recycling or degradation.
Pssm-ID: 438189 [Multi-domain] Cd Length: 49 Bit Score: 41.99 E-value: 7.05e-05
10 20
....*....|....*....|....*....
gi 556079866 2186 CFHVFCYDCLKTRYETRQR-KCPKCNAPF 2213
Cdd:cd16526 20 CGHVYCYYCIKSNLLADDSfTCPRCGSPV 48
|
|
| RING-HC_TRIM9-like_C-I |
cd16576 |
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM9, TRIM67, and ... |
2167-2210 |
7.11e-05 |
|
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM9, TRIM67, and similar proteins; Tripartite motif-containing proteins TRIM9 and TRIM67 belong to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, consisting of three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. TRIM9 (the human ortholog of rat Spring), also known as RING finger protein 91 (RNF91), is a brain-specific E3 ubiquitin-protein ligase collaborating with an E2 ubiquitin conjugating enzyme UBCH5b. TRIM9 plays an important role in the regulation of neuronal functions and participates in neurodegenerative disorders through its ligase activity. TRIM67, also known as TRIM9-like protein (TNL), is a protein selectively expressed in the cerebellum. It interacts with PRG-1, an important molecule in the control of hippocampal excitability dependent on presynaptic LPA2 receptor signaling, and 80K-H, also known as glucosidase II beta, a protein kinase C substrate.
Pssm-ID: 438238 [Multi-domain] Cd Length: 42 Bit Score: 42.01 E-value: 7.11e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 556079866 2167 EQLTCPSCKVKRKDAVLIKCFHVFCYDCLKtryeTRQRKCPKCN 2210
Cdd:cd16576 2 EELKCPVCGSLFTEPVILPCSHNLCLGCAL----NIQLTCPICH 41
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
872-1471 |
7.12e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.51 E-value: 7.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 872 NVKVLQEKndlFLQLEAERMGAGDVEERLNKALTQKGDLE---SQLADLNDRLSHEEDAHASLSQSKKKLEGEISGL--K 946
Cdd:TIGR01612 460 KLKALEKR---FFEIFEEEWGSYDIKKDIDENSKQDNTVKlilMRMKDFKDIIDFMELYKPDEVPSKNIIGFDIDQNikA 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 947 KDIEDMELALQKAEQDKATKDHQIRNLNDEIQHQDELINKLNKEKKHLQEASQKTsedlqatEDKVNHLNKVKAKLEQTL 1026
Cdd:TIGR01612 537 KLYKEIEAGLKESYELAKNWKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEI-------DDEIIYINKLKLELKEKI 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1027 DELEDSLEREKKA---RGDIEKNKRKVEGDLKLAQEAVADLEKNKKEM------------EQNLQRKEKEMASLA----- 1086
Cdd:TIGR01612 610 KNISDKNEYIKKAidlKKIIENNNAYIDELAKISPYQVPEHLKNKDKIystikselskiyEDDIDALYNELSSIVkenai 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1087 ------AKLEDEQALVAKLQKQIKELQARIEELEEeleaerqarAKAEKQRADLareieelserleesggaTSSQIELNK 1160
Cdd:TIGR01612 690 dntedkAKLDDLKSKIDKEYDKIQNMETATVELHL---------SNIENKKNEL-----------------LDIIVEIKK 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1161 RREAELSK-LRRDLEESNLQHEQAMSNLrkkhNDtvaeMSEQIDQLNKHKAKVEKERATMSAEVSdlqslLDhsNKAQAN 1239
Cdd:TIGR01612 744 HIHGEINKdLNKILEDFKNKEKELSNKI----ND----YAKEKDELNKYKSKISEIKNHYNDQIN-----ID--NIKDED 808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1240 AEKQVKQLEVQLADAQFKVDEMNRTLNDLDGGK--------KKLAVENSELQRQLEESESQVAQLNKIKASLatqleeak 1311
Cdd:TIGR01612 809 AKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKddflnkvdKFINFENNCKEKIDSEHEQFAELTNKIKAEI-------- 880
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1312 rmADEEareraaiLGKYRNLEHDLDNLRESVEEEQEAKADFQRQLSKANAEAQLWRSKYESeglarLEELEEAKRKLHGK 1391
Cdd:TIGR01612 881 --SDDK-------LNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYIKICENTKES-----IEKFHNKQNILKEI 946
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1392 LQEAEEAMEQLNAkcsgLEKT-KSHLQGELEDMSIEVDKA--NALASSLEKRQKSFDKVIAEWKA-----KVDDLAAELD 1463
Cdd:TIGR01612 947 LNKNIDTIKESNL----IEKSyKDKFDNTLIDKINELDKAfkDASLNDYEAKNNELIKYFNDLKAnlgknKENMLYHQFD 1022
|
....*...
gi 556079866 1464 ASQKECRN 1471
Cdd:TIGR01612 1023 EKEKATND 1030
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1173-1705 |
7.45e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.18 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1173 LEESNLQHEQAMSNLRKKhndtvaeMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDHSNKA----QANAEKQVKQLE 1248
Cdd:pfam05483 65 LKDSDFENSEGLSRLYSK-------LYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAiqelQFENEKVSLKLE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1249 VQLADAQFKVDEMNRT---LNDLDGGKKKLAVENSELQRQLEESESQVAQLNKIKASLATQLEEAkRMADEEAReraaiL 1325
Cdd:pfam05483 138 EEIQENKDLIKENNATrhlCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEEL-RVQAENAR-----L 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1326 GKYRNLEHDLDNLRESVEEEQEAKADFQRQLSKANAEAQLWRSKYESEGLArLEELEEAKRKLHGKLQEAEEAMEQLNAK 1405
Cdd:pfam05483 212 EMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFL-LEESRDKANQLEEKTKLQDENLKELIEK 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1406 csglektKSHLQGELEDMSIEVDKANALASSLEKRQKSFDKVIAEWkakVDDLAAELDASQKECRNYSTEVFKLRAAYEE 1485
Cdd:pfam05483 291 -------KDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQL---TEEKEAQMEELNKAKAAHSFVVTEFEATTCS 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1486 SQEHYESVKRENKNLQDEVKDLMDQLGEGGRSVHELEKSRKRLEMEKEELQAALEEAEAALEQEEnKVLRAQLELSQVRQ 1565
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKK-QFEKIAEELKGKEQ 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1566 EIDRRIQEKEEEFEN----------TRKNHQRALDSMQASLEAEAKGKAE-------ALRLKKKLESDINELEIALdhaN 1628
Cdd:pfam05483 440 ELIFLLQAREKEIHDleiqltaiktSEEHYLKEVEDLKTELEKEKLKNIEltahcdkLLLENKELTQEASDMTLEL---K 516
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556079866 1629 KANAEAQKNLKKYQQNVKDLQGALEEEQRARDEAREQYASAERRCNAMHGELEESRQLLASSKNSHLRHIEQMEGEE 1705
Cdd:pfam05483 517 KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILE 593
|
|
| RING-HC_TRIM35_C-IV |
cd16599 |
RING finger, HC subclass, found in tripartite motif-containing protein 35 (TRIM35) and similar ... |
2165-2211 |
7.59e-05 |
|
RING finger, HC subclass, found in tripartite motif-containing protein 35 (TRIM35) and similar proteins; TRIM35, also known as hemopoietic lineage switch protein 5 (HLS5), is a putative hepatocellular carcinoma (HCC) suppressor that inhibits phosphorylation of pyruvate kinase isoform M2 (PKM2), which is involved in aerobic glycolysis of cancer cells and further suppresses the Warburg effect and tumorigenicity in HCC. It also negatively regulates Toll-like receptor 7 (TLR7)- and TLR9-mediated type I interferon production by suppressing the stability of interferon regulatory factor 7 (IRF7). Moreover, TRIM35 regulates erythroid differentiation by modulating globin transcription factor 1 (GATA-1) activity. TRIM35 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.
Pssm-ID: 438261 [Multi-domain] Cd Length: 66 Bit Score: 42.45 E-value: 7.59e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 556079866 2165 YKEQLTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYETRQRK-CPKCNA 2211
Cdd:cd16599 1 FKEELLCPICYEPFREAVTLRCGHNFCKGCVSRSWERQPRApCPVCKE 48
|
|
| RING-HC_PCGF |
cd16525 |
RING finger, HC subclass, found in Polycomb Group RING finger homologs (PCGF1, 2, 3, 4, 5 and ... |
2169-2210 |
8.41e-05 |
|
RING finger, HC subclass, found in Polycomb Group RING finger homologs (PCGF1, 2, 3, 4, 5 and 6), and similar proteins; This subfamily includes six Polycomb Group (PcG) RING finger homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR) that use epigenetic mechanisms to maintain or repress expression of their target genes. They were first discovered in fruit flies and are well known for silencing Hox genes through modulation of chromatin structure during embryonic development. PCGF homologs play important roles in cell proliferation, differentiation, and tumorigenesis. They all have been found to associate with ring finger protein 2 (RNF2). The RNF2-PCGF heterodimer is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. Moreover, PCGF homologs are critical components in the assembly of distinct Polycomb Repression Complex 1 (PRC1) related complexes which is involved in the maintenance of gene repression and which target different genes through distinct mechanisms. The Drosophila PRC1 core complex is formed by the Polycomb (Pc), Polyhomeotic (Ph), Posterior sex combs (Psc), and Sex combs extra (Sce, also known as Ring) subunits. In mammals, the composition of PRC1 is much more diverse and varies depending on the cellular context. All PRC1 complexes contain homologs of the Drosophila Ring protein. Ring1A/RNF1 and Ring1B/RNF2 are E3 ubiquitin ligases that mark lysine 119 of histone H2A with a single ubiquitin group (H2AK119ub). Mammalian homologs of the Drosophila Psc protein, such as PCGF2/Mel-18 or PCGF4/BMI1, regulate PRC1 enzymatic activity. PRC1 complexes can be divided into at least two classes according to the presence or absence of CBX proteins, which are homologs of Drosophila Pc. Canonical PRC1 complexes contain CBX proteins that recognize and bind H3K27me3, the mark deposited by PRC2. Therefore, canonical PRC1 complexes and PRC2 can act together to repress gene transcription and maintain this repression through cell division. Non-canonical PRC1 complexes, containing RYBP (together with additional proteins, such as L3mbtl2 or Kdm2b) rather than the CBX proteins have recently been described in mammals. PCGF homologs contain a C3HC4-type RING-HC finger.
Pssm-ID: 438188 [Multi-domain] Cd Length: 42 Bit Score: 41.83 E-value: 8.41e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 556079866 2169 LTCPSCKVKRKDAVLIK-CFHVFCYDCLkTRYETRQRKCPKCN 2210
Cdd:cd16525 1 LTCSLCKGYLIDATTITeCLHSFCKSCI-VRHLETSKNCPVCD 42
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
828-1443 |
8.84e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.97 E-value: 8.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 828 YSKVKPLLSAVRVE-DELKAMEEKLKKTEEALAKEEKLRKELEEHNVKVLQEKNDLFLQLEA---ERMGAGDVEERLNKA 903
Cdd:PRK01156 168 YDKLKDVIDMLRAEiSNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNamdDYNNLKSALNELSSL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 904 LTQKGDLESQLADLNDRLSHEEDAHASLSQSKKKLegeisglKKDIEDMELALQKAEQDKATKDHQIRNLNDEIQHQDEL 983
Cdd:PRK01156 248 EDMKNRYESEIKTAESDLSMELEKNNYYKELEERH-------MKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 984 INKLnkekkhlqEASQKTSEDLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKRKVEGDLKLAQEAVAD 1063
Cdd:PRK01156 321 INKY--------HAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAF 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1064 LEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELqarieeleeeleaerqaRAKAEKQRADLAREIEELSE 1143
Cdd:PRK01156 393 ISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRAL-----------------RENLDELSRNMEMLNGQSVC 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1144 RLEESGGATSSQIELNKRREAELSKLRRDLEEsnLQHEQAMSNLRKKHNDTVAEM--SEQIDQLNKHKAKVEKERATMSA 1221
Cdd:PRK01156 456 PVCGTTLGEEKSNHIINHYNEKKSRLEEKIRE--IEIEVKDIDEKIVDLKKRKEYleSEEINKSINEYNKIESARADLED 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1222 EVSDLQSLLDHSNKAQAnAEKQVKQLEVQLADAQfkvdemNRTLNDLDGGKKKLAVENseLQRQLEESESQVAQLNKIKA 1301
Cdd:PRK01156 534 IKIKINELKDKHDKYEE-IKNRYKSLKLEDLDSK------RTSWLNALAVISLIDIET--NRSRSNEIKKQLNDLESRLQ 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1302 SLATQLEEAKRMADEEARERAAILGKYRNLEHDLDNLRESVEEEQEAKADFQRQLSKANAeaqlwRSKYESEGLARLEEL 1381
Cdd:PRK01156 605 EIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDS-----IIPDLKEITSRINDI 679
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556079866 1382 EEAKRKLHGKLQEAeeameqlNAKCSGLEKTKSHLQGELEDMSIEVDKANALASSLEKRQKS 1443
Cdd:PRK01156 680 EDNLKKSRKALDDA-------KANRARLESTIEILRTRINELSDRINDINETLESMKKIKKA 734
|
|
| RING-HC_RNF185 |
cd16744 |
RING finger, HC subclass, found in RING finger protein 185 (RNF185) and similar proteins; ... |
2171-2222 |
9.06e-05 |
|
RING finger, HC subclass, found in RING finger protein 185 (RNF185) and similar proteins; RNF185 is an E3 ubiquitin-protein ligase of endoplasmic reticulum-associated degradation (ERAD) that targets cystic fibrosis transmembrane conductance regulator (CFTR). It controls the degradation of CFTR and CFTR F508del allele in a RING- and proteasome-dependent manner, but does not control that of other classical ERAD model substrates. It also negatively regulates osteogenic differentiation by targeting dishevelled2 (Dvl2), a key mediator of the Wnt signaling pathway, for degradation. Moreover, RNF185 regulates selective mitochondrial autophagy through interaction with the Bcl-2 family protein BNIP1. It also plays an important role in cell adhesion and migration through the modulation of cell migration by ubiquitinating paxillin. RNF185 contains a C3HC4-type RING-HC finger.
Pssm-ID: 438402 [Multi-domain] Cd Length: 57 Bit Score: 42.22 E-value: 9.06e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 556079866 2171 CPSCKVKRKDAVLIKCFHVFCYDCLKTRYETR--QRKCPKCNAPFGTNDYHRLY 2222
Cdd:cd16744 3 CNICLDTAKDAVVSLCGHLFCWPCLHQWLETRpnRQVCPVCKAGISRDKVIPLY 56
|
|
| RING-HC_CHR27-like |
cd23142 |
RING finger, HC subclass, found in Arabidopsis thaliana protein CHROMATIN REMODELING 27 (CHR27) ... |
2171-2217 |
9.70e-05 |
|
RING finger, HC subclass, found in Arabidopsis thaliana protein CHROMATIN REMODELING 27 (CHR27) and similar proteins; CHR27, also called protein SNF2-RING-HELICASE-LIKE 1, is a probable helicase-like transcription factor involved in transcriptional gene silencing. It associates with SUVR2 and contributes to transcriptional gene silencing at RNA-directed DNA methylation (RdDM) target loci but also at RdDM-independent target loci. It may be involved in nucleosome positioning to form ordered nucleosome arrays on chromatin. It associates with SUVR2 and functions redundantly with FRG2. It is required for the efficient methylation of a broad range of RdDM target loci. CHR27 contains a typical C3HC4-type RING-HC finger.
Pssm-ID: 438504 [Multi-domain] Cd Length: 55 Bit Score: 42.17 E-value: 9.70e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 556079866 2171 CPSCKVKRKDAVLIKCFHVFCYDCLKTRYETRQR-----KCPKCNAPFGTND 2217
Cdd:cd23142 3 CPICNDPPEDAVVTLCGHVFCCECVFQYLSSDRTcrqfnHCPLCRQKLYLDD 54
|
|
| RING-HC_RNFT2 |
cd16742 |
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 2 ... |
2171-2209 |
1.10e-04 |
|
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 2(RNFT2); RNFT2, also known as transmembrane protein 118 (TMEM118), is a multi-pass membrane protein containing a C3HC4-type RING-HC finger. Its biological role remains unclear.
Pssm-ID: 438400 [Multi-domain] Cd Length: 67 Bit Score: 42.17 E-value: 1.10e-04
10 20 30
....*....|....*....|....*....|....*....
gi 556079866 2171 CPSCKVKRKDAVLIKCFHVFCYDCLKTRYEtRQRKCPKC 2209
Cdd:cd16742 16 CAICQAEFREPLILICQHVFCEECLCLWFD-RERTCPLC 53
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
981-1652 |
1.22e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.59 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 981 DELINKLNKEKKHLQEASQKTsEDLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKargDIEKNKRKVEGDlklaQEA 1060
Cdd:PRK01156 141 DSLISGDPAQRKKILDEILEI-NSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNL---ELENIKKQIADD----EKS 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1061 VADLEKNKKEMEQNLQRKEKEMASLAAKLEDEQAL---VAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLARE 1137
Cdd:PRK01156 213 HSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLedmKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYK 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1138 IEELSERLEESGGATSSQIELNKRREAELSKLRRDLEEsnlqheqaMSNLRKKHNDTVaEMSEQIDQLNKhkakvekera 1217
Cdd:PRK01156 293 NRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKK--------LSVLQKDYNDYI-KKKSRYDDLNN---------- 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1218 tmsaEVSDLQSLLDHSNKAQANAEKQVKQLEVQLADAQFKVDEMNRTLNDLDGGKKKLAVENSELQRQLEESESQVAQLN 1297
Cdd:PRK01156 354 ----QILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLN 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1298 KIKASLATQLEEAKR-MADEEARERAAILG-----------------KYRNLEHDLDNLRESVEEEQEAKADFQRQLSKA 1359
Cdd:PRK01156 430 QRIRALRENLDELSRnMEMLNGQSVCPVCGttlgeeksnhiinhyneKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYL 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1360 NAEaQLWRSKYESEGLARLE-ELEEAKRKLhGKLQEAEEAMEQLNakcsglEKTKSHLQGELEDMSIEVDKANALASSL- 1437
Cdd:PRK01156 510 ESE-EINKSINEYNKIESARaDLEDIKIKI-NELKDKHDKYEEIK------NRYKSLKLEDLDSKRTSWLNALAVISLId 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1438 -EKRQKSFDKViaewKAKVDDLAAELDASQKECRNYSTEVFKLRAAYEESQEHYESvkreNKNLQDEVKDLMDQLGEggr 1516
Cdd:PRK01156 582 iETNRSRSNEI----KKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNN----KYNEIQENKILIEKLRG--- 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1517 svhELEKSRKRLEMEKeelqaaleeaeaaleqeenkvlraqlELSQVRQEIDRRIQEKEEEFENTRKnhqrALDSMQASL 1596
Cdd:PRK01156 651 ---KIDNYKKQIAEID--------------------------SIIPDLKEITSRINDIEDNLKKSRK----ALDDAKANR 697
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 556079866 1597 eAEAKGKAEALRlkkkleSDINELEIALDHANKaNAEAQKNLKKYQQNVKDLQGAL 1652
Cdd:PRK01156 698 -ARLESTIEILR------TRINELSDRINDINE-TLESMKKIKKAIGDLKRLREAF 745
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1029-1574 |
1.34e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1029 LEDSLEREKKARGDieKNKRKVEGDLKLAQEAVADLEKNKKEMEQnLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQA 1108
Cdd:COG4717 47 LLERLEKEADELFK--PQGRKPELNLKELKELEEELKEAEEKEEE-YAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1109 RIEELEEeleaeRQARAKAEKQRADLAReieelserleesggatssQIELNKRREAELSKLRRDLEESNLQHEQAMSNLR 1188
Cdd:COG4717 124 LLQLLPL-----YQELEALEAELAELPE------------------RLEELEERLEELRELEEELEELEAELAELQEELE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1189 KKHNDTVAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDhsnkaqaNAEKQVKQLEVQLADAQfkvdemnrtlndl 1268
Cdd:COG4717 181 ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE-------ELEEELEQLENELEAAA------------- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1269 dggkkklavenseLQRQLEESESQVAQLNKIkASLATQLEEAKRMADEEARERAAILGKYRNLEHDLDNLRESVEEEQEA 1348
Cdd:COG4717 241 -------------LEERLKEARLLLLIAAAL-LALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1349 KADFQRQLSKANAEAQLWRSKYESEGLARLEELEEAKR---KLHGKLQEAEEAMEQLnaKCSGLEKTKSHLQGEledmsI 1425
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDrieELQELLREAEELEEEL--QLEELEQEIAALLAE-----A 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1426 EVDKANALASSLEKRQKsfdkvIAEWKAKVDDLAAELDASQKECRNYSTEvfklrAAYEESQEHYESVKRENKNLQDEVK 1505
Cdd:COG4717 380 GVEDEEELRAALEQAEE-----YQELKEELEELEEQLEELLGELEELLEA-----LDEEELEEELEELEEELEELEEELE 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556079866 1506 DLMDQLGEGGRSVHELEKSRKRLEMEkeelqAALEEAEAALEQEENKVLRAQLELSQVRQEIDRRIQEK 1574
Cdd:COG4717 450 ELREELAELEAELEQLEEDGELAELL-----QELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
980-1771 |
1.46e-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: 47.25 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 980 QDELINkLNKEKKHLQEASQKTSEDLQATEDkvnHLNKVKAKLEQTldeledslerEKKAR--GDIEKnkrkVEGDLKLA 1057
Cdd:COG3096 305 QYRLVE-MARELEELSARESDLEQDYQAASD---HLNLVQTALRQQ----------EKIERyqEDLEE----LTERLEEQ 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1058 QEAVADLEKNKKEMEQNLQRKEKEMASLAAKLED-EQALVAKLQKQIKELQARieeleeeleaERQARAKAEKQRADLAr 1136
Cdd:COG3096 367 EEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADyQQALDVQQTRAIQYQQAV----------QALEKARALCGLPDLT- 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1137 eieelserleeSGGATSSQIELnKRREAELSKLRRDLE-------ESNLQHEQAMSNLRKKHNDTVAEMS-----EQIDQ 1204
Cdd:COG3096 436 -----------PENAEDYLAAF-RAKEQQATEEVLELEqklsvadAARRQFEKAYELVCKIAGEVERSQAwqtarELLRR 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1205 LNKHKAKVEKErATMSAEVSDLQSLLDhsnkAQANAEKQVKQLEVQLadaqfkvdemNRTLNDLDggkkKLAVENSELQR 1284
Cdd:COG3096 504 YRSQQALAQRL-QQLRAQLAELEQRLR----QQQNAERLLEEFCQRI----------GQQLDAAE----ELEELLAELEA 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1285 QLEESESQVAQLNKIKASLATQLEEAKRMADEEARERAAILGKYRNLEHDLDNLRESVEEEQEAKADFQRQLSKanaEAQ 1364
Cdd:COG3096 565 QLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLER---ERE 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1365 LWRSKyeSEGLARLEELEEAKRKLHgklQEAEEAMEQLNAKCSglektksHLQGEL-----EDMSIE------------- 1426
Cdd:COG3096 642 ATVER--DELAARKQALESQIERLS---QPGGAEDPRLLALAE-------RLGGVLlseiyDDVTLEdapyfsalygpar 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1427 ----VDKANALASSLEKRQ-------------KSFDKVIAEwkAKVDDLAAELDASQKECRnYS--TEVFKL-RAAYEEs 1486
Cdd:COG3096 710 haivVPDLSAVKEQLAGLEdcpedlyliegdpDSFDDSVFD--AEELEDAVVVKLSDRQWR-YSrfPEVPLFgRAAREK- 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1487 qeHYESVKREnknlQDEVKDLMDQLGEGGRSVHELEKSRKRL-------------EMEKEELQAALEEAEAALEQEENKV 1553
Cdd:COG3096 786 --RLEELRAE----RDELAEQYAKASFDVQKLQRLHQAFSQFvgghlavafapdpEAELAALRQRRSELERELAQHRAQE 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1554 LRAQLELSQVRQEID------------------RRIQEKEEEFENTR------KNHQRAL-------DSMQASLEAEAKG 1602
Cdd:COG3096 860 QQLRQQLDQLKEQLQllnkllpqanlladetlaDRLEELREELDAAQeaqafiQQHGKALaqleplvAVLQSDPEQFEQL 939
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1603 KAEALRLKKKLES------DINELEIALDHANKANAEAQknLKKYQQNVKDLQGALEEEQRARDEAREQYASAERRCNam 1676
Cdd:COG3096 940 QADYLQAKEQQRRlkqqifALSEVVQRRPHFSYEDAVGL--LGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYS-- 1015
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1677 hgeleESRQLLASSKNSH------LRHIEQmEGEEL------LMQKKLRTEVIRLEDALVQVRKEyemlRIEFEQNLAAT 1744
Cdd:COG3096 1016 -----QYNQVLASLKSSRdakqqtLQELEQ-ELEELgvqadaEAEERARIRRDELHEELSQNRSR----RSQLEKQLTRC 1085
|
890 900
....*....|....*....|....*..
gi 556079866 1745 EqtgpinREMRHLITSLQSHNRQLKGE 1771
Cdd:COG3096 1086 E------AEMDSLQKRLRKAERDYKQE 1106
|
|
| RING-HC_EHV1-like |
cd23130 |
RING finger, HC subclass, found in Equid alphaherpesvirus 1 (Equine herpesvirus 1/EHV-1) ... |
2171-2215 |
1.48e-04 |
|
RING finger, HC subclass, found in Equid alphaherpesvirus 1 (Equine herpesvirus 1/EHV-1) regulatory protein and similar proteins; EHV-1 regulatory protein belongs to the Vmw110 (IPC0) protein family. It contains a typical C3HC4-type RING-HC finger and binds zinc stably.
Pssm-ID: 438492 [Multi-domain] Cd Length: 51 Bit Score: 41.18 E-value: 1.48e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 556079866 2171 CPSCKVKRKD-AVLIKCFHVFCYDCLKTRYETRQrKCPKCNAPFGT 2215
Cdd:cd23130 3 CPICLDDPEDeAITLPCLHQFCYTCILRWLQTSP-TCPLCKTPVTS 47
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
930-1110 |
1.51e-04 |
|
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: 47.15 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 930 SLSQSKKKLEGEISGLKKDIEDMELALQKA----EQDKATKDHQIRNLNDEIQHQDELINKLNKEKKHlqeasQKTSEDL 1005
Cdd:pfam09726 427 SLTSLERSLKSELGQLRQENDLLQTKLHNAvsakQKDKQTVQQLEKRLKAEQEARASAEKQLAEEKKR-----KKEEEAT 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1006 QAtedkvnhlnKVKAKLEQTLDELEDSLereKKARGDIEKNKRKVEGDLKLAQEAVADLEKNKKEM---EQNLQRKEKEM 1082
Cdd:pfam09726 502 AA---------RAVALAAASRGECTESL---KQRKRELESEIKKLTHDIKLKEEQIRELEIKVQELrkyKESEKDTEVLM 569
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 556079866 1083 ASLAA-------------------------------KLEDEQALVAKLQKQIKELQARI 1110
Cdd:pfam09726 570 SALSAmqdknqhlenslsaetrikldlfsalgdakrQLEIAQGQIYQKDQEIKDLKQKI 628
|
|
| RING-HC_TRIM38_C-IV |
cd16600 |
RING finger, HC subclass, found in tripartite motif-containing protein 38 (TRIM38) and similar ... |
2166-2213 |
1.52e-04 |
|
RING finger, HC subclass, found in tripartite motif-containing protein 38 (TRIM38) and similar proteins; TRIM38, also known as RING finger protein 15 (RNF15) or zinc finger protein RoRet, is an E3 ubiquitin-protein ligase that promotes K63- and K48-linked ubiquitination of cellular proteins and also catalyzes self-ubiquitination. It negatively regulates Tumor necrosis factor alpha (TNF-alpha)- and interleukin-1beta-triggered Nuclear factor-kappaB (NF-kappaB) activation by mediating lysosomal-dependent degradation of transforming growth factor beta (TGFbeta)-activated kinase 1 (TAK1)-binding protein (TAB)2/3, two critical components of the TAK1 kinase complex. It also inhibits TLR3/4-mediated activation of NF-kappaB and interferon regulatory factor 3 (IRF3) by mediating ubiquitin-proteasomal degradation of TNF receptor-associated factor 6 (Traf6) and NAK-associated protein 1 (Nap1), respectively. Moreover, TRIM38 negatively regulates TLR3-mediated interferon beta (IFN-beta) signaling by targeting ubiquitin-proteasomal degradation of TIR domain-containing adaptor inducing IFN-beta (TRIF). It functions as a valid target for autoantibodies in primary Sjogren's Syndrome. TRIM38 belongs the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.
Pssm-ID: 438262 [Multi-domain] Cd Length: 58 Bit Score: 41.68 E-value: 1.52e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 556079866 2166 KEQLTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYE--------TRQRKCPKCNAPF 2213
Cdd:cd16600 3 REEATCSICLQLMTEPVSINCGHSYCKRCIVSFLEnqsqlepgLETFSCPQCRAPF 58
|
|
| RING_Ubox |
cd00162 |
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ... |
2171-2209 |
1.87e-04 |
|
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type RING fingers are closely related to RING-HC fingers. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are more closely related to RING-H2 fingers. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerate RING fingers of the Siz/PIAS RING (SP-RING) family proteins and sporulation protein RMD5, are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues. They bind only one Zn2+ ion. On the other hand, the RING fingers of the human APC11 and RBX1 proteins can bind a third Zn atom since they harbor four additional Zn ligands. U-box is a modified form of the RING finger domain that lacks metal chelating Cys and His residues. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms. RING finger/U-box-containing proteins are a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enable efficient transfer of ubiquitin from E2 to the substrates.
Pssm-ID: 438111 [Multi-domain] Cd Length: 42 Bit Score: 40.91 E-value: 1.87e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 556079866 2171 CPSCKVKRKDA---VLIKCFHVFCYDCLKTRYETRQRKCPKC 2209
Cdd:cd00162 1 CPICREEMNDRrpvVLLSCGHTFSRSAIARWLEGSKQKCPFC 42
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
874-1224 |
2.05e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 874 KVLQEKNDLFLQLEAERMGAGDVEERLNKALTQKGDLESQLADLNDRLSHEEDAHASLSQSKKKLEGEISGLKKDIEDME 953
Cdd:COG4372 7 KVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 954 LALQKAEQDKATKDHQIRNLNDEIQHQDELINKLNKEKKHLQEASQKTSEDLQATEDKVNHLNKVKAKLEQTLDELEDSL 1033
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1034 EREKKARGDIEKNKRKVEGDLKLAQ---EAVADLEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARI 1110
Cdd:COG4372 167 AALEQELQALSEAEAEQALDELLKEanrNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1111 EELEEELEAERQARAKAEKQRADLAREIEELSERLEESGGATSSQIELNKRREAELSKLRRDLEESNLQHEQAMSNLRKK 1190
Cdd:COG4372 247 DKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
|
330 340 350
....*....|....*....|....*....|....
gi 556079866 1191 HNDTVAEMSEQIDQLNKHKAKVEKERATMSAEVS 1224
Cdd:COG4372 327 KLELALAILLAELADLLQLLLVGLLDNDVLELLS 360
|
|
| RING-HC_XBAT35-like |
cd23129 |
RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 5 (XBAT35) and ... |
2170-2212 |
2.11e-04 |
|
RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 5 (XBAT35) and similar proteins; XBAT35, also known as ankyrin repeat domain and RING finger-containing protein XBAT35, or RING-type E3 ubiquitin transferase XBAT35, has no E3 ubiquitin-protein ligase activity observed when associated with the E2 enzyme UBC8 in vitro. It contains a typical C3HC4-type RING-HC finger.
Pssm-ID: 438491 [Multi-domain] Cd Length: 54 Bit Score: 41.09 E-value: 2.11e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 556079866 2170 TCPSCKVKRKDAVLIKCFHV-FCYDCLKTRYETrQRKCPKCNAP 2212
Cdd:cd23129 4 ECVVCMDAPRDAVCVPCGHVaGCMSCLKALMQS-SPLCPICRAP 46
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
976-1384 |
2.20e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 46.29 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 976 EIQHQDELINKLNKEKKHLQEASQktsedlQATEDKVNHLNKVKAKLEQTLDELEDSL-EREKKARGDIEKNKRKVEgdl 1054
Cdd:pfam09731 39 YIPYGEEVVLYALGEDPPLAPKPK------TFRPLQPSVVSAVTGESKEPKEEKKQVKiPRQSGVSSEVAEEEKEAT--- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1055 KLAQEAVADLEKNKKEMEQNLQRKEKEMASLAAKLEDeQALVAKLQKQI-------KELQARIEELEEELEAERQARAKA 1127
Cdd:pfam09731 110 KDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATA-VAKEAKDDAIQavkahtdSLKEASDTAEISREKATDSALQKA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1128 EKQRADLAREIEELSERLEesgGATSSQIELNKRREAELSKlRRDLEESNLQHEQAMSNLRKKHNDTVAEMSEQIDQlnk 1207
Cdd:pfam09731 189 EALAEKLKEVINLAKQSEE---EAAPPLLDAAPETPPKLPE-HLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQ--- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1208 hkakvekERATMSAEVSDLQSLLDHSNKAQANAekqvkqlevQLADAQFKVDEMNRTLNDLDggkkklAVENSELQRQLE 1287
Cdd:pfam09731 262 -------ELVSIFPDIIPVLKEDNLLSNDDLNS---------LIAHAHREIDQLSKKLAELK------KREEKHIERALE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1288 EsesQVAQLNKIKASLATQLEEA-----KRMADEEARERAAILGKYRN-LEHDLDNLRESVEE---------EQEAKADF 1352
Cdd:pfam09731 320 K---QKEELDKLAEELSARLEEVraadeAQLRLEFEREREEIRESYEEkLRTELERQAEAHEEhlkdvlveqEIELQREF 396
|
410 420 430
....*....|....*....|....*....|..
gi 556079866 1353 QRQLSKANAEAQLWRSKYESEGLARLEELEEA 1384
Cdd:pfam09731 397 LQDIKEKVEEERAGRLLKLNELLANLKGLEKA 428
|
|
| RING-HC_PML_C-V |
cd16579 |
RING finger, HC subclass, found in promyelocytic leukemia protein (PML) and similar proteins; ... |
2166-2212 |
2.31e-04 |
|
RING finger, HC subclass, found in promyelocytic leukemia protein (PML) and similar proteins; Protein PML, also known as RING finger protein 71 (RNF71) or tripartite motif-containing protein 19 (TRIM19), is predominantly a nuclear protein with a broad intrinsic antiviral activity. It is the eponymous component of PML nuclear bodies (PML NBs) and has been implicated in a wide variety of cell processes, including DNA damage signaling, apoptosis, and transcription. PML interferes with the replication of many unrelated viruses, including human immunodeficiency virus 1 (HIV-1), human foamy virus (HFV), poliovirus, influenza virus, rabies virus, EMCV, adeno-associated virus (AAV), and vesicular stomatitis virus (VSV). It also selectively interacts with misfolded proteins through distinct substrate recognition sites and conjugates these proteins with the small ubiquitin-like modifiers (SUMOs) through its SUMO ligase activity. PML belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain.
Pssm-ID: 438241 [Multi-domain] Cd Length: 52 Bit Score: 41.00 E-value: 2.31e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 556079866 2166 KEQLTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYETRQR----KCPKCNAP 2212
Cdd:cd16579 2 FKFLRCPGCKAEYKCPKLLPCLHTVCSGCLEALAEQASEttefQCPICKAS 52
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1186-1398 |
2.78e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1186 NLRKKHNDTVAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDHSNKAQANAEKQVKQLEVQLADAQFKVDEMNRTL 1265
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1266 NDLDGGKKKLAVENSELQRQLEESESQVAQLNKIKASLATQLEEAKRMADEEARERAAILGKYRNLEHDLDNLRESVE-- 1343
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQal 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 556079866 1344 EEQEAKADFQRQLSKANAEAQLWRSKYESEGLARLEELEEAKRKLHGKLQEAEEA 1398
Cdd:COG4372 177 SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL 231
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1090-1398 |
2.78e-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: 46.48 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1090 EDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLAREieelserleesggatssQIELNKRREAELSKL 1169
Cdd:COG3096 832 PDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKL-----------------LPQANLLADETLADR 894
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1170 RRDLEESNLQHEQAMSNLRkKHNDTVAEMSEQIDQLNKHKAKVEkeraTMSAEVSDLQSLLDHSnKAQANAEKQVKQLEV 1249
Cdd:COG3096 895 LEELREELDAAQEAQAFIQ-QHGKALAQLEPLVAVLQSDPEQFE----QLQADYLQAKEQQRRL-KQQIFALSEVVQRRP 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1250 QLA--DAQFKVDEmNRTLNDldggKKKLAVENSELQR-----QLEESESQVAQLNKIKASLATQLEEAKRMADEEARERA 1322
Cdd:COG3096 969 HFSyeDAVGLLGE-NSDLNE----KLRARLEQAEEARreareQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELE 1043
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1323 AIlgkyrnlehdldNLRESVEEEQEAKADFQR---QLS-----KANAEAQLWRSKYESEGLARleELEEAKRKLHGKLQE 1394
Cdd:COG3096 1044 EL------------GVQADAEAEERARIRRDElheELSqnrsrRSQLEKQLTRCEAEMDSLQK--RLRKAERDYKQEREQ 1109
|
....
gi 556079866 1395 AEEA 1398
Cdd:COG3096 1110 VVQA 1113
|
|
| mRING-C3HGC3_RFWD3 |
cd16450 |
Modified RING finger, C3HGC3-type, found in RING finger and WD repeat domain-containing ... |
2184-2222 |
2.80e-04 |
|
Modified RING finger, C3HGC3-type, found in RING finger and WD repeat domain-containing protein 3 (RFWD3) and similar proteins; RFWD3, also known as RING finger protein 201 (RNF201) or FLJ10520, is an E3 ubiquitin-protein ligase that forms a complex with Mdm2 and p53 to synergistically ubiquitinate p53 and acts as a positive regulator of p53 stability in response to DNA damage. It is phosphorylated by checkpoint kinase ATM/ATR and the phosphorylation mutant fails to stimulate p53 ubiquitination. RFWD3 also functions as a novel replication protein A (RPA)-associated protein involved in DNA replication checkpoint control. RFWD3 contains an N-terminal SQ-rich region followed by a RING finger domain that exhibits robust E3 ubiquitin ligase activity toward p53, a coiled-coil domain and three WD40 repeats in the C-terminus, the latter two of which may be responsible for protein-protein interaction. The RING finger in this family is a modified C3HGC3-type RING finger, but not a canonical C3H2C3-type RING-H2 finger or C3HC4-type RING-HC finger.
Pssm-ID: 438114 [Multi-domain] Cd Length: 61 Bit Score: 40.68 E-value: 2.80e-04
10 20 30
....*....|....*....|....*....|....*....
gi 556079866 2184 IKCFHVFCYDCLKTRYETRQRKCPKCNAPFGTNDYHRLY 2222
Cdd:cd16450 23 LKCGHLFGYSCIEKWLKGKGKKCPQCNKKAKRSDIRPLY 61
|
|
| RING-HC_TRIM13_C-V |
cd16762 |
RING finger, HC subclass, found in tripartite motif-containing protein 13 (TRIM13) and similar ... |
2166-2209 |
2.86e-04 |
|
RING finger, HC subclass, found in tripartite motif-containing protein 13 (TRIM13) and similar proteins; TRIM13, also known as B-cell chronic lymphocytic leukemia tumor suppressor Leu5, leukemia-associated protein 5, putative tumor suppressor RFP2, RING finger protein 77 (RNF77), or Ret finger protein 2, is an endoplasmic reticulum (ER) membrane anchored E3 ubiquitin-protein ligase that interacts with proteins localized to the ER, including valosin-containing protein (VCP), a protein indispensable for ER-associated degradation (ERAD). It also targets the known ER proteolytic substrate CD3-delta, but not the N-end rule substrate Ub-R-YFP (yellow fluorescent protein) for degradation. Moreover, TRIM13 regulates ubiquitination and degradation of NEMO to suppress tumor necrosis factor (TNF) induced nuclear factor-kappaB (NF- kappa B) activation. It is also involved in NF-kappaB p65 activation and nuclear factor of activated T-cells (NFAT)-dependent activation of c-Rel upon T-cell receptor engagement. Furthermore, TRIM13 negatively regulates melanoma differentiation-associated gene 5 (MDA5)-mediated type I interferon production. It also regulates caspase-8 ubiquitination, translocation to autophagosomes, and activation during ER stress induced cell death. Meanwhile, TRIM13 enhances ionizing radiation-induced apoptosis by increasing p53 stability and decreasing AKT kinase activity through MDM2 and AKT degradation. TRIM13 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region. In addition, TRIM13 contains a C-terminal transmembrane domain.
Pssm-ID: 438418 [Multi-domain] Cd Length: 56 Bit Score: 40.67 E-value: 2.86e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 556079866 2166 KEQLTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYETRQR--------KCPKC 2209
Cdd:cd16762 1 EEDLTCPICCCLFDDPRVLPCSHNFCKKCLEGILEGNVRtmlwrppfKCPTC 52
|
|
| COG4487 |
COG4487 |
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown]; |
924-1110 |
2.96e-04 |
|
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 443580 [Multi-domain] Cd Length: 425 Bit Score: 45.71 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 924 EEDAHASLSQSKKKLEGEISGLKKDIEDMELALQKAEQDKATKdhqirnLNDEIQHQDeliNKLNKEKKHLQEASQKtsE 1003
Cdd:COG4487 17 ESLYADIVKQRRAEFEKELAERLADAAKREAALELAEAKAKAQ------LQEQVAEKD---AEIAELRARLEAEERK--K 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1004 DLQATEDKVNHLnkvkAKLEQTLDELEDSLEREKKARGDIEKNKRKvegdLKLA-QEAVADLEK----NKKEMEQNLQRK 1078
Cdd:COG4487 86 ALAVAEEKEKEL----AALQEALAEKDAKLAELQAKELELLKKERE----LEDAkREAELTVEKerdeELDELKEKLKKE 157
|
170 180 190
....*....|....*....|....*....|...
gi 556079866 1079 EKEmaslaaKLEDEQAL-VAKLQKQIKELQARI 1110
Cdd:COG4487 158 EEE------KQLAEKSLkVAEYEKQLKDMQEQI 184
|
|
| RING-HC_RING1-like |
cd16531 |
RING finger, HC subclass, found in really interesting new gene proteins RING1, RING2 and ... |
2169-2212 |
3.08e-04 |
|
RING finger, HC subclass, found in really interesting new gene proteins RING1, RING2 and similar proteins; RING1, also known as polycomb complex protein RING1, RING finger protein 1 (RNF1), or RING finger protein 1A (RING1A), is a transcriptional repressor that is associated with the Polycomb group (PcG) protein complex involved in stable repression of gene activity. RING2, also known as huntingtin-interacting protein 2-interacting protein 3, HIP2-interacting protein 3, protein DinG, RING finger protein 1B (RING1B), RING finger protein 2 (RNF2), or RING finger protein BAP-1, is an E3 ubiquitin-protein ligase that interacts with both nucleosomal DNA and an acidic patch on histone H4 to achieve the specific monoubiquitination of K119 on histone H2A (H2AK119ub), thereby playing a central role in histone code and gene regulation. Both RING1 and RING2 are core components of polycomb repressive complex 1 (PRC1) that functions as an E3-ubuiquitin ligase transferring the mono-ubuiquitin mark to the C-terminal tail of Histone H2A at K118/K119. PRC1 is also capable of chromatin compaction, a function not requiring histone tails, and this activity appears important in gene silencing. RING2 acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity. Members of this family contain a C3HC4-type RING-HC finger.
Pssm-ID: 438193 [Multi-domain] Cd Length: 66 Bit Score: 40.72 E-value: 3.08e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 556079866 2169 LTCPSCKVKRKDAVLIK-CFHVFCYDCLKTRYETRQRKCPKCNAP 2212
Cdd:cd16531 2 LMCPICLGIIKNTMTVKeCLHRFCAECIEKALRLGNKECPTCRKH 46
|
|
| RING-HC_TRIM13_like_C-V |
cd16581 |
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM13, TRIM59 and ... |
2167-2210 |
3.16e-04 |
|
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM13, TRIM59 and similar proteins; TRIM13 and TRIM59, two closely related tripartite motif-containing proteins, belong to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, followed by a C-terminal transmembrane domain. TRIM13, also known as B-cell chronic lymphocytic leukemia tumor suppressor Leu5, leukemia-associated protein 5, putative tumor suppressor RFP2, RING finger protein 77 (RNF77), or Ret finger protein 2, is an endoplasmic reticulum (ER) membrane anchored E3 ubiquitin-protein ligase that interacts with proteins localized to the ER, including valosin-containing protein (VCP), a protein indispensable for ER-associated degradation (ERAD). TRIM59, also known as RING finger protein 104 (RNF104) or tumor suppressor TSBF-1, is a putative E3 ubiquitin-protein ligase that functions as a novel multiple cancer biomarker for immunohistochemical detection of early tumorigenesis.
Pssm-ID: 438243 [Multi-domain] Cd Length: 50 Bit Score: 40.19 E-value: 3.16e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 556079866 2167 EQLTCPSCKVKRKDAVLIKCFHVFCYDCL------KTRYETRQRKCPKCN 2210
Cdd:cd16581 1 EELTCSICYNIFDDPKILPCSHTFCKNCLekllaaSGYYLLASLKCPTCR 50
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1163-1415 |
3.18e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1163 EAELSKLRR----------DLEESNLQHEQAMSNLRKK------------------HNDTVAEMSEQIDQLNKHKAKVEK 1214
Cdd:PRK04863 836 EAELRQLNRrrveleralaDHESQEQQQRSQLEQAKEGlsalnrllprlnlladetLADRVEEIREQLDEAEEAKRFVQQ 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1215 ERATMSA---EVSDLQSllDHSNKAQAnaEKQVKQLEVQLADAQ---------------FKVDEMNRTLND-------LD 1269
Cdd:PRK04863 916 HGNALAQlepIVSVLQS--DPEQFEQL--KQDYQQAQQTQRDAKqqafaltevvqrrahFSYEDAAEMLAKnsdlnekLR 991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1270 GGKKKLAVENSELQRQLEESESQVAQLNKIKASLATQLEEAKRMADEeareraailgkyrnLEHDLDNLRESVEEEQEAK 1349
Cdd:PRK04863 992 QRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQE--------------LKQELQDLGVPADSGAEER 1057
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556079866 1350 ADFQR-QLSKANAEAQLWRSKYESEGL---ARLEELEEAKRKLHGKLQEAEEAMEQLNA-KCSGLEKTKSH 1415
Cdd:PRK04863 1058 ARARRdELHARLSANRSRRNQLEKQLTfceAEMDNLTKKLRKLERDYHEMREQVVNAKAgWCAVLRLVKDN 1128
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1438-1693 |
3.31e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1438 EKRQKSFDKVIAEWKAKVDDLAAELDASQKECRNYSTEVFKLRAAYEESQEHYESVKRENKNLQDEVKDLMDQLGEGGRS 1517
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1518 VHELEKSRKRLEMekeelqaaleeaeaaleqeenkVLRAQlELSQV--RQEIDRRIQEKEEEFENTRKNHQRALDSMQAS 1595
Cdd:COG3883 95 LYRSGGSVSYLDV----------------------LLGSE-SFSDFldRLSALSKIADADADLLEELKADKAELEAKKAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1596 LEAEakgKAEALRLKKKLESDINELEIALDHANKANAEAQKNLKKYQQNVKDLQGALEEEQRARDEAREQYASAERRCNA 1675
Cdd:COG3883 152 LEAK---LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
250
....*....|....*...
gi 556079866 1676 MHGELEESRQLLASSKNS 1693
Cdd:COG3883 229 AAAAAAAAAAAAAAAASA 246
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1569-1688 |
3.58e-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: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1569 RRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRLKKKLESDineLEIALDHANKA-NA-EAQKNLKKYQQNVK 1646
Cdd:COG3096 281 RELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQD---YQAASDHLNLVqTAlRQQEKIERYQEDLE 357
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 556079866 1647 DLQGALEEEQRARDEAREQYASAERRCNAMHGELEESRQLLA 1688
Cdd:COG3096 358 ELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLA 399
|
|
| RING-HC_RNF5 |
cd16743 |
RING finger, HC subclass, found in RING finger protein 5 (RNF5) and similar proteins; RNF5, ... |
2171-2211 |
4.36e-04 |
|
RING finger, HC subclass, found in RING finger protein 5 (RNF5) and similar proteins; RNF5, also known as protein G16 or Ram1, is an E3 ubiquitin-protein ligase anchored to the outer membrane of the endoplasmic reticulum (ER). It acts at early stages of cystic fibrosis (CF) transmembrane conductance regulator (CFTR) biosynthesis and functions as a target for therapeutic modalities to antagonize mutant CFTR proteins in CF patients carrying the F508del allele. It also regulates the turnover of specific G protein-coupled receptors by ubiquitinating JNK-associated membrane protein (JAMP) and preventing proteasome recruitment. RNF5 limits basal levels of autophagy and influences susceptibility to bacterial infection through the regulation of ATG4B stability. It is also involved in the degradation of Pendrin, a transmembrane chloride/anion exchanger highly expressed in thyroid, kidney, and inner ear. RNF5 plays an important role in cell adhesion and migration. It can modulate cell migration by ubiquitinating paxillin. Furthermore, RNF5 interacts with virus-induced signaling adaptor (VISA) at mitochondria in a viral infection-dependent manner, and further targets VISA at K362 and K461 for K48-linked ubiquitination and degradation after viral infection. It also negatively regulates virus-triggered signaling by targeting MITA, also known as STING, for ubiquitination and degradation at the mitochondria. In addition, RNF5 determines breast cancer response to ER stress-inducing chemotherapies through the regulation of the L-glutamine carrier proteins SLC1A5 and SLC38A2 (SLC1A5/38A2). It also has been implicated in muscle organization and in recognition and processing of misfolded proteins. RNF5 contains a C3HC4-type RING-HC finger.
Pssm-ID: 438401 [Multi-domain] Cd Length: 54 Bit Score: 40.25 E-value: 4.36e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 556079866 2171 CPSCKVKRKDAVLIKCFHVFCYDCLKTRYETR--QRKCPKCNA 2211
Cdd:cd16743 3 CNICLETARDAVVSLCGHLFCWPCLHQWLETRpeRQECPVCKA 45
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1188-1731 |
4.72e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.66 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1188 RKKHNDTVAEmseqIDQLNKHKAKVEKERATMSAEVSDLQSL---LDHSNKAQANAEKQVKQLEVQLADAQFKVDEMNRT 1264
Cdd:PRK01156 151 RKKILDEILE----INSLERNYDKLKDVIDMLRAEISNIDYLeekLKSSNLELENIKKQIADDEKSHSITLKEIERLSIE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1265 LNDLDGGKKKLAVENSELQRQLEESESQVAQLNKIKASLATQLEEAKRMADEEAR-----------ERAAILGkYRNLEH 1333
Cdd:PRK01156 227 YNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERhmkiindpvykNRNYIND-YFKYKN 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1334 DLDNLRESVEEEQEAKADFQRQLSKAnAEAQLWRSKYEsEGLARLEELEEAKRKL---HGKLQEAEEAMEQLNAKCSGLE 1410
Cdd:PRK01156 306 DIENKKQILSNIDAEINKYHAIIKKL-SVLQKDYNDYI-KKKSRYDDLNNQILELegyEMDYNSYLKSIESLKKKIEEYS 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1411 KTKSHLQGELedmSIEVDKANALASSLEKRQKSFDKVIAEWKAKVDDLAAELDA--SQKECRNYSTEVFKLRAAY----- 1483
Cdd:PRK01156 384 KNIERMSAFI---SEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRAlrENLDELSRNMEMLNGQSVCpvcgt 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1484 ---EESQEHYESVKRENKN-LQDEVKDLMDQLGEGGRSVHELEKSRKRLEMEKEELQAALEEAEAALEQEENKVLRAQLE 1559
Cdd:PRK01156 461 tlgEEKSNHIINHYNEKKSrLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1560 LSQVR---QEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEA--KGKAEALRLKKKLESDINELEIALDHANKANAEA 1634
Cdd:PRK01156 541 LKDKHdkyEEIKNRYKSLKLEDLDSKRTSWLNALAVISLIDIETnrSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKS 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1635 QKNLKKYQQNVKDLQGALEEEQRARDEAREQYASAERRCNAMHG----ELEESRQLLASSKN-----SHLRHIEQMEGEE 1705
Cdd:PRK01156 621 IREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSiipdLKEITSRINDIEDNlkksrKALDDAKANRARL 700
|
570 580
....*....|....*....|....*.
gi 556079866 1706 LLMQKKLRTEVIRLEDALVQVRKEYE 1731
Cdd:PRK01156 701 ESTIEILRTRINELSDRINDINETLE 726
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1948-2166 |
5.16e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1948 MKKIRGLEETVaslhksLTAQKQEvweeALLSEMEVTGQAFEDMQEQnLRLIQQLREKDDANFKLMSERIKSNQIHKLlQ 2027
Cdd:COG4913 234 FDDLERAHEAL------EDAREQI----ELLEPIRELAERYAAARER-LAELEYLRAALRLWFAQRRLELLEAELEEL-R 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 2028 EEKAMLSEQGATLQAQVEAQNQVVRKLEEkeRLLQNS---LSTLEKELSLRQQAAEMHRRKAVESAQSAADLKLHLEKYL 2104
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEA--QIRGNGgdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA 379
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556079866 2105 AQLKDAQGIVTDRTAVLSQEtfkTKRLQEEILSLRRKVERAKKfELATntdevLMEEIKEYK 2166
Cdd:COG4913 380 EEFAALRAEAAALLEALEEE---LEALEEALAEAEAALRDLRR-ELRE-----LEAEIASLE 432
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1563-1688 |
5.31e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1563 VRQEIDRRIQEKEE-EFENTRKNHQRALDSMQASLEAEAKGKAEALRLKKKLESDineLEIALDHANKANA--EAQKNLK 1639
Cdd:PRK04863 275 MRHANERRVHLEEAlELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQD---YQAASDHLNLVQTalRQQEKIE 351
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 556079866 1640 KYQQNVKDLQGALEEEQRARDEAREQYASAERRCNAMHGELEESRQLLA 1688
Cdd:PRK04863 352 RYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLA 400
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1075-1260 |
5.76e-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: 43.76 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1075 LQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLAreieelserleesggatss 1154
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1155 qiELNKRREAELSKLRRDLEESNLQHEQAMSNLRK-KHNDTVAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDhs 1233
Cdd:COG1579 73 --ARIKKYEEQLGNVRNNKEYEALQKEIESLKRRIsDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD-- 148
|
170 180
....*....|....*....|....*..
gi 556079866 1234 nKAQANAEKQVKQLEVQLADAQFKVDE 1260
Cdd:COG1579 149 -EELAELEAELEELEAEREELAAKIPP 174
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
839-1086 |
5.83e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 839 RVEDELKAMEEKLKKTEEALAKEEKLRKELEEHNVKVLQEKNDLFLQLEAERMGAGDVEERLNKALTQKGDLESQ----- 913
Cdd:PRK01156 480 RLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRykslk 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 914 LADLNDRLSHEEDAHASLS----QSKKKLEGEISGLKKDIED-MELALQKAEQDKATKDHQIRNLNDEIQHQDELINKLn 988
Cdd:PRK01156 560 LEDLDSKRTSWLNALAVISlidiETNRSRSNEIKKQLNDLESrLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEI- 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 989 KEKKHLQEASQKTSEDLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKRKVEGDLKLAQEAVADLEKNK 1068
Cdd:PRK01156 639 QENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRI 718
|
250
....*....|....*...
gi 556079866 1069 KEMEQNLQRKEKEMASLA 1086
Cdd:PRK01156 719 NDINETLESMKKIKKAIG 736
|
|
| RING-HC_RNF151 |
cd16547 |
RING finger, HC subclass, found in RING finger protein 151 (RNF151) and similar proteins; ... |
2169-2212 |
6.49e-04 |
|
RING finger, HC subclass, found in RING finger protein 151 (RNF151) and similar proteins; RNF151 is a testis-specific RING finger protein that interacts with dysbindin, a synaptic and microtubular protein that binds brain snapin, a SNARE-binding protein that mediates intracellular membrane fusion in both neuronal and non-neuronal cells. Thus, it may be involved in acrosome formation of spermatids by interacting with multiple proteins participating in membrane biogenesis and microtubule organization. RNF151 contains a C3HC4-type RING finger domain, a putative nuclear localization signal (NLS), and a TNF receptor associated factor (TRAF)-type zinc finger domain.
Pssm-ID: 438209 [Multi-domain] Cd Length: 49 Bit Score: 39.37 E-value: 6.49e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 556079866 2169 LTCPSCKVKRKDAVLIKCFHVFCYDCLkTRYETRQRKCPKCNAP 2212
Cdd:cd16547 4 LICSICHGVLRCPVRLSCSHIFCKKCI-LQWLKRQETCPCCRKE 46
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
931-1361 |
6.68e-04 |
|
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: 45.10 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 931 LSQSKKKLEGEISGLKkdIEDMELALQKAEQDKATKdhqIRNlNDEIQhQDELINKLNKEKKHLQEASQ--KTSEDLQAT 1008
Cdd:pfam05483 365 LRTEQQRLEKNEDQLK--IITMELQKKSSELEEMTK---FKN-NKEVE-LEELKKILAEDEKLLDEKKQfeKIAEELKGK 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1009 EDKVNHLNKVKaklEQTLDELEDSLEREKKARGDIEKNKRKVEGDLKLAQEAVADLEKNKKEMEQNLQRKEKEMASLAAK 1088
Cdd:pfam05483 438 EQELIFLLQAR---EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLE 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1089 LEDEQALVAKLQKQIKELQARIEELEEELEAERQ----ARAKAEKQRADLAREIEELSERLEESGGATSSQIELNKRREA 1164
Cdd:pfam05483 515 LKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDelesVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILEN 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1165 ELSKLRRDLEESNLQHEQamsnLRKKHNDTVAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDHSNKAQANAEKQV 1244
Cdd:pfam05483 595 KCNNLKKQIENKNKNIEE----LHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISE 670
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1245 KQLEVQLADAQFKVDEMNRTLNDLDggkKKLAVENSELQRQLEESESqvaQLNKIKASLATQLEEAKRMADEEARERAAI 1324
Cdd:pfam05483 671 EKLLEEVEKAKAIADEAVKLQKEID---KRCQHKIAEMVALMEKHKH---QYDKIIEERDSELGLYKNKEQEQSSAKAAL 744
|
410 420 430
....*....|....*....|....*....|....*..
gi 556079866 1325 LGKYRNLEHDLDNLRESVEEEQEAKADFQRQLSKANA 1361
Cdd:pfam05483 745 EIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTA 781
|
|
| RING-HC_TRIM26_C-IV |
cd16598 |
RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar ... |
2166-2213 |
6.85e-04 |
|
RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar proteins; TRIM26, also known as acid finger protein (AFP), RING finger protein 95 (RNF95), or zinc finger protein 173 (ZNF173), is an E3 ubiquitin-protein ligase that negatively regulates interferon-beta production and antiviral response through polyubiquitination and degradation of nuclear transcription factor IRF3. It functions as an important regulator for RNA virus-triggered innate immune response by bridging TBK1 to NEMO (NF-kappaB essential modulator, also known as IKKgamma) and mediating TBK1 activation. It also acts as a novel tumor suppressor of hepatocellular carcinoma by regulating cancer cell proliferation, colony forming ability, migration, and invasion. TRIM26 belongs the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.
Pssm-ID: 438260 [Multi-domain] Cd Length: 64 Bit Score: 39.76 E-value: 6.85e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 556079866 2166 KEQLTCPSCKVKRKDAVLIKCFHVFCYDCLkTRY-----ETRQRKCPKCNAPF 2213
Cdd:cd16598 2 EEEVTCSICLDYLRDPVTIDCGHNFCRSCI-TDYcpisgGHERPVCPLCRKPF 53
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
826-1037 |
6.94e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 6.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 826 KLYSKVKPLLSAVRVEDELKAMEEKLKKTEEALAKEEKLRKELEEHNVKVLQEKNDLFLQLEAERMGAGDVEERLNKALT 905
Cdd:PRK02224 493 EVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEARE 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 906 QKGDLESQLADLNDRLSHEEDAHASLSQsKKKLEGEISGLKKDIEDM-ELALQKAEQDKATKDhQIRNLNDEiqHQDELI 984
Cdd:PRK02224 573 EVAELNSKLAELKERIESLERIRTLLAA-IADAEDEIERLREKREALaELNDERRERLAEKRE-RKRELEAE--FDEARI 648
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 556079866 985 NKLNKEKKHLQEASQKTSEDLQATEDKVNHLNKVKAKLEQTLDELEDSLEREK 1037
Cdd:PRK02224 649 EEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERRE 701
|
|
| RING-HC_ScPSH1-like |
cd16568 |
RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated ... |
2165-2209 |
7.11e-04 |
|
RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated protein 1 (ScPSH1) and similar proteins; ScPSH1 is a Cse4-specific E3 ubiquitin ligase that interacts with the kinetochore protein Pat1 and targets the degradation of budding yeast centromeric histone H3 variant, CENP-ACse4, which is essential for faithful chromosome segregation. ScPSH1 contains a C3HC4-type RING-HC finger and a DNA directed RNA polymerase domain.
Pssm-ID: 438230 [Multi-domain] Cd Length: 54 Bit Score: 39.66 E-value: 7.11e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 556079866 2165 YKEQLTCPSCKVKRKDAVLIKCFHVFCYDCLKTRY-ETRQRKCPKC 2209
Cdd:cd16568 1 ILETQECIICHEYLYEPMVTTCGHTYCYTCLNTWFkSNRSLSCPDC 46
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1382-2102 |
7.23e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 7.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1382 EEAKRKLHGKLQE---AEEAMEQLNAKCSGLEKTKSHLQGELEDM-SIEVDKANALASSLEKRQKSFDKVIAEWKAKVDD 1457
Cdd:PTZ00121 1101 EEAKKTETGKAEEarkAEEAKKKAEDARKAEEARKAEDARKAEEArKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEA 1180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1458 LAAELDASQKECRNYSTEVFKLRAA--YEESQEHYESVKRENKNLQDEVKDlMDQLGEGGRSVHELEKSRKRLEMEKEEL 1535
Cdd:PTZ00121 1181 ARKAEEVRKAEELRKAEDARKAEAArkAEEERKAEEARKAEDAKKAEAVKK-AEEAKKDAEEAKKAEEERNNEEIRKFEE 1259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1536 QAALEEAEAALEQEENKVLRAQ--LELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAE-AKGKAEALrlKKK 1612
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKADelKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEeAKKKADAA--KKK 1337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1613 LESDINELEIALDHANKANAEAQKNLKKYQQNVKDlqgalEEEQRARDEAREQYASAERRCNAMHGELEESRQLLASSKN 1692
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK-----KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK 1412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1693 shlRHIEQMEGEELlmqKKLRTEVIRLEDAlvqvRKEYEMLRIEFEQNLAATEQTGPINREmRHLITSLQSHNRQLKGEV 1772
Cdd:PTZ00121 1413 ---AAAAKKKADEA---KKKAEEKKKADEA----KKKAEEAKKADEAKKKAEEAKKAEEAK-KKAEEAKKADEAKKKAEE 1481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1773 SRYKRKLREAAAEAARLKQTLEMSNVAVSSTTVPSSASSTSSDNGSSRGEEGAPVscpQPGQGGREEGGTPSASSQRREE 1852
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA---DEAKKAEEKKKADELKKAEELK 1558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1853 EAREEEPIPEREKGKSDLDIIRDLKAQLKKSQEAQRELKLLLDMYKGAPKEQR----DKVQLMAAEKKARAEVEEHRQQL 1928
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEakkaEEAKIKAEELKKAEEEKKKVEQL 1638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1929 KKLAEHERKERRKLADEDAMKKIRGLEEtvaslhksltAQKQEvweeallsemEVTGQAFEDMQEQnlrliQQLREKDDA 2008
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKAAEE----------AKKAE----------EDKKKAEEAKKAE-----EDEKKAAEA 1693
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 2009 NFKLMSERIKSNQIHKLLQEEKAMLSEQGATLQAQVEAQNQVVRKLEEKERLLQNSLSTLEKELSLRQQAAEMHRRKAVE 2088
Cdd:PTZ00121 1694 LKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEI 1773
|
730
....*....|....
gi 556079866 2089 SAQSAADLKLHLEK 2102
Cdd:PTZ00121 1774 RKEKEAVIEEELDE 1787
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1155-1715 |
7.68e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.81 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1155 QIELNKRREAELSKLRRDLEE---SNLQHEQAMSNLRKKHNDTVAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLL- 1230
Cdd:pfam10174 86 QRDLNQLLQQDFTTSPVDGEDkfsTPELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKLLe 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1231 --------------DHSNKAQ-ANAEKQVKQLEVQLADAQFKV----DEMNRTLNDLDGGKKKLAvenseLQRQLEESES 1291
Cdd:pfam10174 166 mlqskglpkksgeeDWERTRRiAEAEMQLGHLEVLLDQKEKENihlrEELHRRNQLQPDPAKTKA-----LQTVIEMKDT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1292 QVAQLNKIKASLATQLEEAKRMAD---EEARERAAILGKYRN----LEHDLDNLRESVEEEQEAKADFQRQLSKANAEAQ 1364
Cdd:pfam10174 241 KISSLERNIRDLEDEVQMLKTNGLlhtEDREEEIKQMEVYKShskfMKNKIDQLKQELSKKESELLALQTKLETLTNQNS 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1365 LWRSKYE--SEGLARLEE----LEEAKRKLHGKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEVD----KANALA 1434
Cdd:pfam10174 321 DCKQHIEvlKESLTAKEQraaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDvkerKINVLQ 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1435 SSLEKRQ---KSFDKVIAEWKAKVDDLaaELDASQKECRNYSTE---------VFKLRAAYE----ESQEHYESVKRENK 1498
Cdd:pfam10174 401 KKIENLQeqlRDKDKQLAGLKERVKSL--QTDSSNTDTALTTLEealsekeriIERLKEQREredrERLEELESLKKENK 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1499 NLQDEVKDLMDQLGEGGRSVHELEKSRKRLEMEKEELQAALEEAEAALEQEENKVLRAQLEL---------SQVRQEIDR 1569
Cdd:pfam10174 479 DLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLkkahnaeeaVRTNPEIND 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1570 RIQEKEEEFENTRKNHQRAldsmQASLEAEAKGKAEALRLKKKLESDINELEIALDHANKANAEAQKNLKKYQQNVKDLQ 1649
Cdd:pfam10174 559 RIRLLEQEVARYKEESGKA----QAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKG 634
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556079866 1650 GALEEEQRARDEAREQyASAERRCNAMHGELEESRQLLASSKnSHLRHIEQMEGEELLMQKKLRTE 1715
Cdd:pfam10174 635 AQLLEEARRREDNLAD-NSQQLQLEELMGALEKTRQELDATK-ARLSSTQQSLAEKDGHLTNLRAE 698
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1197-1351 |
7.78e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1197 EMSEQIDQLNKHKAKVEKERATMSA--EVSDLQSLLDHSNKAQanaEKQVKQLEVQLADaqfKVDEMNRTLNDLDGGKKK 1274
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKKEALLEAkeEIHKLRNEFEKELRER---RNELQKLEKRLLQ---KEENLDRKLELLEKREEE 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556079866 1275 LAVENSELQRQLEESESQVAQLNKIKASLATQLEEAKRMADEEARERaaILGKYRN-LEHDLDNLRESVEEEQEAKAD 1351
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEI--LLEKVEEeARHEAAVLIKEIEEEAKEEAD 187
|
|
| RING-HC_CeBARD1-like |
cd23143 |
RING finger, HC subclass, found in Caenorhabditis elegans BRCA1-associated RING domain protein ... |
2171-2213 |
8.21e-04 |
|
RING finger, HC subclass, found in Caenorhabditis elegans BRCA1-associated RING domain protein 1 (CeBARD1) and similar proteins; CeBARD1, also called Ce-BRD-1, Cebrd-1, or RING-type E3 ubiquitin transferase BARD1, is a constituent of the CeBCD complex that possesses E3 ubiquitin-protein ligase activity. It plays a role in triggering cellular responses at damage sites in response to DNA damage that may be induced by ionizing radiation. It protects against chromosome non-disjunction and nuclear fragmentation during meiotic double-strand break repair to ensure sister chromatid recombination and aid chromosome stability. CeBARD1 contains a typical C3HC4-type RING-HC finger.
Pssm-ID: 438505 [Multi-domain] Cd Length: 47 Bit Score: 39.07 E-value: 8.21e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 556079866 2171 CPSCKVKRKDAVLIK-CFHVFCYDCLKTRYETRQrKCPKCNAPF 2213
Cdd:cd23143 4 CVICSEPQIDTFLLSsCGHIYCWECFTEFIEKRH-MCPSCRFPL 46
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1084-1468 |
8.64e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 44.29 E-value: 8.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1084 SLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLAREIEELSERLEESGGATSSQIELnkrrE 1163
Cdd:pfam19220 14 EMADRLEDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEEL----V 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1164 AELSKLRRDLEESNLQHEQAMSNLRKK----------------HNDTVAE----MSEQIDQLNKHKAKVEKERATmsaeV 1223
Cdd:pfam19220 90 ARLAKLEAALREAEAAKEELRIELRDKtaqaealerqlaaeteQNRALEEenkaLREEAQAAEKALQRAEGELAT----A 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1224 SDLQSLLDHSNKA-QANAEKQVkqleVQLADAQFKVDEMNRTLND----LDGGKKKLAVENSELQRQLEESESQVAQLNK 1298
Cdd:pfam19220 166 RERLALLEQENRRlQALSEEQA----AELAELTRRLAELETQLDAtrarLRALEGQLAAEQAERERAEAQLEEAVEAHRA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1299 IKASLATQLEEAkrmadeEARERAA--ILGKYRNlehdldNLRESVEEeqeakadfQRQLSKANAEAQLWRSKYEseglA 1376
Cdd:pfam19220 242 ERASLRMKLEAL------TARAAATeqLLAEARN------QLRDRDEA--------IRAAERRLKEASIERDTLE----R 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1377 RLEELEEAKRKLHGKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMsieVDKANALASSLEKRQKSFDKVIAEWKAKVD 1456
Cdd:pfam19220 298 RLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERA---EERIASLSDRIAELTKRFEVERAALEQANR 374
|
410
....*....|..
gi 556079866 1457 DLAAELDASQKE 1468
Cdd:pfam19220 375 RLKEELQRERAE 386
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1867-2059 |
8.89e-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: 44.34 E-value: 8.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1867 KSDLDIIRDLKAQLKKSQEAQRELKLLLDMYKGAPKEQRD-KVQLMAAEK-----KARAEVEEHRQQLKKL--AEHERKE 1938
Cdd:pfam17380 395 RQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQrEVRRLEEERaremeRVRLEEQERQQQVERLrqQEEERKR 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1939 RRKLADEDAMKKIRGLEETVASLHKSLTAQKQEVWEEA-----LLSEMEVTGQAFedMQEQNLRLIQQLREKDdanfKLM 2013
Cdd:pfam17380 475 KKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEErkrklLEKEMEERQKAI--YEEERRREAEEERRKQ----QEM 548
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 556079866 2014 SERiksnqihKLLQEEKAMLSEQGATLQAqVEAQNQVVRKLEEKER 2059
Cdd:pfam17380 549 EER-------RRIQEQMRKATEERSRLEA-MEREREMMRQIVESEK 586
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1975-2171 |
8.95e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1975 EALLSEMEVTGQAFEDMQEQNLRLIQQLREKDDANFKLMSERIKSNQIHKLLQEEKAmLSEQGATLQAQVEAQNQVVRKL 2054
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE-LKEEIEELEKELESLEGSKRKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 2055 EEKERLLQNSLSTLEKELS-LRQQAAEMHRRKAVESAQSA--------ADLKLHLEKYLAQLKDAQGIVTDRTAVLSQET 2125
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEeLEEKVKELKELKEKAEEYIKlsefyeeyLDELREIEKRLSRLEEEINGIEERIKELEEKE 337
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 556079866 2126 FKTKRLQEEILSLRRKVERAKKFELATNTDEVLMEEIKEYKEQLTC 2171
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTG 383
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1225-1401 |
9.23e-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: 9.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1225 DLQSL---LDHSNKAQANAEKQVKQLEVQLADAQFKVDEMNRTLNDLDGGKKKLAVENSELQRQLEESESQVAQLNKIK- 1300
Cdd:COG1579 11 DLQELdseLDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKe 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1301 -ASLATQLEEAKRMADEeareraailgkyrnLEHDLDNLRESVEEEQEAKADFQRQLSKANAEAQLWRSKYEseglARLE 1379
Cdd:COG1579 91 yEALQKEIESLKRRISD--------------LEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD----EELA 152
|
170 180
....*....|....*....|..
gi 556079866 1380 ELEEAKRKLHGKLQEAEEAMEQ 1401
Cdd:COG1579 153 ELEAELEELEAEREELAAKIPP 174
|
|
| RING-H2_RNF32_rpt1 |
cd16677 |
first RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; ... |
2171-2212 |
9.56e-04 |
|
first RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; RNF32 is mainly expressed in testis spermatogenesis, most likely in spermatocytes and/or in spermatids, suggesting a possible role in sperm formation. RNF32 contains two C3H2C3-type RING-H2 fingers separated by an IQ domain of unknown function. Although the biological function of RNF32 remains unclear, proteins with double RING-H2 fingers may act as scaffolds for binding several proteins that function in the same pathway. This model corresponds to the first RING-H2 finger.
Pssm-ID: 438339 [Multi-domain] Cd Length: 49 Bit Score: 38.82 E-value: 9.56e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 556079866 2171 CPSCK--VKRKDAVLIKCFHVFCYDCLKtRYE--TRQRKCPKCNAP 2212
Cdd:cd16677 2 CPICLedFGLQQQVLLSCSHVFHRACLE-SFErfSGKKTCPMCRKE 46
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1569-2030 |
9.63e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 9.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1569 RRIQEKEEEFENTRKNHQRaLDSMQASLEAEAKGKAEALRLKKKLESDINELEIALDHAN--KANAEAQKNLKKYQQNVK 1646
Cdd:COG4717 71 KELKELEEELKEAEEKEEE-YAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1647 dlqgALEEEQRARDEAREQYASAERRCNAMHGELEESRQLLASSKNSHLrhieqmegeellmqKKLRTEVIRLEDALVQV 1726
Cdd:COG4717 150 ----ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL--------------QDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1727 RKEYEMLRIEFEQNLAATEQTgpinrEMRHLITSLQSHNRQLKGEVSRYKRKLREAAAEAARLKQTLEMSNVAVSSTTVP 1806
Cdd:COG4717 212 EEELEEAQEELEELEEELEQL-----ENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1807 SSASSTSSDNGSSRGEEGAPVSCPQPGQGGREEGGTPSASSQ---RREEEAREEEPIPEREKGKSDLDIIRDLKAQLKKs 1883
Cdd:COG4717 287 ALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRIEELQELLREAEELEEELQL- 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1884 QEAQRELKLLLDMYKGAPKEQ-RDKVQLMAAEKKARAEVEEHRQQLKKLAEHERKERRKLADEDAMKKIRGLEETVASLH 1962
Cdd:COG4717 366 EELEQEIAALLAEAGVEDEEElRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELE 445
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556079866 1963 KSLTAQKQEVWE-EALLSEMEvTGQAFEDMQEQNLRLIQQLREKDDANFKLMSERIKSNQIHKLLQEEK 2030
Cdd:COG4717 446 EELEELREELAElEAELEQLE-EDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1040-1243 |
1.03e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 43.68 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1040 RGDIEKNKRKVEGDLKLAQEAVADLEKNKKEMEQNLQR-KEKEMASLAAKLEDEQALVAKL-QKQIKELQARieeleEEL 1117
Cdd:TIGR02794 56 QQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKElEQRAAAEKAAKQAEQAAKQAEEkQKQAEEAKAK-----QAA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1118 EAERQARAKAEKQRADLAREIEELSERLEESGGATSSQIELNKRREAELSKlrRDLEESNLQHEQAMSNLRKKHNDTVAE 1197
Cdd:TIGR02794 131 EAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKA--KAEAEAKAKAEEAKAKAEAAKAKAAAE 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 556079866 1198 MSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDHSNKAQANAEKQ 1243
Cdd:TIGR02794 209 AAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARG 254
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1553-1731 |
1.06e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1553 VLRAQLELSQVRQEIDR------RIQEKEEEFENTRKNHQRALDSMQASLeAEAKGKAealrlKKKLESDINELEIALDH 1626
Cdd:COG4913 283 LWFAQRRLELLEAELEElraelaRLEAELERLEARLDALREELDELEAQI-RGNGGDR-----LEQLEREIERLERELEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1627 ANKANAEAQKNLKK-----------YQQNVKDLQGALEEEQRARDEAREQYASAERRCNAMHGELEESRQLLASSKNSHL 1695
Cdd:COG4913 357 RERRRARLEALLAAlglplpasaeeFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 556079866 1696 RhieqMEGEELLMQKKLRTEV-IRLEDA-----LVQVRKEYE 1731
Cdd:COG4913 437 N----IPARLLALRDALAEALgLDEAELpfvgeLIEVRPEEE 474
|
|
| RING-HC_RNF213 |
cd16561 |
RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; ... |
2171-2209 |
1.15e-03 |
|
RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; RNF213, also known as ALK lymphoma oligomerization partner on chromosome 17 or Moyamoya steno-occlusive disease-associated AAA+ and RING finger protein (mysterin), is an intracellular soluble protein that functions as an E3 ubiquitin-protein ligase and AAA+ ATPase, which possibly contributes to vascular development through mechanical processes in the cell. It plays a unique role in endothelial cells for proper gene expression in response to inflammatory signals from the environment. Mutations in RNF213 may be associated with Moyamoya disease (MMD), an idiopathic cerebrovascular occlusive disorder prevalent in East Asia. It also acts as a nuclear marker for acanthomorph phylogeny. RNF213 contains two tandem enzymatically active AAA+ ATPase modules and a C3HC4-type RING-HC finger. It can form a huge ring-shaped oligomeric complex.
Pssm-ID: 438223 [Multi-domain] Cd Length: 50 Bit Score: 38.80 E-value: 1.15e-03
10 20 30
....*....|....*....|....*....|....*....
gi 556079866 2171 CPSCKVKRKDAVLIKCFHVFCYDCLKTRYETRQRkCPKC 2209
Cdd:cd16561 5 CSICLEDLNDPVKLPCDHVFCEECIRQWLPGQMS-CPLC 42
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1006-1175 |
1.21e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1006 QATEDKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIEknkrkVEGDLKLAQEAVADLEKNKKEMEQNLQRKEKEMASL 1085
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVD-----LSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1086 AAKLED---------EQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLAREIEELSERLEEsggATSSQI 1156
Cdd:COG3206 246 RAQLGSgpdalpellQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILA---SLEAEL 322
|
170
....*....|....*....
gi 556079866 1157 ELNKRREAELSKLRRDLEE 1175
Cdd:COG3206 323 EALQAREASLQAQLAQLEA 341
|
|
| RING-HC_RING1 |
cd16739 |
RING finger, HC subclass, found in really interesting new gene 1 protein (RING1) and similar ... |
2168-2209 |
1.21e-03 |
|
RING finger, HC subclass, found in really interesting new gene 1 protein (RING1) and similar proteins; RING1, also known as polycomb complex protein RING1, RING finger protein 1 (RNF1), or RING finger protein 1A (RING1A), was identified as a transcriptional repressor that is associated with the Polycomb group (PcG) protein complex involved in stable repression of gene activity. It is a core component of polycomb repressive complex 1 (PRC1) that functions as an E3-ubuiquitin ligase that transferring the mono-ubuiquitin mark to the C-terminal tail of Histone H2A at K118/K119. PRC1 is also capable of chromatin compaction, a function not requiring histone tails, and this activity appears important in gene silencing. RING1 interacts with multiple PcG proteins and displays tumorigenic activity. It also shows zinc-dependent DNA binding activity. Moreover, RING1 inhibits transactivation of the DNA-binding protein recombination signal binding protein-Jkappa (RBP-J) by Notch through interaction with the LIM domains of KyoT2. RING1 contains a C3HC4-type RING-HC finger.
Pssm-ID: 438397 [Multi-domain] Cd Length: 70 Bit Score: 39.29 E-value: 1.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 556079866 2168 QLTCPSCKVKRKDAVLIK-CFHVFCYDCLKTRYETRQRKCPKC 2209
Cdd:cd16739 3 ELMCPICLDMLKNTMTTKeCLHRFCSDCIVTALRSGNKECPTC 45
|
|
| RING-HC_RNFT1 |
cd16741 |
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 1 ... |
2171-2209 |
1.22e-03 |
|
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 1 (RNFT1); RNFT1, also known as protein PTD016, is a multi-pass membrane protein containing a C3HC4-type RING-HC finger. Its biological role remains unclear.
Pssm-ID: 438399 [Multi-domain] Cd Length: 58 Bit Score: 39.10 E-value: 1.22e-03
10 20 30
....*....|....*....|....*....|....*....
gi 556079866 2171 CPSCKVKRKDAVLIKCFHVFCYDCLkTRYETRQRKCPKC 2209
Cdd:cd16741 17 CAICQAEFRKPILLICQHVFCEECI-SLWFNREKTCPLC 54
|
|
| RING-HC_TRIM4_C-IV |
cd16590 |
RING finger, HC subclass, found in tripartite motif-containing protein TRIM4 and similar ... |
2163-2212 |
1.25e-03 |
|
RING finger, HC subclass, found in tripartite motif-containing protein TRIM4 and similar proteins; TRIM4 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. TRIM4, also known as RING finger protein 87 (RNF87), is a cytoplasmic E3 ubiquitin-protein ligase that has recently evolved and is present only in higher mammals. It transiently interacts with mitochondria, induces mitochondrial aggregation and sensitizes the cells to hydrogen peroxide (H2O2) induced death. Its interaction with peroxiredoxin 1 (PRX1) is critical for the regulation of H2O2 induced cell death. Moreover, TRIM4 functions as a positive regulator of RIG-I-mediated type I interferon induction. It regulates the K63-linked ubiquitination of RIG-1 and assembly of antiviral signaling complex at the mitochondria.
Pssm-ID: 438252 [Multi-domain] Cd Length: 61 Bit Score: 39.24 E-value: 1.25e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 556079866 2163 KEYKEQLTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYET--RQRKCPKCNAP 2212
Cdd:cd16590 1 EDIQEELTCPICLDYFQDPVSIECGHNFCRGCLHRNWAPggGPFPCPECRHP 52
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1902-2182 |
1.26e-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: 43.96 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1902 KEQRDKVQLMAAEKkARAEVEEHRQQLKKLAEHERKERRKLADEDAMKKIRGLEETVASLHKSltaQKQEVWEEALLSEM 1981
Cdd:pfam17380 287 RQQQEKFEKMEQER-LRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERER---ELERIRQEERKREL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1982 EVTGQAFEDMQEQNLRLIQQLREKDDANFKLMSERIKSNQIHKLLQEEKAMLSEQGATLQAQV-----EAQNQVVRKLEE 2056
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIraeqeEARQREVRRLEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 2057 K-----ERLLQNSLSTLEKELSLRQQAAEmHRRKAVESAQSAADLKLHLEKYLAQLKdaQGIVTDRTAVLSQETfKTKRL 2131
Cdd:pfam17380 443 EraremERVRLEEQERQQQVERLRQQEEE-RKRKKLELEKEKRDRKRAEEQRRKILE--KELEERKQAMIEEER-KRKLL 518
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 556079866 2132 QEEILSLRRKV---ERAKKFELATNTdEVLMEEIKEYKEQLTCPSCKVKRKDAV 2182
Cdd:pfam17380 519 EKEMEERQKAIyeeERRREAEEERRK-QQEMEERRRIQEQMRKATEERSRLEAM 571
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1236-1413 |
1.26e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 43.69 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1236 AQANAEKQVKQLEVQLADAQFKVDEMNRTLNDLDggkkklavenseLQRQLEESESQVAQLNKIKASLATQLEEAKRMAD 1315
Cdd:COG3524 178 AVRFAEEEVERAEERLRDAREALLAFRNRNGILD------------PEATAEALLQLIATLEGQLAELEAELAALRSYLS 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1316 EEAREraailgkYRNLEHDLDNLRESVEEEqeakadfQRQLSKANAEAQLwrskyeSEGLARLEELEEakrklhgklqEA 1395
Cdd:COG3524 246 PNSPQ-------VRQLRRRIAALEKQIAAE-------RARLTGASGGDSL------ASLLAEYERLEL----------ER 295
|
170
....*....|....*...
gi 556079866 1396 EEAMEQLNAKCSGLEKTK 1413
Cdd:COG3524 296 EFAEKAYTSALAALEQAR 313
|
|
| RING-HC_TRIM47-like_C-IV |
cd16604 |
RING finger, HC subclass, found in tripartite motif-containing protein 47 (TRIM47) and similar ... |
2169-2213 |
1.28e-03 |
|
RING finger, HC subclass, found in tripartite motif-containing protein 47 (TRIM47) and similar proteins; TRIM47, also known as gene overexpressed in astrocytoma protein (GOA) or RING finger protein 100 (RNF100), belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. It plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis. This subfamily also includes RING finger protein 135 (RNF135). RNF135, also known as RIG-I E3 ubiquitin ligase (REUL) or Riplet, is a widely expressed E3 ubiquitin-protein ligase that consists of an N-terminal C3HC4-type RING-HC finger and C-terminal B30.2/SPRY and PRY motifs, but lacks the B-box and coiled-coil domains that are also typically present in TRIM proteins. RNF135 serves as a specific retinoic acid-inducible gene-I (RIG-I)-interacting protein that ubiquitinates RIG-I and specifically stimulates RIG-I-mediated innate antiviral activity to produce antiviral type-I interferon (IFN) during the early phase of viral infection. It also has been identified as a bio-marker and therapy target of glioblastoma. It associates with the ERK signal transduction pathway and plays a role in glioblastoma cell proliferation, migration and cell cycle.
Pssm-ID: 438266 [Multi-domain] Cd Length: 49 Bit Score: 38.56 E-value: 1.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 556079866 2169 LTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYETRQRK---CPKCNAPF 2213
Cdd:cd16604 1 LSCPICLDLLKDPVTLPCGHSFCMGCLGALWGAGRGGrasCPLCRQTF 48
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1285-1464 |
1.28e-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: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1285 QLEESESQVAQLNKIKASLATQLEEAKRMADEEARERAAILGKYRNLEHDLDNLRESVEEEQEAKADFQRQLSKAnaeaq 1364
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1365 lwRSKYESEGLAR-LEELEEAKRKLHGKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEdmsievdkanALASSLEKRQKS 1443
Cdd:COG1579 86 --RNNKEYEALQKeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELE----------EKKAELDEELAE 153
|
170 180
....*....|....*....|.
gi 556079866 1444 FDKVIAEWKAKVDDLAAELDA 1464
Cdd:COG1579 154 LEAELEELEAEREELAAKIPP 174
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1027-1376 |
1.33e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.70 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1027 DELEDSLEREKKARGDIEKNKRKvEGDLKLAQEAVADLEKNKKEMEQNLQRKEKEmaslaaKLEDEQALVAKLQKQIKEL 1106
Cdd:pfam02029 3 DEEEAARERRRRAREERRRQKEE-EEPSGQVTESVEPNEHNSYEEDSELKPSGQG------GLDEEEAFLDRTAKREERR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1107 QARIEELEEELEAERQARAKAEKQRADLAREIEELSERLEESGgaTSSQIELNKRREAELSKLRRDLEESNLQHEQAMSN 1186
Cdd:pfam02029 76 QKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKE--EKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1187 LRKKHNDTVAEMSEQIDQLNKHKAKVEKERATMSAEVS-DLQSLLD----HSNKAQANAEKQVKQLEVQladAQFKVDEM 1261
Cdd:pfam02029 154 EEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKyESKVFLDqkrgHPEVKSQNGEEEVTKLKVT---TKRRQGGL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1262 NRTLNDLDGGKKKLAVENS--ELQRQLEESESQVA-QLNKIKASLATQLEEAKRMADEEARERAAILGKYRNLEHDldnl 1338
Cdd:pfam02029 231 SQSQEREEEAEVFLEAEQKleELRRRRQEKESEEFeKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAE---- 306
|
330 340 350
....*....|....*....|....*....|....*...
gi 556079866 1339 RESVEEEQeaKADFQRQLSKANAEAQLWRSKYESEGLA 1376
Cdd:pfam02029 307 RKLREEEE--KRRMKEEIERRRAEAAEKRQKLPEDSSS 342
|
|
| RING-HC_PRT1-like |
cd23132 |
RING finger, HC subclass, found in Arabidopsis thaliana proteolysis 1 protein (PRT1) and ... |
2167-2214 |
1.35e-03 |
|
RING finger, HC subclass, found in Arabidopsis thaliana proteolysis 1 protein (PRT1) and similar proteins; PRT1, also called RING-type E3 ubiquitin transferase PRT1, is an E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. It functions in the N-end rule pathway of protein degradation, where it specifically recognizes and ubiquitinates proteins with an N-terminal bulky aromatic amino acid (Phe). It does not act on aliphatic hydrophobic and basic N-terminal residues (Arg or Leu) containing proteins. PRT1 contains a typical C3HC4-type RING-HC finger.
Pssm-ID: 438494 [Multi-domain] Cd Length: 52 Bit Score: 38.56 E-value: 1.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 556079866 2167 EQLTCPSCKVKRKDAVLIKCFHVFCYDCL-KTRYETRQRKCPKCNAPFG 2214
Cdd:cd23132 1 EEFLCCICLDLLYKPVVLECGHVFCFWCVhRCMNGYDESHCPLCRRPYD 49
|
|
| RING-HC_RNF208 |
cd16559 |
RING finger, HC subclass, found in RING finger protein 208 (RNF208) and similar proteins; ... |
2169-2209 |
1.36e-03 |
|
RING finger, HC subclass, found in RING finger protein 208 (RNF208) and similar proteins; RNF208 is an E3 ubiquitin-protein ligase whose activity can be modulated by S-nitrosylation. It contains a C3HC4-type RING-HC finger.
Pssm-ID: 438221 [Multi-domain] Cd Length: 56 Bit Score: 38.76 E-value: 1.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 556079866 2169 LTCPSCK----VKRKDAVLIKCFHVFCYDCLKTRYETRQRK----CPKC 2209
Cdd:cd16559 2 LLCPTCGhsynFTNKRPRILSCLHSVCEECLQILYESCPKYkfisCPTC 50
|
|
| zf-RING_5 |
pfam14634 |
zinc-RING finger domain; |
2171-2210 |
1.40e-03 |
|
zinc-RING finger domain;
Pssm-ID: 434085 [Multi-domain] Cd Length: 43 Bit Score: 38.18 E-value: 1.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 556079866 2171 CPSC---KVKRKDAVLIKCFHVFCYDCLKTryETRQRKCPKCN 2210
Cdd:pfam14634 2 CNKCfkeLSKTRPFYLTSCGHIFCEECLTR--LLQERQCPICK 42
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
939-1319 |
1.50e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.66 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 939 EGEISGLKKDIEDMELALQ--KAEQDKATKDHQ--IRNLNDEIQHQDELINKLNKEKkhlQEASQKTSEdLQATEDKVNH 1014
Cdd:pfam10174 239 DTKISSLERNIRDLEDEVQmlKTNGLLHTEDREeeIKQMEVYKSHSKFMKNKIDQLK---QELSKKESE-LLALQTKLET 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1015 LNKVKAKLEQTLDELEDSLErEKKARGDI---EKNKRKVEGDLKLA-----QEAVADLEKNK-------KEMEQNLQRKE 1079
Cdd:pfam10174 315 LTNQNSDCKQHIEVLKESLT-AKEQRAAIlqtEVDALRLRLEEKESflnkkTKQLQDLTEEKstlageiRDLKDMLDVKE 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1080 KEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLAREIEELSERLEESGGATSSQIEL- 1158
Cdd:pfam10174 394 RKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESl 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1159 ---NKRREAELSKLRRDLEEsnlqHEQAMSNLRKKHNDTVAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSLLDHSNK 1235
Cdd:pfam10174 474 kkeNKDLKEKVSALQPELTE----KESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1236 AQANAE--KQVKQLEVQLA-------DAQFKVDEMNRTLNDLDGGK----KKLAVENSELQRQLEESESQVAQL----NK 1298
Cdd:pfam10174 550 VRTNPEinDRIRLLEQEVArykeesgKAQAEVERLLGILREVENEKndkdKKIAELESLTLRQMKEQNKKVANIkhgqQE 629
|
410 420
....*....|....*....|.
gi 556079866 1299 IKASLATQLEEAKRMADEEAR 1319
Cdd:pfam10174 630 MKKKGAQLLEEARRREDNLAD 650
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1064-1404 |
1.56e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.35 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1064 LEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLAREIEELSE 1143
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1144 RLEesggATSSQIELNKRREAELSKLRRDLEESNLQHEQAMSNLRKKHNDTVAEMSEQIDQLNKHKAKV---EKERATMS 1220
Cdd:pfam07888 116 EKD----ALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLqqtEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1221 AEVSDLQSLLDHSNKAQANAEKQVKQLEVQLADAQFKVDEMNRTLNDLDGGKKKLAVEN-------SEL----------Q 1283
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASErkveglgEELssmaaqrdrtQ 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1284 RQLEESESQVAQLNKIKASLATQLEEAKrmaDEEARERAAILgkyRNLEHDLDNLRESVEEEQEAKADFQRQLS-KANAE 1362
Cdd:pfam07888 272 AELHQARLQAAQLTLQLADASLALREGR---ARWAQERETLQ---QSAEADKDRIEKLSAELQRLEERLQEERMeREKLE 345
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 556079866 1363 AQLWRSKYESegLARLEELEEAKRKLHGKLQEAEEAMEQLNA 1404
Cdd:pfam07888 346 VELGREKDCN--RVQLSESRRELQELKASLRVAQKEKEQLQA 385
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1198-1371 |
1.57e-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: 42.60 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1198 MSEQIDQLNK------HKAKVEKERATMSAEVSDLQSLLDHSNKAQANAEKQVKQLEVQLADAQFKVDEMNRTLNDLDgg 1271
Cdd:COG1579 2 MPEDLRALLDlqeldsELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1272 KKKLAVENSE----LQRQLEESESQVAQLNKIKASLATQLEEAKRMADEEARERAAILGKYRNLEHDLDNLRESVEEEQE 1347
Cdd:COG1579 80 EQLGNVRNNKeyeaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
170 180
....*....|....*....|....
gi 556079866 1348 AKADfQRQLSKANAEAQLWRsKYE 1371
Cdd:COG1579 160 ELEA-EREELAAKIPPELLA-LYE 181
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1058-1624 |
1.58e-03 |
|
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: 43.58 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1058 QEAVADLEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIeeleeelEAERQARAKAEKqradlare 1137
Cdd:pfam05557 5 IESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRI-------RLLEKREAEAEE-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1138 ieelserleesggATSSQIELNKRREAELSKLRRDLEESNLQHEQAmsnlrkkhNDTVAEMSEQIDQLNKHKAKVEKERA 1217
Cdd:pfam05557 70 -------------ALREQAELNRLKKKYLEALNKKLNEKESQLADA--------REVISCLKNELSELRRQIQRAELELQ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1218 TMSAEVSDLQSLLDHSNKAQANAEKQVKQLEVQ---LADAQFKVDEMNRTLNDLDGGKKKLAVENSELQRqLEESESQVA 1294
Cdd:pfam05557 129 STNSELEELQERLDLLKAKASEAEQLRQNLEKQqssLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELAR-IPELEKELE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1295 QLNKIKASLATqLEEAKRMADEEAreraailgkyrnleHDLDNLRESVEEEQEAKADFQRQLSKANAEAQLWRSKYESEG 1374
Cdd:pfam05557 208 RLREHNKHLNE-NIENKLLLKEEV--------------EDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1375 L---------ARLEELEEAKRKLHGKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEVDKANALASSLEKRQKSFD 1445
Cdd:pfam05557 273 LnlrspedlsRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLT 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1446 KVIAEWKAKVDDLAAELDASqkecrNYSTevfKLRAAYEESQEHYESVKRENKNLQDEVKDLMDQLGEGGRSVHELEKSR 1525
Cdd:pfam05557 353 KERDGYRAILESYDKELTMS-----NYSP---QLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLEREL 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1526 KRLEMEKEELQAALEEAEAALEQEENKVLRAQlelsqvRQEIDRRIQEKEEEFE-----------NTRKNHQR---ALDS 1591
Cdd:pfam05557 425 QALRQQESLADPSYSKEEVDSLRRKLETLELE------RQRLREQKNELEMELErrclqgdydpkKTKVLHLSmnpAAEA 498
|
570 580 590
....*....|....*....|....*....|...
gi 556079866 1592 MQASLEAEAKGKAEALRLKKKLESDINELEIAL 1624
Cdd:pfam05557 499 YQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVL 531
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
951-1165 |
1.63e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.91 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 951 DMELALQKAEQDKATKDHQIRNLNDEIQHQDELINKLNKEKKHLQEASQKTSEDLQATEDKVNHLNKVKAKLEQTLDELE 1030
Cdd:TIGR02794 44 DPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1031 DSLEREKKArgdieKNKRKVEGDLKLAQEAVADLEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARI 1110
Cdd:TIGR02794 124 AKAKQAAEA-----KAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKA 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 556079866 1111 EELEEELEAERQARAKAEKQRADLAREIEELSERLEESGGATSSQIELNKRREAE 1165
Cdd:TIGR02794 199 EAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGAR 253
|
|
| zf-RING_UBOX |
pfam13445 |
RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases. |
2171-2207 |
1.63e-03 |
|
RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.
Pssm-ID: 463881 [Multi-domain] Cd Length: 38 Bit Score: 38.15 E-value: 1.63e-03
10 20 30
....*....|....*....|....*....|....*....
gi 556079866 2171 CPSCKVKRKDAVLiKCFHVFCYDCL--KTRYETRQRKCP 2207
Cdd:pfam13445 1 CPICLELFTDPVL-PCGHTFCRECLeeMSQKKGGKFKCP 38
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
929-1110 |
1.69e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 43.51 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 929 ASLSQSKKKLEGEISGLK---KDIEDMELALQKAEQDKATKDHQIRNLNDEIqhqDELINKLNKEKKHLQEASQKTS--E 1003
Cdd:pfam13166 286 NRLQKLIEKVESAISSLLaqlPAVSDLASLLSAFELDVEDIESEAEVLNSQL---DGLRRALEAKRKDPFKSIELDSvdA 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1004 DLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKargdieknkrkvegdlKLAQEAVADLEKNKKEMEQNLQRKEKEMA 1083
Cdd:pfam13166 363 KIESINDLVASINELIAKHNEITDNFEEEKNKAKK----------------KLRLHLVEEFKSEIDEYKDKYAGLEKAIN 426
|
170 180
....*....|....*....|....*..
gi 556079866 1084 SLAAKLEDEQALVAKLQKQIKELQARI 1110
Cdd:pfam13166 427 SLEKEIKNLEAEIKKLREEIKELEAQL 453
|
|
| RING-HC_ScRAD18-like |
cd23148 |
RING finger, HC subclass, found in Saccharomyces cerevisiae radiation sensitivity protein 18 ... |
2169-2213 |
1.73e-03 |
|
RING finger, HC subclass, found in Saccharomyces cerevisiae radiation sensitivity protein 18 (RAD18) and similar proteins; RAD18, also called RING-type E3 ubiquitin transferase RAD18, acts as a postreplication repair E3 ubiquitin-protein ligase that associates with the E2 ubiquitin conjugating enzyme UBC2/RAD6 to form the UBC2-RAD18 ubiquitin ligase complex involved in postreplicative repair (PRR) of damaged DNA. The UBC2-RAD18 complex cooperates with RAD5 and the UBC13-MMS2 dimer to attach mono-ubiquitin chains on 'Lys-164' of POL30, which is necessary for PRR. The UBC2-RAD18 complex is also involved in prevention of spontaneous mutations caused by 7,8-dihydro-8-oxoguanine. RAD18 is an E3 RING-finger protein belonging to the UBC2/RAD6 epistasis group. It contains a typical C3HC4-type RING-HC finger.
Pssm-ID: 438510 [Multi-domain] Cd Length: 52 Bit Score: 38.28 E-value: 1.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 556079866 2169 LTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYEtRQRKCPKCNAPF 2213
Cdd:cd23148 4 LRCHICKDLLKAPMRTPCNHTFCSFCIRTHLN-NDARCPLCKAEV 47
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
837-1231 |
1.90e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 837 AVRVEDELKAMEEKLKKTEEALAKEEKlrkeleehnvkvlqekndlflQLEAERMGAGDVEERLNKALTQKGDLESQLAD 916
Cdd:PRK02224 358 AEELREEAAELESELEEAREAVEDRRE---------------------EIEELEEEIEELRERFGDAPVDLGNAEDFLEE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 917 LndrlsheEDAHASLSQSKKKLEGEISGLKKDIEDMElALQKA------EQDKATKDHQirnlnDEIQHQDELINKLNKE 990
Cdd:PRK02224 417 L-------REERDELREREAELEATLRTARERVEEAE-ALLEAgkcpecGQPVEGSPHV-----ETIEEDRERVEELEAE 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 991 KKHLQEASQK------TSEDLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKRKVEGDLKLAQEAVADL 1064
Cdd:PRK02224 484 LEDLEEEVEEveerleRAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1065 EKNKKEMEQNLQRKEKEMASLA------AKLEDEQALVAKLQKQIKELQARieeleeeleaeRQARAKAEKQRADlarei 1138
Cdd:PRK02224 564 EEEAEEAREEVAELNSKLAELKerieslERIRTLLAAIADAEDEIERLREK-----------REALAELNDERRE----- 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1139 eelserleesggatssqiELNKRREaELSKLRRDLEESNLqhEQAMSNlRKKHNDTVAEMSEQIDQLNKHKAKVEKERAT 1218
Cdd:PRK02224 628 ------------------RLAEKRE-RKRELEAEFDEARI--EEARED-KERAEEYLEQVEEKLDELREERDDLQAEIGA 685
|
410
....*....|...
gi 556079866 1219 MSAEVSDLQSLLD 1231
Cdd:PRK02224 686 VENELEELEELRE 698
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
981-1081 |
2.08e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 981 DELINKLNKEKKHLQEASQKTSEDLQATEDKVNHLNKVKAKLEQTLDELEDSLERE-----KKARGDIEKNKRKVEGDLK 1055
Cdd:PRK00409 519 NELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEaqqaiKEAKKEADEIIKELRQLQK 598
|
90 100
....*....|....*....|....*...
gi 556079866 1056 LAQEAVA--DLEKNKKEMEQNLQRKEKE 1081
Cdd:PRK00409 599 GGYASVKahELIEARKRLNKANEKKEKK 626
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1378-1506 |
2.10e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 43.51 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1378 LEELEEAKRKLHGKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMsievDKANALA-----------SSLEKRQKSFDK 1446
Cdd:pfam05911 690 FEQLKSEKENLEVELASCTENLESTKSQLQESEQLIAELRSELASL----KESNSLAetqlkcmaesyEDLETRLTELEA 765
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556079866 1447 VIAEWKAKVDDLAAELdasQKECRNYStevfKLRAAYEESQEHYESV-KRENKNLQDEVKD 1506
Cdd:pfam05911 766 ELNELRQKFEALEVEL---EEEKNCHE----ELEAKCLELQEQLERNeKKESSNCDADQED 819
|
|
| RING-HC_RNF222 |
cd16564 |
RING finger, HC subclass, found in RING finger protein 222 (RNF222) and similar proteins; ... |
2170-2212 |
2.15e-03 |
|
RING finger, HC subclass, found in RING finger protein 222 (RNF222) and similar proteins; RNF222 is an uncharacterized C3HC4-type RING-HC finger-containing protein. It may function as an E3 ubiquitin-protein ligase.
Pssm-ID: 438226 [Multi-domain] Cd Length: 50 Bit Score: 38.15 E-value: 2.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 556079866 2170 TCPSCKVKRKDA-VLIKCFHVFCYDCLKTRYETRQRKCPKCNAP 2212
Cdd:cd16564 2 ECPVCYEDFDDApRILSCGHSFCEDCLVKQLVSMTISCPICRRV 45
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1873-2171 |
2.33e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1873 IRDLKAQLKKSQEAQRELKLLLDMYKGAPKEQRDkvqlMAAEKKARAEVEEHRQQLKKLAEHERKERRKLAdEDAMKKIR 1952
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLKKESE----LIKLKELAEQLKELEEKLKKYNLEELEKKAEEY-EKLKEKLI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1953 GLEETVASLHKSLTAqkqevwEEALLSEMEVTGQAFEDMQEQNLRLIQQLREKDDANFKLMSERIKS-NQIHKLLQEEKA 2031
Cdd:PRK03918 536 KLKGEIKSLKKELEK------LEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKElEPFYNEYLELKD 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 2032 MLSEqgatLQAQVEAQNQVVRKLEEKERLLQNSLSTLEKelsLRQQAAEMHRRKAVESAQSAADLKLHLEKYLAQLKDAQ 2111
Cdd:PRK03918 610 AEKE----LEREEKELKKLEEELDKAFEELAETEKRLEE---LRKELEELEKKYSEEEYEELREEYLELSRELAGLRAEL 682
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556079866 2112 GIVTDRTavlsQETFKT-KRLQEEILSLRRKVERAKKFELATNTDEVLMEEIKEYKEQLTC 2171
Cdd:PRK03918 683 EELEKRR----EEIKKTlEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKE 739
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
897-1294 |
2.33e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 897 EERLNKALTQKGDLESQLADLNDRLSHEEDAHaslSQSKKKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLNDe 976
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERY---KRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 977 iqhqdeLINKLNKEKKHLQEASQKTSEDLQATEDKVNHLNKVKAKLEQTLDELEDSLEREKKARGDIEKNKRKVEGDLKL 1056
Cdd:pfam07888 109 ------SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1057 AQEAVADLEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQRADLar 1136
Cdd:pfam07888 183 TEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEEL-- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1137 eieelserleesggatSSQIELNKRREAELSKLRRDLEESNLQHEQAMSNLRKKHNDTVAEMSEQIDQLNKHKAKVEKER 1216
Cdd:pfam07888 261 ----------------SSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1217 ATMSAEVSDLQSLLDHSNKAQANAEKQVKQLEVQLADAQFKVDEMNRTLNDLDGGKKKLAVENSELQ---RQLEESESQV 1293
Cdd:pfam07888 325 AELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLeyiRQLEQRLETV 404
|
.
gi 556079866 1294 A 1294
Cdd:pfam07888 405 A 405
|
|
| RING-HC_TRIM5-like_C-IV |
cd16591 |
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, ... |
2166-2213 |
2.41e-03 |
|
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, TRIM34 and similar proteins; TRIM5, TRIM6, TRIM22, and TRIM34, four closely related tripartite motif-containing proteins, belong to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. TRIM5, also known as RING finger protein 88 (RNF88), is a capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses in a species-specific manner by binding to and destabilizing the retroviral capsid lattice before reverse transcription is completed. Its retroviral restriction activity correlates with the ability to activate TAK1-dependent innate immune signaling. TRIM5 also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Moreover, TRIM5 plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. It also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction. TRIM6, also known as RING finger protein 89 (RNF89), is an E3-ubiquitin ligase that cooperates with the E2-ubiquitin conjugase UbE2K to catalyze the synthesis of unanchored K48-linked polyubiquitin chains, and further stimulates the interferon-I kappa B kinase epsilon (IKKepsilon) kinase-mediated antiviral response. It also regulates the transcriptional activity of Myc during the maintenance of embryonic stem (ES) cell pluripotency, and may act as a novel regulator for Myc-mediated transcription in ES cells. TRIM22, also known as 50 kDa-stimulated trans-acting factor (Staf-50) or RING finger protein 94 (RNF94), is an E3 ubiquitin-protein ligase that plays an integral role in the host innate immune response to viruses. It has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 acts as a suppressor of basal HIV-1 long terminal repeat (LTR)-driven transcription by preventing the transcription factor specificity protein 1 (Sp1) binding to the HIV-1 promoter. It also controls FoxO4 activity and cell survival by directing Toll-like receptor 3 (TLR3)-stimulated cells toward type I interferon (IFN) type I gene induction or apoptosis. Moreover, TRIM22 can activate the noncanonical nuclear factor-kappaB (NF-kappaB) pathway by activating I kappa B kinase alpha (IKKalpha). It also regulates nucleotide binding oligomerization domain containing 2 (NOD2)-dependent activation of interferon-beta signaling and nuclear factor-kappaB. TRIM34, also known as interferon-responsive finger protein 1 or RING finger protein 21 (RNF21), may function as antiviral protein that contribute to the defense against retroviral infections.
Pssm-ID: 438253 [Multi-domain] Cd Length: 72 Bit Score: 38.58 E-value: 2.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 556079866 2166 KEQLTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYETRQ-----RKCPKCNAPF 2213
Cdd:cd16591 4 KEEVTCPICLELLTEPLSLDCGHSFCQACITANHKESVnqegeSSCPVCRTSY 56
|
|
| RING-HC_AtBARD1-like |
cd23146 |
RING finger, HC subclass, found in Arabidopsis thaliana BRCA1-associated RING domain protein 1 ... |
2168-2217 |
2.45e-03 |
|
RING finger, HC subclass, found in Arabidopsis thaliana BRCA1-associated RING domain protein 1 (AtBARD1) and similar proteins; AtBARD1, also called protein REPRESSOR OF WUSCHEL 1, binds specifically to H3K4me3 regions of target gene (e.g. WUS and WOX5) promoters to repress their transcription via chromatin remodeling. It is required for the shoot apical meristem (SAM) organization and maintenance, by confining WUS expression to the organizing center, and for the quiescent center (QC) development in the root apical meristem (RAM), by repressing WOX5 expression in the root proximal meristem. AtBARD1 plays a role in DNA repair and in cell-cycle control. It is required for the repair of DNA double-strand breaks (DSBs), both natural and induced by genotoxic stress, by homologous recombination (HR). AtBARD1 contains a typical C3HC4-type RING-HC finger.
Pssm-ID: 438508 [Multi-domain] Cd Length: 54 Bit Score: 37.84 E-value: 2.45e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 556079866 2168 QLTCPSCKVKRKDAVLIKCFHVFCYDCLkTRYETRQRKCPKCNAPFGTND 2217
Cdd:cd23146 4 ELKCPICLKLLNRPVLLPCDHIFCSSCI-TDSTKVGSDCPVCKLPYHSQD 52
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
876-1047 |
2.48e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 876 LQEKNDLFLQLEAERMGAGDVEERLNKALTqkgDLESQLADLNDRLSHEEDAHASLSQSKKKLEGEISGLKK-------- 947
Cdd:PHA02562 215 IARKQNKYDELVEEAKTIKAEIEELTDELL---NLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptct 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 948 -DIEDMELALQKAEQDKATKDHQIRNLNDEIQHQDELINKLNKEKKHLQEASQKTSEDLQATEDKVNHLNKVKAKLEQT- 1025
Cdd:PHA02562 292 qQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELq 371
|
170 180 190
....*....|....*....|....*....|.
gi 556079866 1026 ---------LDELEDSLEREKKARGDIEKNK 1047
Cdd:PHA02562 372 aefvdnaeeLAKLQDELDKIVKTKSELVKEK 402
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1048-1353 |
2.55e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1048 RKVEGDLKLAQEAVADLEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKA 1127
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1128 EKQRADLAREIEELSERLEESGGATSSQIELNKRREAELSKLRRDLEESNLQHEQAMSNLRKKHNDTVAEMSEQIDQLNK 1207
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1208 HKAKVEKERATMSAEVSDLQSLLDHSNKAQA----NAEKQVKQLEVQLADAQFKVDEMNRTLNDLDGGKKKLAVENSELQ 1283
Cdd:COG4372 201 ELAEAEKLIESLPRELAEELLEAKDSLEAKLglalSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1284 RQLEESESQVAQLNKIKASLATQLEEAKRMADEEARERAAILGKYRNLEHDLDNLRESVEEEQEAKADFQ 1353
Cdd:COG4372 281 AALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
|
|
| RING-HC_RNF125 |
cd16542 |
RING finger, HC subclass, found in RING finger protein 125 (RNF125); RNF125, also known as ... |
2169-2211 |
2.57e-03 |
|
RING finger, HC subclass, found in RING finger protein 125 (RNF125); RNF125, also known as T-cell RING activation protein 1 (TRAC-1), is an E3 ubiquitin-protein ligase that is predominantly expressed in lymphoid cells, and functions as a positive regulator of T cell activation. It also down-modulates HIV replication and inhibits pathogen-induced cytokine production. It negatively regulates type I interferon signaling, which conjugates Lys(48)-linked ubiquitination to retinoic acid-inducible gene-I (RIG-I) and subsequently leads to the proteasome-dependent degradation of RIG-I. Further, RNF125 conjugates ubiquitin to melanoma differentiation-associated gene 5 (MDA5), a family protein of RIG-I. It thus acts as a negative regulator of RIG-I signaling, and is a direct target of miR-15b in the context of Japanese encephalitis virus (JEV) infection. Moreover, RNF125 binds to and ubiquitinates JAK1, prompting its degradation and inhibition of receptor tyrosine kinase (RTK) expression. It also negatively regulates p53 function through physical interaction and ubiquitin-mediated proteasome degradation. Mutations in RNF125 may lead to overgrowth syndromes (OGS). RNF125, together with three closely related proteins: RNF114, RNF138 and RNF166, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM). The UIM of RNF125 binds K48-linked poly-ubiquitin chains and is, together with the RING domain, required for auto-ubiquitination.
Pssm-ID: 438204 [Multi-domain] Cd Length: 50 Bit Score: 37.94 E-value: 2.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 556079866 2169 LTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYETRQRKCPKCNA 2211
Cdd:cd16542 2 FDCAVCLEVLHQPVRTRCGHVFCRPCIATSLRNNTWTCPYCRA 44
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1196-1344 |
2.59e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 42.36 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1196 AEMSEQIDQLNKHKAKVEKERATMSAEvSDLQSLLDHSNKAQANAEKQVKQL---EVQLADAQFKVDEMNRTLNDLDGGK 1272
Cdd:cd22656 94 AEILELIDDLADATDDEELEEAKKTIK-ALLDDLLKEAKKYQDKAAKVVDKLtdfENQTEKDQTALETLEKALKDLLTDE 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556079866 1273 kklavENSELQRQLEESESQVAQLNK-IKASLATQLEEAKR-MADEEARERAA--ILGKYRNLEHDLDNLRESVEE 1344
Cdd:cd22656 173 -----GGAIARKEIKDLQKELEKLNEeYAAKLKAKIDELKAlIADDEAKLAAAlrLIADLTAADTDLDNLLALIGP 243
|
|
| RING-HC_TRIM21_C-IV |
cd16596 |
RING finger, HC subclass, found in tripartite motif-containing protein TRIM21 and similar ... |
2167-2213 |
2.75e-03 |
|
RING finger, HC subclass, found in tripartite motif-containing protein TRIM21 and similar proteins; TRIM21, also known as 52 kDa Ro protein, 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Ro(SS-A), RING finger protein 81 (RNF81), or Sjoegren syndrome type A antigen (SS-A), is a ubiquitously expressed E3 ubiquitin-protein ligase and a high affinity antibody receptor uniquely expressed in the cytosol of mammalian cells. As a cytosolic Fc receptor, TRIM21 binds the Fc of virus-associated antibodies and targets the complex in the cytosol for proteasomal degradation in a process known as antibody-dependent intracellular neutralization (ADIN), and provides an intracellular immune response to protect host defense against pathogen infection. It shows remarkably broad isotype specificity as it does not only bind IgG, but also IgM and IgA. Moreover, TRIM21 promotes the cytosolic DNA sensor cGAS and the cytosolic RNA sensor RIG-I sensing of viral genomes during infection by antibody-opsonized virus. It stimulates inflammatory signaling and activates innate transcription factors, such as nuclear factor-kappaB (NF-kappaB). TRIM21 also plays an essential role in p62-regulated redox homeostasis, suggesting it may be a viable target for treating pathological conditions resulting from oxidative damage. Furthermore, TRIM21 may have implications for various autoimmune diseases associated with uncontrolled antiviral signaling through the regulation of Nmi-IFI35 complex-mediated inhibition of innate antiviral response. TRIM21 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.
Pssm-ID: 438258 [Multi-domain] Cd Length: 77 Bit Score: 38.73 E-value: 2.75e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 556079866 2167 EQLTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYETRQRKCPKCNAPF 2213
Cdd:cd16596 8 EEVTCPICLDPFVEPVSIECGHSFCQECISQVGKGGGSVCPVCRQRF 54
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1551-1734 |
2.78e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1551 NKVLRAQLELsqvrQEIDRRIQekeeEFENTRKNHQRALDSMQASLEAEAKGKAEALRLKKKLESDINELEIALDHANKA 1630
Cdd:COG1579 3 PEDLRALLDL----QELDSELD----RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1631 NAEAQ------KNLKKYQ------QNVKDLQGALEEEQRARDEAREQyasAERRCNAMHGELEESRQLLASSKNSHLRHI 1698
Cdd:COG1579 75 IKKYEeqlgnvRNNKEYEalqkeiESLKRRISDLEDEILELMERIEE---LEEELAELEAELAELEAELEEKKAELDEEL 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 556079866 1699 EQMEGEELLMQKKLRTEVIRLEDALVqvrKEYEMLR 1734
Cdd:COG1579 152 AELEAELEELEAEREELAAKIPPELL---ALYERIR 184
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1395-1636 |
2.83e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1395 AEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEVDKANALASSLEKRqksfdkvIAEWKAKVDDLAAELDASQKECRNYST 1474
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE-------LEALQAEIDKLQAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1475 EVFK-LRAAYEE-SQEHYESVKRENKNLQDEVK--DLMDQLGEGGRS-VHELEKSRKRLEMEKEELQAaleeaeaaleqE 1549
Cdd:COG3883 87 ELGErARALYRSgGSVSYLDVLLGSESFSDFLDrlSALSKIADADADlLEELKADKAELEAKKAELEA-----------K 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1550 ENKVLRAQLELSQVRQEIDRRIQEKEEEFENTRKNhQRALDSMQASLEAEAKGKAEALRLKKKLESDINELEIALDHANK 1629
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAE-EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
....*..
gi 556079866 1630 ANAEAQK 1636
Cdd:COG3883 235 AAAAAAA 241
|
|
| RING-HC_TRIM10_C-IV |
cd16593 |
RING finger, HC subclass, found in tripartite motif-containing protein 10 (TRIM10) and similar ... |
2167-2213 |
2.88e-03 |
|
RING finger, HC subclass, found in tripartite motif-containing protein 10 (TRIM10) and similar proteins; TRIM10, also known as B30-RING finger protein (RFB30), RING finger protein 9 (RNF9), or hematopoietic RING finger 1 (HERF1), is a novel hematopoiesis-specific RING finger protein required for terminal differentiation of erythroid cells. TRIM10 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.
Pssm-ID: 438255 [Multi-domain] Cd Length: 61 Bit Score: 37.97 E-value: 2.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 556079866 2167 EQLTCPSCKVKRKDAVLIKCFHVFCYDCLkTRY-------ETRQRKCPKCNAPF 2213
Cdd:cd16593 4 DEVNCPICQGTLREPVTIDCGHNFCRACL-TRYceipgpdLEEPPTCPLCKEPF 56
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1307-1457 |
2.89e-03 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 42.82 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1307 LEEAKRMADEEareraailgkyrnlEHDLDNLRESVEEEQEAKADFQRQLSKANAEAQLWRSKYESEgLARLEE-----L 1381
Cdd:COG1193 502 IERARELLGEE--------------SIDVEKLIEELERERRELEEEREEAERLREELEKLREELEEK-LEELEEekeeiL 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1382 EEAKRKLHGKL----QEAEEAMEQLNAKCSGLEKTKShLQGELEDMsievdkANALASSLEKRQKSFDKVIAEWKAKVDD 1457
Cdd:COG1193 567 EKAREEAEEILrearKEAEELIRELREAQAEEEELKE-ARKKLEEL------KQELEEKLEKPKKKAKPAKPPEELKVGD 639
|
|
| RING-HC_CHFR |
cd16503 |
RING finger, HC subclass, found in checkpoint with forkhead and RING finger domains protein ... |
2167-2212 |
2.90e-03 |
|
RING finger, HC subclass, found in checkpoint with forkhead and RING finger domains protein (CHFR); CHFR, also known as RING finger protein 196 (RNF196), is a checkpoint protein that delays entry into mitosis in response to stress. It functions as an E3 ubiquitin ligase that ubiquitinates and degrades its target proteins, such as Aurora-A, Plk1, Kif22, and PARP-1, which are critical for proper mitotic transitions. It also plays an important role in cell cycle progression and tumor suppression, and is negatively regulated by SUMOylation-mediated proteasomal ubiquitylation. Moreover, CHFR is involved in the early stage of the DNA damage response, which mediates the crosstalk between ubiquitination and poly-ADP-ribosylation. CHFR contains a fork head associated (FHA) domain and a C3HC4-type RING-HC finger.
Pssm-ID: 438166 [Multi-domain] Cd Length: 55 Bit Score: 37.73 E-value: 2.90e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 556079866 2167 EQLTCPSCKVKRKDAV-LIKCFHVFCYDCLKTRYETRQRKCPKCNAP 2212
Cdd:cd16503 1 ENLTCSICQDLLHDCVsLQPCMHNFCAACYSDWMERSNTECPTCRAT 47
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
878-1106 |
3.01e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.97 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 878 EKNdlFLQLEAERMGAgdvEERLNKALTQKGDLESQLADLNDRLShEEDAHASLSQSKK-----------------KLEG 940
Cdd:PLN02939 141 EKN--ILLLNQARLQA---LEDLEKILTEKEALQGKINILEMRLS-ETDARIKLAAQEKihveileeqleklrnelLIRG 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 941 EISGLKKDIEDMELALQKAEQDKATKDHQ-IRNLNDEIQHQDELINKLNKEKKHLQEASQKTSEDLQATEDKVNHLNKVK 1019
Cdd:PLN02939 215 ATEGLCVHSLSKELDVLKEENMLLKDDIQfLKAELIEVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQ 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1020 AK-LEQTLDELEDSLEREKK----------ARGDIEKNKRKVEGDL------KLAQEAVADLEKNKKEMEQNLQRKEKEM 1082
Cdd:PLN02939 295 YDcWWEKVENLQDLLDRATNqvekaalvldQNQDLRDKVDKLEASLkeanvsKFSSYKVELLQQKLKLLEERLQASDHEI 374
|
250 260
....*....|....*....|....
gi 556079866 1083 ASlaaKLEDEQALVAKLQKQIKEL 1106
Cdd:PLN02939 375 HS---YIQLYQESIKEFQDTLSKL 395
|
|
| RING-HC_TRIM8_C-V |
cd16580 |
RING finger, HC subclass, found in tripartite motif-containing protein 8 (TRIM8) and similar ... |
2165-2213 |
3.02e-03 |
|
RING finger, HC subclass, found in tripartite motif-containing protein 8 (TRIM8) and similar proteins; TRIM8, also known as glioblastoma-expressed RING finger protein (GERP) or RING finger protein 27 (RNF27), is a probable E3 ubiquitin-protein ligase that may promote proteasomal degradation of suppressor of cytokine signaling 1 (SOCS1) and further regulate interferon-gamma signaling. It functions as a new p53 modulator that stabilizes p53 impairing its association with MDM2 and inducing the reduction of cell proliferation. TRIM8 deficit dramatically impairs p53 stabilization and activation in response to chemotherapeutic drugs. TRIM8 also modulates tumor necrosis factor-alpha (TNFalpha) and interleukin-1beta (IL-1beta)-triggered nuclear factor-kappaB (NF- kappa B) activation by targeting transforming growth factor beta (TGFbeta) activated kinase 1 (TAK1) for K63-linked polyubiquitination. Moreover, TRIM8 modulates translocation of phosphorylated STAT3 into the nucleus through interaction with Hsp90beta and consequently regulates transcription of Nanog in embryonic stem cells. It also interacts with protein inhibitor of activated STAT3 (PIAS3), which inhibits IL-6-dependent activation of STAT3. TRIM8 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as an uncharacterized region positioned C-terminal to the RBCC domain. The coiled coil domain is required for homodimerization and the region immediately C-terminal to the RING motif is sufficient to mediate the interaction with SOCS1.
Pssm-ID: 438242 [Multi-domain] Cd Length: 67 Bit Score: 38.34 E-value: 3.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 556079866 2165 YKEQLTCPSCKVKRKDAVLIKCFHVFCYDCLKTRY--ETRQRKCPKCNAPF 2213
Cdd:cd16580 8 FEEELICPICLHVFVEPVQLPCKHNFCRGCIGEAWakDAGLVRCPECNQAY 58
|
|
| mRING-HC-C3HC3D_TRAF7 |
cd16644 |
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) ... |
2167-2207 |
3.03e-03 |
|
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) receptor-associated factor 7 (TRAF7) and similar proteins; TRAF7, also known as RING finger and WD repeat-containing protein 1 or RING finger protein 119 (RNF119), is an E3 ubiquitin-protein ligase involved in signal transduction pathways that lead either to activation or repression of NF-kappaB transcription factor by promoting K29-linked ubiquitination of several cellular targets, including the NF-kappaB essential modulator (NEMO) and the p65 subunit of NF-kappaB transcription factor. It is also involved in K29-linked polyubiquitination that has been implicated in lysosomal degradation of proteins. Moreover, TRAF7 is required for K48-linked ubiquitination of p53, a key tumor suppressor and a master regulator of various signaling pathways, such as those related to apoptosis, cell cycle and DNA repair. It is also required for tumor necrosis factor alpha (TNFalpha)-induced Jun N-terminal kinase activation and promotes cell death by regulating polyubiquitination and lysosomal degradation of c-FLIP protein. Furthermore, TRAF7 functions as small ubiquitin-like modifier (SUMO) E3 ligase involved in other post-translational modification, such as sumoylation. It binds to and stimulates sumoylation of the proto-oncogene product c-Myb, a transcription factor regulating proliferation and differentiation of hematopoietic cells. It potentiates MEKK3-induced AP1 and CHOP activation and induces apoptosis. Meanwhile, TRAF7 mediates MyoD1 regulation of the pathway and cell-cycle progression in myoblasts. It also plays a role in Toll-like receptors (TLR) signaling. TRAF7 contains an N-terminal domain with a modified C3HC3D-type RING-HC finger and an adjacent zinc finger, and a unique C-terminal domain that comprises a coiled coil domain and seven WD40 repeats.
Pssm-ID: 438306 [Multi-domain] Cd Length: 47 Bit Score: 37.33 E-value: 3.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 556079866 2167 EQLTCPSCKVKRKDAVLIKCFHVFCYDCLKTRyetRQRKCP 2207
Cdd:cd16644 4 VKLYCPLCQRVFKDPVITSCGHTFCRRCALTA---PGEKCP 41
|
|
| RING-HC_RNF113A_B |
cd16539 |
RING finger, HC subclass, found in RING finger proteins RNF113A, RNF113B, and similar proteins; ... |
2170-2212 |
3.07e-03 |
|
RING finger, HC subclass, found in RING finger proteins RNF113A, RNF113B, and similar proteins; RNF113A, also known as zinc finger protein 183 (ZNF183), is an E3 ubiquitin-protein ligase that physically interacts with the E2 protein, UBE2U. A nonsense mutation in RNF113A is associated with an X-linked trichothiodystrophy (TTD). Its yeast ortholog Cwc24p is predicted to have a spliceosome function and acts in a complex with Cef1p to participate in pre-U3 snoRNA splicing, indirectly affecting pre-rRNA processing. It is also important for the U2 snRNP binding to primary transcripts and co-migrates with spliceosomes. Moreover, the ortholog of RNF113A in fruit flies may also act as a spliceosome and is hypothesized to be involved in splicing, namely within the central nervous system. The ortholog in Caenorhabditis elegans is involved in DNA repair of inter-strand crosslinks. RNF113B, also known as zinc finger protein 183-like 1, shows high sequence similarity with RNF113A. Both RNF113A and RNF113B contain a CCCH-type zinc finger, which is commonly found in RNA-binding proteins involved in splicing, and a C3HC4-type RING-HC finger, which is frequently found in E3 ubiquitin ligases.
Pssm-ID: 438201 [Multi-domain] Cd Length: 54 Bit Score: 37.57 E-value: 3.07e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 556079866 2170 TCPSCKVKRKDAVLIKCFHVFCYDCLKTRYETRQrKCPKCNAP 2212
Cdd:cd16539 7 ACFICRKPFKNPVVTKCGHYFCEKCALKHYRKSK-KCFVCGKQ 48
|
|
| RING-HC_RING2 |
cd16740 |
RING finger, HC subclass, found in really interesting new gene 2 protein (RING2) and similar ... |
2163-2209 |
3.24e-03 |
|
RING finger, HC subclass, found in really interesting new gene 2 protein (RING2) and similar proteins; RING2, also known as huntingtin-interacting protein 2-interacting protein 3, HIP2-interacting protein 3, protein DinG, RING finger protein 1B (RING1B), RING finger protein 2 (RNF2), or RING finger protein BAP-1, is an E3 ubiquitin-protein ligase that interacts with both nucleosomal DNA and an acidic patch on histone H4 to achieve the specific monoubiquitination of K119 on histone H2A (H2AK119ub), thereby playing a central role in histone code and gene regulation. RING2 is a core component of polycomb repressive complex 1 (PRC1) that functions as an E3-ubuiquitin ligase transferring the mono-ubuiquitin mark to the C-terminal tail of Histone H2A at K118/K119. PRC1 is also capable of chromatin compaction, a function not requiring histone tails, and this activity appears important in gene silencing. The enzymatic activity of RING2 is enhanced by the interaction with BMI1/PCGF4, and it is dispensable for early embryonic development and much of the gene repression activity of PRC1. Moreover, RING2 plays a key role in terminating neural precursor cell (NPC)-mediated production of subcerebral projection neurons (SCPNs) during neocortical development. It also plays a critical role in nonhomologous end-joining (NHEJ)-mediated end-to-end chromosome fusions. Furthermore, RING2 is essential for expansion of hepatic stem/progenitor cells. It promotes hepatic stem/progenitor cell expansion through simultaneous suppression of cyclin-dependent kinase inhibitors (CDKIs) Cdkn1a and Cdkn2a, known negative regulators of cell proliferation. RING2 also negatively regulates p53 expression through directly binding with both p53 and MDM2 and promoting MDM2-mediated p53 ubiquitination in selective cancer cell types to stimulate tumor development. RING2 contains a C3HC4-type RING-HC finger.
Pssm-ID: 438398 [Multi-domain] Cd Length: 77 Bit Score: 38.53 E-value: 3.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 556079866 2163 KEYKEQLTCPSCKVKRKDAVLIK-CFHVFCYDCLKTRYETRQRKCPKC 2209
Cdd:cd16740 7 RSLHSELMCPICLDMLKNTMTTKeCLHRFCADCIITALRSGNKECPTC 54
|
|
| RING-HC_SH3RF2 |
cd16749 |
RING finger, HC subclass, found in SH3 domain-containing RING finger protein 2 (SH3RF2) and ... |
2169-2212 |
3.38e-03 |
|
RING finger, HC subclass, found in SH3 domain-containing RING finger protein 2 (SH3RF2) and similar proteins; SH3RF2, also known as heart protein phosphatase 1-binding protein (HEPP1), plenty of SH3s (POSH)-eliminating RING protein (POSHER), protein phosphatase 1 regulatory subunit 39, or RING finger protein 158 (RNF158), is a putative E3 ubiquitin-protein ligase that acts as an anti-apoptotic regulator for the c-Jun N-terminal kinase (JNK) pathway by binding to and promoting the proteasomal degradation of SH3RF1 (or POSH), a scaffold protein that is required for pro-apoptotic JNK activation. It may also play a role in cardiac functions together with protein phosphatase 1. SH3RF2 contains an N-terminal C3HC4-type RING-HC finger responsible for the E3 ligase activity and four Src Homology 3 (SH3) domains, which are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs.
Pssm-ID: 438407 [Multi-domain] Cd Length: 46 Bit Score: 37.22 E-value: 3.38e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 556079866 2169 LTCPSCKVKRK-DAVLIKCFHVFCYDCLKTRYETRQR-KCPKCNAP 2212
Cdd:cd16749 1 LECPVCFEKLDvTAKVLPCQHTFCKPCLQRIFKARKElRCPECRTP 46
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1046-1272 |
3.53e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.10 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1046 NKRKVEGDLKLAQEAVADLEKNKKEMEQNLQRKEKEmaSLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARA 1125
Cdd:PRK09510 74 AKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKE--RLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1126 KAeKQRADLAREIEELSERLEESGGATSSQIELNKRREAELSKlrrdleesnlqheQAMSNLRKKhndTVAEMSEQIDQL 1205
Cdd:PRK09510 152 EA-KRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAA-------------KAAAEAKKK---AEAEAKKKAAAE 214
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556079866 1206 NKHKAKVEKERATMSAEVsdlqslldhsnKAQANAEKQVKQLEVQLADAQFKVDEMNRTLNDLDGGK 1272
Cdd:PRK09510 215 AKKKAAAEAKAAAAKAAA-----------EAKAAAEKAAAAKAAEKAAAAKAAAEVDDLFGGLDSGK 270
|
|
| RING-HC_AtBRCA1-like |
cd23147 |
RING finger, HC subclass, found in Arabidopsis thaliana protein BREAST CANCER SUSCEPTIBILITY 1 ... |
2168-2220 |
3.61e-03 |
|
RING finger, HC subclass, found in Arabidopsis thaliana protein BREAST CANCER SUSCEPTIBILITY 1 homolog (AtBRCA1) and similar proteins; AtBRCA1 plays a role in DNA repair and in cell-cycle control. It is required for the repair of DNA double-strand breaks (DSBs), both natural and induced by genotoxic stress, by homologous recombination (HR). AtBRCA1 contains a typical C3HC4-type RING-HC finger.
Pssm-ID: 438509 [Multi-domain] Cd Length: 54 Bit Score: 37.45 E-value: 3.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 556079866 2168 QLTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYETRQrKCPKCNAPfgtndYHR 2220
Cdd:cd23147 4 ELKCPICLSLFKSAANLSCNHCFCAGCIGESLKLSA-ICPVCKIP-----ATR 50
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
839-1109 |
3.68e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.52 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 839 RVEDELKAMEEKLKKTEEALAKEEKLRKELEEHNVKVLQEKNDLFLQLEAERMGAGDVEERLNKALTQKGDLESQLADLN 918
Cdd:PRK04778 109 EIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEFSQFVELT 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 919 DRLSHEEdAHASLSQskkkLEGEISGLKKDIEDMELALQKAEQDKATkdhQIRNLNDEIQhqdELINK--------LNKE 990
Cdd:PRK04778 189 ESGDYVE-AREILDQ----LEEELAALEQIMEEIPELLKELQTELPD---QLQELKAGYR---ELVEEgyhldhldIEKE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 991 KKHLQEASQKTSEDLQATE-DKVNHLNKvkaKLEQTLDELEDSLEREKKARGDIEKNKRKVEGDLKLAQEAVADLEKNKK 1069
Cdd:PRK04778 258 IQDLKEQIDENLALLEELDlDEAEEKNE---EIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEID 334
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 556079866 1070 EMEQNLQRKEKEMASlaakledeqalVAKLQKQIKELQAR 1109
Cdd:PRK04778 335 RVKQSYTLNESELES-----------VRQLEKQLESLEKQ 363
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1556-1697 |
4.11e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1556 AQLELSQVRQEIDRRIQEKEEEFENTRKnhqraldsmqaslEAEAKGKAEALRLKKKLESDINELEIALDHANKANAEAQ 1635
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKKEAEAIKK-------------EALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKE 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556079866 1636 KNLKKYQQNVKDLQGALEEEQRARDEAREQYASAERRCNAMHGEL------------EESRQLLASSKNSHLRH 1697
Cdd:PRK12704 96 ENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQlqelerisgltaEEAKEILLEKVEEEARH 169
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1355-1665 |
4.19e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 42.20 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1355 QLSKANAEAQLWRSKYESEGLARLEELEEAKRKLHgklQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIEvdkANALA 1434
Cdd:pfam15964 357 QCEQLKSELERQKERLEKELASQQEKRAQEKEALR---KEMKKEREELGATMLALSQNVAQLEAQVEKVTRE---KNSLV 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1435 SSLEKRQKSF-------DKVIAEWKAKVDDLAAELDASQKECRNYST-----------EVFKLRAAYEESQEHYESVKRE 1496
Cdd:pfam15964 431 SQLEEAQKQLasqemdvTKVCGEMRYQLNQTKMKKDEAEKEHREYRTktgrqleikdqEIEKLGLELSESKQRLEQAQQD 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1497 NKNLQDEVKDLMDQLGEGGRSVHeleksRKRLEMEkeelqaaleeaeAALEQEENKVLRAQLELSQVRQEIDRRIQEKEE 1576
Cdd:pfam15964 511 AARAREECLKLTELLGESEHQLH-----LTRLEKE------------SIQQSFSNEAKAQALQAQQREQELTQKMQQMEA 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1577 EFENTrKNHQRALDSMQASLeaEAKGKAEALRLKKKLEsdinelEIALDHANKANAEAQKNlkkyqqnvKDLQGALEEEQ 1656
Cdd:pfam15964 574 QHDKT-VNEQYSLLTSQNTF--IAKLKEECCTLAKKLE------EITQKSRSEVEQLSQEK--------EYLQDRLEKLQ 636
|
....*....
gi 556079866 1657 RARDEAREQ 1665
Cdd:pfam15964 637 KRNEELEEQ 645
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1019-1110 |
4.75e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1019 KAKLEQTLDELEDSLEREKK-----ARGDIEKNKRKVEGDLKLAQEAVADLEKNKKEMEQNLQRKEKEMASLAAKLEDEQ 1093
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKealleAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKE 116
|
90
....*....|....*..
gi 556079866 1094 ALVAKLQKQIKELQARI 1110
Cdd:PRK12704 117 KELEQKQQELEKKEEEL 133
|
|
| RING-HC_PCGF6 |
cd16738 |
RING finger found in polycomb group RING finger protein 6 (PCGF6) and similar proteins; PCGF6, ... |
2162-2210 |
4.86e-03 |
|
RING finger found in polycomb group RING finger protein 6 (PCGF6) and similar proteins; PCGF6, also known as Mel18 and Bmi1-like RING finger (MBLR), or RING finger protein 134 (RNF134), is one of six PcG RING finger (PCGF) homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR). It serves as the core component of a noncanonical Polycomb repressive complex 1 (PRC1)-like L3MBTL2 complex, which is composed of some canonical components, such as RNF2, CBX3, CXB4, CXB6, CXB7, and CXB8, as well as some noncanonical components, such as L3MBTL2, E2F6, WDR5, HDAC1, and RYBP, and plays a critical role in epigenetic transcriptional silencing in higher eukaryotes. Like other PCGF homologs, PCGF6 possesses the transcriptional repression activity, and also associates with ring finger protein 2 (RNF2) to form a RNF2-PCGF heterodimer, which is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. Moreover, PCGF6 can regulate the enzymatic activity of JARID1d/KDM5D, a trimethyl H3K4 demethylase, through direct interaction. Furthermore, PCGF6 is expressed predominantly in meiotic and post-meiotic male germ cells and may play important roles in mammalian male germ cell development. It also regulates mesodermal lineage differentiation in mammalian embryonic stem cells (ESCs) and functions in induced pluripotent stem (iPS) reprogramming. The activity of PCGF6 is found to be regulated by cell cycle dependent phosphorylation. PCGF6 contains a C3HC4-type RING-HC finger.
Pssm-ID: 438396 [Multi-domain] Cd Length: 59 Bit Score: 37.20 E-value: 4.86e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 556079866 2162 IKEYKEQLTCPSCKVKRKDAVLI-KCFHVFCYDCLKTRYETRQRkCPKCN 2210
Cdd:cd16738 1 LAELNPYILCSICKGYFIDATTItECLHTFCKSCIVRHFYYSNR-CPKCN 49
|
|
| RING-HC_DTX3-like |
cd16506 |
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3), Deltex-3-like ... |
2170-2210 |
5.32e-03 |
|
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3), Deltex-3-like (DTX3L) and similar proteins; This subfamily contains Deltex3 (DTX3) and Deltex-3-like (DTX3L), both of which are E3 ubiquitin-protein ligases belonging to the Deltex (DTX) family. DTX3, also known as RING finger protein 154 (RNF154), has a biological function that remains unclear. DTX3L, also known as B-lymphoma- and BAL-associated protein (BBAP) or Rhysin-2 (Rhysin2), regulates endosomal sorting of the G protein-coupled receptor CXCR4 from endosomes to lysosomes. It also regulates subcellular localization of its partner protein, B aggressive lymphoma (BAL), by a dynamic nucleocytoplasmic trafficking mechanism. In contrast to other DTXs, both DTX3 and DTX3L contain a C3HC4-type RING-HC finger, and a previously unidentified C-terminal domain. DTX3L can associate with DTX1 through its unique N termini and further enhance self-ubiquitination.
Pssm-ID: 438169 [Multi-domain] Cd Length: 45 Bit Score: 36.57 E-value: 5.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 556079866 2170 TCPSC--KVKRKDaVLIKCFHVFCYDCLKTRYETRQrKCPKCN 2210
Cdd:cd16506 2 TCPICldEIQNKK-TLEKCKHSFCEDCIDRALQVKP-VCPVCG 42
|
|
| BRE1 |
pfam08647 |
BRE1 E3 ubiquitin ligase; BRE1 is an E3 ubiquitin ligase that has been shown to act as a ... |
1977-2071 |
5.37e-03 |
|
BRE1 E3 ubiquitin ligase; BRE1 is an E3 ubiquitin ligase that has been shown to act as a transcriptional activator through direct activator interactions.
Pssm-ID: 462547 [Multi-domain] Cd Length: 95 Bit Score: 38.33 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1977 LLSEMEVTGQAFEDMQEQNLRLIQQLREKDDANFKLMSERIKSNQIHKLLQEEKAMLSEQGATLQAQVEAQNQVVRKLEE 2056
Cdd:pfam08647 1 LQTELVKLEQAFEELSEQLDKKVKDLTILEEKKLRLEAEKAKADQKYFAAMRSKDALENENKKLNTLLSKSSELIEQLKE 80
|
90
....*....|....*
gi 556079866 2057 KERLLQNSLSTLEKE 2071
Cdd:pfam08647 81 TEKEFVRKLKNLEKE 95
|
|
| RING-HC_PCGF1 |
cd16733 |
RING finger, HC subclass, found in polycomb group RING finger protein 1 (PCGF1) and similar ... |
2162-2210 |
5.55e-03 |
|
RING finger, HC subclass, found in polycomb group RING finger protein 1 (PCGF1) and similar proteins; PCGF1, also known as nervous system Polycomb-1 (NSPc1) or RING finger protein 68 (RNF68), is one of six PcG RING finger (PCGF) homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR). It serves as the core component of a noncanonical Polycomb repressive complex 1 (PRC1)-like BCOR complex that also contains RING1, RNF2, RYBP, SKP1, as well as the BCL6 co-repressor BCOR and the histone demethylase KDM2B, and is required to maintain the transcriptionally repressive state of some genes, such as Hox genes, BCL6 and the cyclin-dependent kinase inhibitor, CDKN1A. PCGF1 promotes cell cycle progression and enhances cell proliferation as well. It is a cell growth regulator that acts as a transcriptional repressor of p21Waf1/Cip1 via the retinoid acid response element (RARE element). Moreover, PCGF1 functions as an epigenetic regulator involved in hematopoietic cell differentiation. It cooperates with the transcription factor runt-related transcription factor 1 (Runx1) in regulating differentiation and self-renewal of hematopoietic cells. Furthermore, PCGF1 represents a physical and functional link between Polycomb function and pluripotency. PCGF1 contains a C3HC4-type RING-HC finger.
Pssm-ID: 438391 [Multi-domain] Cd Length: 71 Bit Score: 37.63 E-value: 5.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 556079866 2162 IKEYKEQLTCPSCKVKRKDAVLI-KCFHVFCYDCLkTRYETRQRKCPKCN 2210
Cdd:cd16733 3 IKDLNEHIVCYLCAGYFIDATTItECLHTFCKSCI-VKYLQTSKYCPMCN 51
|
|
| mRING-HC-C4C4_TRIM37_C-VIII |
cd16619 |
Modified RING finger, HC subclass (C4C4-type), found in tripartite motif-containing protein 37 ... |
2169-2209 |
5.62e-03 |
|
Modified RING finger, HC subclass (C4C4-type), found in tripartite motif-containing protein 37 (TRIM37) and similar proteins; TRIM37, also known as mulibrey nanism protein, or MUL, is a peroxisomal E3 ubiquitin-protein ligase that is involved in the tumorigenesis of several cancer types, including pancreatic ductal adenocarcinoma (PDAC), hepatocellular carcinoma (HCC), breast cancer, and sporadic fibrothecoma. It mono-ubiquitinates histone H2A, a chromatin modification associated with transcriptional repression. Moreover, TRIM37 possesses anti-HIV-1 activity, and interferes with viral DNA synthesis. Mutations in the human TRIM37 gene (also known as MUL) cause Mulibrey (muscle-liver-brain-eye) nanism, a rare growth disorder of prenatal onset characterized by dysmorphic features, pericardial constriction, and hepatomegaly. TRIM37 belongs to the C-VIII subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C4C4-type RING finger, whose overall folding is similar to that of the typical C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a MATH (meprin and TRAF-C homology) domain positioned C-terminal to the RBCC domain. Its MATH domain has been shown to interact with the TRAF (TNF-Receptor-Associated Factor) domain of six known TRAFs in vitro.
Pssm-ID: 438281 [Multi-domain] Cd Length: 43 Bit Score: 36.57 E-value: 5.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 556079866 2169 LTCPSCKVKRKDAVL-IKCFHVFCYDCLKTRYETRQRKCPKC 2209
Cdd:cd16619 1 FRCFICMEKLRDPRLcPHCSKLFCKGCIRRWLSEQRSSCPHC 42
|
|
| mRING-HC-C3HC3D_LNX1-like |
cd16637 |
Modified RING finger, HC subclass (C3HC3D-type), found in ligand of Numb protein LNX1, LNX2, ... |
2169-2207 |
6.07e-03 |
|
Modified RING finger, HC subclass (C3HC3D-type), found in ligand of Numb protein LNX1, LNX2, and similar proteins; The ligand of Numb protein X (LNX) family, also known as PDZ and RING (PDZRN) family, includes LNX1-5, which can interact with Numb, a key regulator of neurogenesis and neuronal differentiation. LNX5 (also known as PDZK4 or PDZRN4L) shows high sequence homology to LNX3 and LNX4, but it lacks the RING domain. LNX1-4 proteins function as E3 ubiquitin ligases and have a unique domain architecture consisting of an N-terminal RING-HC finger for E3 ubiquitin ligase activity and either two or four PDZ domains necessary for substrate-binding. LNX1/LNX2-like proteins contain a modified C3HC3D-type RING-HC finger and four PDZ domains. This model corresponds to the RING finger.
Pssm-ID: 438299 [Multi-domain] Cd Length: 42 Bit Score: 36.61 E-value: 6.07e-03
10 20 30
....*....|....*....|....*....|....*....
gi 556079866 2169 LTCPSCKVKRKDAVLIKCFHVFCYDCLKTrYETRQRKCP 2207
Cdd:cd16637 2 LTCHICLQPLVEPLDTPCGHTFCYKCLTN-YLKIQQCCP 39
|
|
| mRING-HC-C3HC3D_TRAF6 |
cd16643 |
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) ... |
2171-2217 |
6.38e-03 |
|
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) receptor-associated factor 6 (TRAF6) and similar proteins; TRAF6, also known as interleukin-1 signal transducer or RING finger protein 85 (RNF85), is a cytoplasmic adapter protein that mediates signals induced by the tumor necrosis factor receptor (TNFR) superfamily and Toll-like receptor (TLR)/interleukin-1 receptor (IL-1R) family. It functions as a mediator involved in the activation of mitogen-activated protein kinase (MAPK), phosphoinositide 3-kinase (PI3K), and interferon regulatory factor pathways, as well as in IL-1R-mediated activation of NF-kappaB. TRAF6 is also an oncogene that plays a vital role in K-RAS-mediated oncogenesis. TRAF6 contains an N-terminal domain with a modified C3HC3D-type RING-HC finger and several zinc fingers, and a C-terminal TRAF domain that comprises a coiled coil domain and a conserved TRAF-C domain.
Pssm-ID: 438305 [Multi-domain] Cd Length: 58 Bit Score: 36.97 E-value: 6.38e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 556079866 2171 CPSCKVKRKDAVLIKCFHVFCYDC-LKTRYETRQRkCPKCNAPFGTND 2217
Cdd:cd16643 4 CPICLMALREPVQTPCGHRFCKACiLKSIREAGHK-CPVDNEPLLENQ 50
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
835-1394 |
6.63e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 41.66 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 835 LSAVRVEDELKAMEEKLKKTEE-----ALAKEEKLRKELEEHNVKVLQEKNDLFLQLEAERMGAGdvEERLNKALTQKGD 909
Cdd:pfam07111 96 LEAQAMELDALAVAEKAGQAEAeglraALAGAEMVRKNLEEGSQRELEEIQRLHQEQLSSLTQAH--EEALSSLTSKAEG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 910 LESQLADLNDRLSHEEDAHASLSQSKKKLEGEISglkKDIEDMELALQKAEQDKATKDHQIRNlndEIQHQDELI--NKL 987
Cdd:pfam07111 174 LEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLS---KTQEELEAQVTLVESLRKYVGEQVPP---EVHSQTWELerQEL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 988 NKEKKHLQEasqkTSEDLQATED----KVNHLNKVKAKLEQTLD---ELEDSLERE--KKARGDIEKNKRKV-------- 1050
Cdd:pfam07111 248 LDTMQHLQE----DRADLQATVEllqvRVQSLTHMLALQEEELTrkiQPSDSLEPEfpKKCRSLLNRWREKVfalmvqlk 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1051 EGDLKlAQEAVADLEKNKKEMEQNLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAERQARAKAEKQ 1130
Cdd:pfam07111 324 AQDLE-HRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQ 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1131 R----ADLAREIEELSERLEESGGATSSQIELNKRREAELSKLR-------RDLEESNLQHEQamSNLRKKHNDTVAEMS 1199
Cdd:pfam07111 403 LkfvvNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHtikglmaRKVALAQLRQES--CPPPPPAPPVDADLS 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1200 EQIDQLNKHKAKVEKErATMSAEVsdLQSLLDHSnKAQANAEKQ-----VKQLEVQLADAQFKVDEMNRTLNDLDGGKKK 1274
Cdd:pfam07111 481 LELEQLREERNRLDAE-LQLSAHL--IQQEVGRA-REQGEAERQqlsevAQQLEQELQRAQESLASVGQQLEVARQGQQE 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1275 LAVENSELQRQLEESESQVAQ-----LNKIKASLATQLEEAKRMADEEARERAAILGKYRNLEHdldnlRESVEEEQeak 1349
Cdd:pfam07111 557 STEEAASLRQELTQQQEIYGQalqekVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQH-----RATQEKER--- 628
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 556079866 1350 adfQRQLSKANAEAQlwrsKYESEGLA-RLEELEEAKRKLHGKLQE 1394
Cdd:pfam07111 629 ---NQELRRLQDEAR----KEEGQRLArRVQELERDKNLMLATLQQ 667
|
|
| RING-HC_AtRMA-like |
cd16745 |
RING finger, HC subclass, found in Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) ... |
2171-2211 |
6.65e-03 |
|
RING finger, HC subclass, found in Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) and similar proteins; AtRMAs, including AtRma1, AtRma2, and AtRma3, are endoplasmic reticulum (ER)-localized Arabidopsis homologs of human outer membrane of the ER-anchor E3 ubiquitin-protein ligase, RING finger protein 5 (RNF5). AtRMAs possess E3 ubiquitin ligase activity, and may play a role in the growth and development of Arabidopsis. The AtRMA1 and AtRMA3 genes are predominantly expressed in major tissues, such as cotyledons, leaves, shoot-root junction, roots, and anthers, while AtRMA2 expression is restricted to the root tips and leaf hydathodes. AtRma1 probably functions with the Ubc4/5 subfamily of E2. AtRma2 is likely involved in the cellular regulation of ABP1 expression levels through interacting with auxin binding protein 1 (ABP1). AtRMA proteins contain an N-terminal C3HC4-type RING-HC finger and a trans-membrane-anchoring domain in their extreme C-terminal region.
Pssm-ID: 438403 [Multi-domain] Cd Length: 45 Bit Score: 36.31 E-value: 6.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 556079866 2171 CPSCKVKRKDAVLIKCFHVFCYDCLK--TRYETRQRKCPKCNA 2211
Cdd:cd16745 3 CNICLDLAQDPVVTLCGHLFCWPCLHkwLRRQSSQPECPVCKA 45
|
|
| RING-HC_RNF114 |
cd16540 |
RING finger, HC subclass, found in RING finger protein 114 (RNF114) and similar proteins; ... |
2169-2212 |
6.69e-03 |
|
RING finger, HC subclass, found in RING finger protein 114 (RNF114) and similar proteins; RNF114, also known as zinc finger protein 228 (ZNF228) or zinc finger protein 313 (ZNF313), is a p21(WAF1)-targeting ubiquitin E3 ligase that interacts with X-linked inhibitor of apoptosis (XIAP)-associated factor 1 (XAF1) and may play a role in p53-mediated cell-fate decisions. It is involved in the immune response to double-stranded RNA in disease pathogenesis. Moreover, RNF114 interacts with A20 and modulates its ubiquitylation. It negatively regulates nuclear factor-kappaB (NF-kappaB)-dependent transcription and positively regulates T-cell activation. RNF114 may play a putative role in the regulation of immune responses, since it corresponds to a novel psoriasis susceptibility gene, ZNF313. RNF114, together with three closely related proteins: RNF125, RNF138 and RNF166, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM).
Pssm-ID: 438202 [Multi-domain] Cd Length: 46 Bit Score: 36.66 E-value: 6.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 556079866 2169 LTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYETRQRKCPKCNAP 2212
Cdd:cd16540 2 FTCPVCLEIFETPVRVPCGHVFCNACLQECLKPKKPVCAVCRSP 45
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
942-1110 |
6.78e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 40.27 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 942 ISGLKKDIEDMELALQKAEQDKATKDHQIRNLNDEIQHQDELINKLNKEKKHlqeaSQKTSEDLQATEDKVNHLNKVKAK 1021
Cdd:pfam13851 28 IKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLEN----YEKDKQSLKNLKARLKVLEKELKD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1022 LEQTLDELEDSLEREKKARGDIeknKRKVEGDLKLAQEAVAD----LEKNKKEMEQNLQRKEKEMASL--AAKLEDE--Q 1093
Cdd:pfam13851 104 LKWEHEVLEQRFEKVERERDEL---YDKFEAAIQDVQQKTGLknllLEKKLQALGETLEKKEAQLNEVlaAANLDPDalQ 180
|
170
....*....|....*..
gi 556079866 1094 ALVAKLQKQIKELQARI 1110
Cdd:pfam13851 181 AVTEKLEDVLESKNQLI 197
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
900-1154 |
6.99e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 41.74 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 900 LNKALTQkgDLESQLAdLNDRLSHEEDAHaSLSQSKKKLEGEISGLKKDIEDME-LALQKAEQD-KATKDHQIRNLNDEI 977
Cdd:NF012221 1547 VSKHAKQ--DDAAQNA-LADKERAEADRQ-RLEQEKQQQLAAISGSQSQLESTDqNALETNGQAqRDAILEESRAVTKEL 1622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 978 QHQDELINKLNKEKKHLQEASQKTSEDLqatedKVNHLNKVKAKLEQTldeledslerEKKARGDIEKNKRKVEGDLKLA 1057
Cdd:NF012221 1623 TTLAQGLDALDSQATYAGESGDQWRNPF-----AGGLLDRVQEQLDDA----------KKISGKQLADAKQRHVDNQQKV 1687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1058 QEAVADLEKNKKEMEQNLQRKEK--EMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELEAER---QARAKAEKQRA 1132
Cdd:NF012221 1688 KDAVAKSEAGVAQGEQNQANAEQdiDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQdasAAENKANQAQA 1767
|
250 260
....*....|....*....|..
gi 556079866 1133 DlAREIEELSERLEESGGATSS 1154
Cdd:NF012221 1768 D-AKGAKQDESDKPNRQGAAGS 1788
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1909-2134 |
7.09e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1909 QLMAAEKKARAEVEEHRQQLKKLAEHERKE---RRKLADedAMKKIRGLEETVASLHKSLTAQKQEVWEEALLSEMEvtg 1985
Cdd:PRK11281 53 LLEAEDKLVQQDLEQTLALLDKIDRQKEETeqlKQQLAQ--APAKLRQAQAELEALKDDNDEETRETLSTLSLRQLE--- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1986 qafeDMQEQNLRLIQQLREK-DDANFKLMS-----ERIKS-------------NQIHKLLQEEKAMLSEQGATLQAQ--- 2043
Cdd:PRK11281 128 ----SRLAQTLDQLQNAQNDlAEYNSQLVSlqtqpERAQAalyansqrlqqirNLLKGGKVGGKALRPSQRVLLQAEqal 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 2044 VEAQNQVVRKLEEKERLLQNSLSTLEKELSLRQQaaemhrrkavesaqsaadlklHLEKYLAQLkdaQGIVTDRTAVLSQ 2123
Cdd:PRK11281 204 LNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQ---------------------RLEHQLQLL---QEAINSKRLTLSE 259
|
250
....*....|.
gi 556079866 2124 ETFKTKRLQEE 2134
Cdd:PRK11281 260 KTVQEAQSQDE 270
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1202-1417 |
7.32e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1202 IDQLNKHKAKVEKERATMSAEVSDLQSLLDHSNKAQANAEKQVKQLEVQLADAQFKVDEMNRTLNDLDGGKKKLAVENSE 1281
Cdd:PHA02562 194 QQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQ 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1282 LQRQLEESESqvaqlNKIKASLATQLEEAKRMADEeareraaILGKYRNLEHDLDNLRESVEEEQEAKADFQRQLSKANA 1361
Cdd:PHA02562 274 FQKVIKMYEK-----GGVCPTCTQQISEGPDRITK-------IKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLE 341
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556079866 1362 eaqlWRSKYESEGLARLEELEEAKR--KLHGKLQEA----EEAMEQLNA-------KCSGLEKTKSHLQ 1417
Cdd:PHA02562 342 ----LKNKISTNKQSLITLVDKAKKvkAAIEELQAEfvdnAEELAKLQDeldkivkTKSELVKEKYHRG 406
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1880-2169 |
7.41e-03 |
|
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: 41.57 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1880 LKKSQEAQRELKLLLDMYKGAPKEQRDKVQLMAAEKKARAEV---EEHRQQLKKLAEHERKERRKlADEDAMKKIRGLEE 1956
Cdd:TIGR00606 687 FQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglAPGRQSIIDLKEKEIPELRN-KLQKVNRDIQRLKN 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1957 TVASLHKSL-TAQKQEVWEEALLSEMEVTGQAFEDMQEQNLRLIQQLREKDDANFKLMSERIKSNQIHKllQEEKAMLSE 2035
Cdd:TIGR00606 766 DIEEQETLLgTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEK--QHELDTVVS 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 2036 QGATLQAQVEAQNQVVRKLEEKERLLQNSLSTLEKELSLRQQAAEMHRRKAVEsaqsaadlklhLEKYLAQLKDAqgivt 2115
Cdd:TIGR00606 844 KIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTE-----------VQSLIREIKDA----- 907
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 556079866 2116 dRTAVLSQETFKTKRLQEEILSLRRKVERAKKFELATNTDEVLMEEIKEYKEQL 2169
Cdd:TIGR00606 908 -KEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDI 960
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1151-1692 |
7.72e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.74 E-value: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1151 ATSSQIELNKRREAELSklrRDLEESNLQHEQAMSNLRKKHNDTVAEMSEQ-IDQLNKHKAKVEKERATMSAEVSDLqsl 1229
Cdd:NF041483 244 STAAESDQARRQAAELS---RAAEQRMQEAEEALREARAEAEKVVAEAKEAaAKQLASAESANEQRTRTAKEEIARL--- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1230 ldhSNKAQANAEKQVKQLEVQLADAQFKVDemnrtlndldggkkKLAVENSELQRQLEESESqvaqlnkikaslATQLEE 1309
Cdd:NF041483 318 ---VGEATKEAEALKAEAEQALADARAEAE--------------KLVAEAAEKARTVAAEDT------------AAQLAK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1310 AKRMADEeareraaILGKyrnlehdldnlresveeeqeAKADFQRQLSKANAEAQLWRSKYESEGLARLEELEEAKRKLH 1389
Cdd:NF041483 369 AARTAEE-------VLTK--------------------ASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQLK 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1390 GklqEAEEAMEQLNAKCSGLEKTKSHLQGELEDMSIE-VDKANAL--------ASSLEKRQKSFDKVIAEWKAKVDDLAA 1460
Cdd:NF041483 422 G---AAKDDTKEYRAKTVELQEEARRLRGEAEQLRAEaVAEGERIrgearreaVQQIEEAARTAEELLTKAKADADELRS 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1461 ELDASQKECRNYSTE-VFKLRAAYEESQEHyesVKRENKNLQDEVkdlmDQLGEGGRSVHELEKSRKRLEMEKEELQAAL 1539
Cdd:NF041483 499 TATAESERVRTEAIErATTLRRQAEETLER---TRAEAERLRAEA----EEQAEEVRAAAERAARELREETERAIAARQA 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1540 EEAEAAL---EQEENKVLRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEA---------------- 1600
Cdd:NF041483 572 EAAEELTrlhTEAEERLTAAEEALADARAEAERIRREAAEETERLRTEAAERIRTLQAQAEQEAerlrteaaadasaara 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1601 KGKAEALRLKKKLESDINELEI-ALDHANKANAEAQKNLKKY-QQNVKDLQGALEEEQRARDEAREQYASAERRCNAMHG 1678
Cdd:NF041483 652 EGENVAVRLRSEAAAEAERLKSeAQESADRVRAEAAAAAERVgTEAAEALAAAQEEAARRRREAEETLGSARAEADQERE 731
|
570
....*....|....*
gi 556079866 1679 EL-EESRQLLASSKN 1692
Cdd:NF041483 732 RArEQSEELLASARK 746
|
|
| zf-4CXXC_R1 |
pfam10497 |
Zinc-finger domain of monoamine-oxidase A repressor R1; R1 is a transcription factor repressor ... |
2170-2209 |
7.77e-03 |
|
Zinc-finger domain of monoamine-oxidase A repressor R1; R1 is a transcription factor repressor that inhibits monoamine oxidase A gene expression. This domain is a four-CXXC zinc finger putative DNA-binding domain found at the C-terminal end of R1. The domain carries 12 cysteines of which four pairs are of the CXXC type.
Pssm-ID: 463117 Cd Length: 99 Bit Score: 38.01 E-value: 7.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 556079866 2170 TCPSCKVKRKDAV----LIKCFHV---FCYDCLKTRY-----ETRQRK---CPKC 2209
Cdd:pfam10497 8 TCHQCRQKTLDTKtscrNSQCKGVrgqFCGDCLRNRYgenveEALANPdwiCPKC 62
|
|
| COG5391 |
COG5391 |
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ... |
1153-1470 |
7.77e-03 |
|
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];
Pssm-ID: 227680 [Multi-domain] Cd Length: 524 Bit Score: 41.32 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1153 SSQIELNKRREAELSKLRRDLEESNLQHEQAMSNLRKKHNDTVAEMSEQIDQLNKHKAKVEKeraTMSAEVSDLQSLLDH 1232
Cdd:COG5391 215 FSDEFIEERRQSLQNFLRRVSTHPLLSNYKNSKSWESHSTLLSSFIENRKSVPTPLSLDLTS---TTQELDMERKELNES 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1233 SNKAQANAEKQVKQLE---VQLADAQFKVDEMNRTLNDLDggKKKLAVENSELQRQLEESESQVAQLNKIKASLATQLEE 1309
Cdd:COG5391 292 TSKAIHNILSIFSLFEkilIQLESEEESLTRLLESLNNLL--LLVLNFSGVFAKRLEQNQNSILNEGVVQAETLRSSLKE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1310 AKRMADEEARERAAILGKYRNLEHDLDNLRESVEEEQEAKADFQRQLSKanaeaQLWRSKyESEGLARLEeleeakRKLH 1389
Cdd:COG5391 370 LLTQLQDEIKSRESLILTDSNLEKLTDQNLEDVEELSRSLRKNSSQRAV-----VSQQPE-GLTSFSKLS------YKLR 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1390 GKLQEAeeamEQLNAKCSgLEKTKSHLQGELEDMSIEVDKANalaSSLEKRQKSFDKVI-AEWKAKVDDLAAELDASQKE 1468
Cdd:COG5391 438 DFVQEK----SRSKSIES-LQQDKEKLEEQLAIAEKDAQEIN---EELKNELKFFFSVRnSDLEKILKSVADSHIEWAEE 509
|
..
gi 556079866 1469 CR 1470
Cdd:COG5391 510 NL 511
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
895-1319 |
7.78e-03 |
|
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: 41.21 E-value: 7.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 895 DVEERLNKALTQKGDLESQLADLNDRLSHEEDAHASLSQSKKKLegeiSGLKKDIEDMELALQKAEQdkATKDHQIRnln 974
Cdd:pfam05622 18 ELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKY----LLLQKQLEQLQEENFRLET--ARDDYRIK--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 975 deiqhqdelINKLNKEKKHLQEasqkTSEDLQATEDKVNHLnkvkaKLEqtLDELEDSLEREKKARGDIEKNKRKVE--G 1052
Cdd:pfam05622 89 ---------CEELEKEVLELQH----RNEELTSLAEEAQAL-----KDE--MDILRESSDKVKKLEATVETYKKKLEdlG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1053 DL----KLAQEAVADLEKNKKEMEQNLQRK----------EKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELE 1118
Cdd:pfam05622 149 DLrrqvKLLEERNAEYMQRTLQLEEELKKAnalrgqletyKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1119 AERQARaKAEKQRADLAREIEELSERLEESGGATSSQIELNKRREAEL--SKLRRDLEEsnLQHEQAMSNLRKK--HNDT 1194
Cdd:pfam05622 229 RLIIER-DTLRETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEImpAEIREKLIR--LQHENKMLRLGQEgsYRER 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1195 VAEMSEQIDQLNKHKAKVEKERATMSAEVSDLQSlldhsnkaqanaekQVKQLEVQLADAQFKVDEMNRTLNDLDGGKKK 1274
Cdd:pfam05622 306 LTELQQLLEDANRRKNELETQNRLANQRILELQQ--------------QVEELQKALQEQGSKAEDSSLLKQKLEEHLEK 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 556079866 1275 LAVENSELQRQLEESESQVAQLNKIKASLATQLEEAKRMADEEAR 1319
Cdd:pfam05622 372 LHEAQSELQKKKEQIEELEPKQDSNLAQKIDELQEALRKKDEDMK 416
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
840-1109 |
7.79e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 41.38 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 840 VEDELKAMEEKLKKTEEALAKEEKLRKELEEHNVKVLQEKNDLFLQLEAERMGAGDVEERLNKALTQKGDLESQLADLND 919
Cdd:pfam06160 91 IEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSQFEELTE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 920 RLSHEEdAHASLSqskkKLEGEISGLKKDIEDMELALQKAEQDKATKDHQIRNLNDEIQHQDELINKLN--KEKKHLQEA 997
Cdd:pfam06160 171 SGDYLE-AREVLE----KLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGYALEHLNvdKEIQQLEEQ 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 998 SQKTSEDLQATE-DKVNHLNKvkaKLEQTLDELEDSLEREKKARGDIEKNKRKVEGDLKlaqeavadleknkkEMEQNLQ 1076
Cdd:pfam06160 246 LEENLALLENLElDEAEEALE---EIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLE--------------HAEEQNK 308
|
250 260 270
....*....|....*....|....*....|....*.
gi 556079866 1077 RKEKEMASLAAKL---EDEQALVAKLQKQIKELQAR 1109
Cdd:pfam06160 309 ELKEELERVQQSYtlnENELERVRGLEKQLEELEKR 344
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
960-1133 |
8.22e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.95 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 960 EQDKATKDHQIRNLNDEIQHQDELINKLNKEKKHLQEASQktsEDLQATEDKvnhlnkvKAKLEQTLDELEDSLEREKKA 1039
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEK---ERLAAQEQK-------KQAEEAAKQAALKQKQAEEAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1040 RGDIEKNKRKVEGDLKLAQEAVADLEKNKKEMEQ-NLQRKEKEMASLAAKLEDEQALVAKLQKQIKELQARIEELEEELE 1118
Cdd:PRK09510 139 AKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEaEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKK 218
|
170
....*....|....*
gi 556079866 1119 AERQARAKAEKQRAD 1133
Cdd:PRK09510 219 AAAEAKAAAAKAAAE 233
|
|
| RING-HC_BRCA1 |
cd16498 |
RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and ... |
2153-2213 |
8.31e-03 |
|
RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also known as RING finger protein 53 (RNF53), is a RING finger protein encoded by the tumor suppressor gene BRCA1 that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus.
Pssm-ID: 438161 [Multi-domain] Cd Length: 94 Bit Score: 37.66 E-value: 8.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556079866 2153 NTDEVLMEEIKEYKEQLTCPSCKVKRKDAVLIKCFHVFCYDCLktrYETRQRK-----CPKCNAPF 2213
Cdd:cd16498 1 SRIERVQEVISAMQKNLECPICLELLKEPVSTKCDHQFCRFCI---LKLLQKKkkpapCPLCKKSV 63
|
|
| RING-HC_RAD16-like |
cd16567 |
RING finger, HC subclass, found in Saccharomyces cerevisiae DNA repair protein RAD16, ... |
2171-2213 |
8.91e-03 |
|
RING finger, HC subclass, found in Saccharomyces cerevisiae DNA repair protein RAD16, Schizosaccharomyces pombe rhp16, and similar proteins; Budding yeast RAD16, also known as ATP-dependent helicase RAD16, is encoded by a yeast excision repair gene homologous to the recombinational repair gene RAD54 and to the SNF2 gene involved in transcriptional activation. It is a component of the global genome repair (GGR) complex that promotes global genome nucleotide excision repair (GG-NER) by removing DNA damage from non-transcribing DNA. RAD16 is involved in differential repair of DNA after UV damage, and repairs preferentially the MAT-alpha locus compared with the HML-alpha locus. Fission yeast rhp16, also known as ATP-dependent helicase rhp16, is a RAD16 homolog. It is involved in GGR via nucleotide excision repair (NER), in conjunction with rhp7, after UV irradiation. Both RAD16 and rhp16 contain a C3HC4-type RING-HC finger, as well as a DEAD-like helicase domain and a helicase superfamily C-terminal domain.
Pssm-ID: 438229 [Multi-domain] Cd Length: 48 Bit Score: 36.16 E-value: 8.91e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 556079866 2171 CPSCKVKRKDAVLIKCFHVFCYDCLKTRYET---RQRKCPKCNAPF 2213
Cdd:cd16567 3 CGICHEEAEDPVVARCHHVFCRACVKEYIESapgGKVTCPTCHKPL 48
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
970-1110 |
9.24e-03 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 41.24 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 970 IRNLNDEIQhqdelINKLNKEKKHLQEASQKTSEDLQATEDKVNHLnkvkAKLEqTLDELEDSLEREKKARGDIEKNKRk 1049
Cdd:PRK05729 730 IRNIRAEMN-----IPPSKKLPLLLKGADAEDRARLEANEAYIKRL----ARLE-SLEILADDEEAPEGAASAVVGGAE- 798
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556079866 1050 vegdLKLAQEAVADLEKNKKEMEQNLQRKEKEMASLAAKL--------------EDEQALVAKLQKQIKELQARI 1110
Cdd:PRK05729 799 ----LFLPLEGLIDVEAELARLEKELAKLEKEIERVEKKLsnegfvakapeevvEKEREKLAEYEEKLAKLKERL 869
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1155-1397 |
9.38e-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: 41.26 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1155 QIELNKRREAELSKL--RRDLEESNLQHEQAM---SNLRKKHNDTVAEMSEQIDQLNKHKAKVEKER---ATMSAEVSDL 1226
Cdd:pfam17380 298 QERLRQEKEEKAREVerRRKLEEAEKARQAEMdrqAAIYAEQERMAMERERELERIRQEERKRELERirqEEIAMEISRM 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1227 QSLLDHSNKAQANAEKQVKQLEvqladaqfkvdemnrtlndldgGKKKLAVENSELQRQLEESESQVAQLNKIKASlaTQ 1306
Cdd:pfam17380 378 RELERLQMERQQKNERVRQELE----------------------AARKVKILEEERQRKIQQQKVEMEQIRAEQEE--AR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1307 LEEAKRMADEEARERAAILGKYRNLEHDLDNLRESVEEEQEAKADFQRQLSKANAEAQLWRSKYESEGLARLEELEEAKR 1386
Cdd:pfam17380 434 QREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEER 513
|
250
....*....|.
gi 556079866 1387 KLHGKLQEAEE 1397
Cdd:pfam17380 514 KRKLLEKEMEE 524
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
924-1247 |
9.42e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 40.90 E-value: 9.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 924 EEDAHASLSQSKKKLEGEISGLKKDIEDMELALQKAEqDKATKDHQIRNLNDEIQHQDELINKLNKEKKHLQEASQKTSE 1003
Cdd:pfam09731 123 EQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAV-KAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1004 DLQATEDKVNHLN----KVKAKLEQTLDELEDSLEREKKARGDIEK-NKRKVEGDLKLAQEAVAdleknkkeMEQNLQRK 1078
Cdd:pfam09731 202 AKQSEEEAAPPLLdaapETPPKLPEHLDNVEEKVEKAQSLAKLVDQyKELVASERIVFQQELVS--------IFPDIIPV 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1079 EKEMASLAAklEDEQALVAKLQKQIKELQARIEELEEELEaeRQARAKAEKQRADLAREIEELSERLEESGGATSSQIEL 1158
Cdd:pfam09731 274 LKEDNLLSN--DDLNSLIAHAHREIDQLSKKLAELKKREE--KHIERALEKQKEELDKLAEELSARLEEVRAADEAQLRL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1159 -NKRREAEL-----SKLRRDLEESNLQHEQAMSNlrkkhNDTVAEMSEQIDQLNKHKAKVEKERA-------TMSAEVSD 1225
Cdd:pfam09731 350 eFEREREEIresyeEKLRTELERQAEAHEEHLKD-----VLVEQEIELQREFLQDIKEKVEEERAgrllklnELLANLKG 424
|
330 340
....*....|....*....|..
gi 556079866 1226 LQSLLDhSNKAQANAEKQVKQL 1247
Cdd:pfam09731 425 LEKATS-SHSEVEDENRKAQQL 445
|
|
| RING-HC_ORTHRUS_rpt1 |
cd23138 |
first RING finger, HC subclass, found in Arabidopsis thaliana ORTHRUS and similar proteins; ... |
2167-2213 |
9.81e-03 |
|
first RING finger, HC subclass, found in Arabidopsis thaliana ORTHRUS and similar proteins; This subfamily includes Arabidopsis thaliana ORTHRUS 1-5. They are E3 ubiquitin-protein ligases that may participate in CpG methylation-dependent transcriptional regulation and/or epigenetic transcriptional silencing. ORTHRUS 1 mediates ubiquitination with the E2 ubiquitin-conjugating enzymes UBC11, UBC8 and UBC8 homologs (e.g. UBC10, UBC11, UBC28 and UBC29) but not with UBC27, UBC30, UBC32, UBC34 and UBC36. ORTHRUS 2 and 5 mediate ubiquitination with the E2 ubiquitin-conjugating enzyme UBC11. ORTHRUS 1 and 2 promote methylation-mediated gene silencing leading, for example, to early flowering. They can bind to CpG, CpNpG, and CpNpN DNA motifs, with a strong preference for methylated forms, and with highest affinity for CpG substrates. Members of this subfamily contain two typical C3HC4-type RING-HC fingers. This model corresponds to the first one.
Pssm-ID: 438500 [Multi-domain] Cd Length: 48 Bit Score: 36.27 E-value: 9.81e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 556079866 2167 EQLTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYETRQRKCPKCNAPF 2213
Cdd:cd23138 1 DELNCSFCMQLPERPVTTPCGHNFCLKCFQKWMGQGKKTCGTCRSPI 47
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1300-1424 |
9.91e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 9.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556079866 1300 KASLATQLEEAKRMAD---EEARERAAILGKyrnlehdlDNLRESVEEEQEAKADFQRQLSKANAEAQLW--RSKYESEG 1374
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKrilEEAKKEAEAIKK--------EALLEAKEEIHKLRNEFEKELRERRNELQKLekRLLQKEEN 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 556079866 1375 LAR-LEELEEAKRKLHGKLQEAEEAMEQLNAKCSGLEKTKSHLQGELEDMS 1424
Cdd:PRK12704 98 LDRkLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIS 148
|
|
| RING-HC_TRIM43-like_C-IV |
cd16603 |
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM43, TRIM48, TRIM49, ... |
2165-2216 |
9.97e-03 |
|
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM43, TRIM48, TRIM49, TRIM51, TRIM64 and similar proteins; The family includes a group of closely related uncharacterized tripartite motif-containing proteins, TRIM43, TRIM43B, TRIM48/RNF101, TRIM49/RNF18, TRIM49B, TRIM49C/TRIM49L2, TRIM49D/TRIM49L, TRIM51/SPRYD5, TRIM64, TRIM64B, and TRIM64C, whose biological function remain unclear. TRIM49, also known as testis-specific RING-finger protein, has moderate similarity with SS-A/Ro52 antigen, suggesting it may be one of the target proteins of autoantibodies in the sera of patients with these autoimmune disorders. All family members belong to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. In RBCC region, they all have a C3HC4-type RING-HC finger.
Pssm-ID: 438265 [Multi-domain] Cd Length: 59 Bit Score: 36.31 E-value: 9.97e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 556079866 2165 YKEQLTCPSCKVKRKDAVLIKCFHVFCYDCLKTRYETRQ--RKCPKCNAP-----FGTN 2216
Cdd:cd16603 1 FQRELTCPICMNYFIDPVTIDCGHSFCRPCLYLNWQDIPflAQCPECRKTteqrnLKTN 59
|
|
| |
