|
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, ... |
96-767 |
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: 1304.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTG 175
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 176 ESGAGKTENTKKVIQYLAVIASSHKPKKDINP--GELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLV 253
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKkkGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 254 GAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNS-YSFLMGGHVEIPGLQDDELFEETLEAMEIM 332
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSyYFFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 333 GFTQEERLGMLKVVSTVLQLGNIRFEKERNNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQTKQQ 412
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 413 ADFAVEALAKAMYERLFRWILARVNKTLDKsKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIMEQ 492
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLDT-KSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 493 EEYKREGIEWNFIDFGLDLQPCIELIERPNnpPGILALLDEECWFPKATDTTFVEKLMNTHSAHAK-FSKPKQHKDKLMF 571
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKPN--MGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKPKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 572 TVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDVDRVvgldtinkmsqSSVPTSTKSKKGMFRTVGQ 651
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEES-----------GGGGGKKKKKGGSFRTVSQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 652 LYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAGS 731
Cdd:cd01377 547 LHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNA 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 1343958102 732 IPKGFMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd01377 627 IPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
844-1924 |
0e+00 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 1252.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 844 TRQEEEMGQKEEELKAVREAAAKAEADLKDITQKHSQLVEEQAMLEAKLQAEAELYAEAEDMRVRLEAKKQELEEVLHEM 923
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 924 EARLEEEEERSISLQQEKKEMEQELQLMEAHIVQEEDARQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLLEER 1003
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1004 LADMSSNLAEEEEKSKNLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAA 1083
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1084 KEEELQTTQACLDEESRQRGAALKRVRDLEALLAELQEDLEAEKVARGKAEAARRDLGEELNSLRSELEDSLDTTAAQQE 1163
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1164 LRVKREQEMAMLKKAMEDEGRSHETQIQELRQKHGQAVEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTK 1243
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1244 QDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQELLSEE 1323
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1324 TRQKLNLSGRLRQLEEDKGCLMEQLEEEMEAKQAVERQASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGD 1403
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1404 YEEKAAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSAKSAEERDRAEAELREKETKVLA 1483
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1484 LMKMLEDKQEALQEAERTVKALRVEMEDLISSKDDVGKSVHDLERAKRGLEAFVEEMKTQMEELEDELQVAEDAKLRLEV 1563
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1564 NSQALRAQHERELQAREEQGEEKRRQLLKQVRELEAELEEERKQRTLASAARKKLEGEVKNTEEQLEAASRGRDEALKQL 1643
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1644 RKNQGQLKELHRELEEGRAAHKEILASAREAERRCKNLEAEILQMQEMLAAAERARKQAETERDELSEEVAGGSSGRSLL 1723
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1724 SDEKRRLEAKISQLEEELEEEQANVETLNERLRKSQQLVDQLGAELTAERASSQNREGSRLQLEKQTRDLKAKLQDVESQ 1803
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1804 ARSKLKSSVAALEAKLREAEEQLEVESRERQASAKNLRQKEKKLKDLTAQMEDERKQAQDYKDQMEKSSARMKQLKHQLE 1883
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 1343958102 1884 EAEEEAQRVAAARRKLQRELDEALEANDALSREVSSLRSKL 1924
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
96-767 |
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: 1182.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTG 175
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 176 ESGAGKTENTKKVIQYLAVIASSHKPKKDIN-PGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVG 254
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNiPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 255 AFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFLMGGHVEIPGLQDDELFEETLEAMEIMGF 334
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 335 TQEERLGMLKVVSTVLQLGNIRFEKERNNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQTKQQAD 414
Cdd:cd14920 241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 415 FAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIMEQEE 494
Cdd:cd14920 321 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 495 YKREGIEWNFIDFGLDLQPCIELIERPNNPPGILALLDEECWFPKATDTTFVEKLMNTHSAHAKFSKPKQHKDKLMFTVL 574
Cdd:cd14920 401 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 575 HYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDVDRVVGLDTINKMSQSSVPTSTKSKKGMFRTVGQLYK 654
Cdd:cd14920 481 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 655 ESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAGSIPK 734
Cdd:cd14920 561 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 1343958102 735 GFMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd14920 641 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
96-767 |
0e+00 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 1164.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTG 175
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 176 ESGAGKTENTKKVIQYLAVIASSHKPKKDIN-PGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVG 254
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 255 AFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFLMGGHVEIPGLQDDELFEETLEAMEIMGF 334
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 335 TQEERLGMLKVVSTVLQLGNIRFEKERNNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQTKQQAD 414
Cdd:cd14921 241 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 415 FAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIMEQEE 494
Cdd:cd14921 321 FAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 495 YKREGIEWNFIDFGLDLQPCIELIERPNNPPGILALLDEECWFPKATDTTFVEKLMNTHSAHAKFSKPKQHKDKLMFTVL 574
Cdd:cd14921 401 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 575 HYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDVDRVVGLDTINKMSQSSVPTSTKSKKGMFRTVGQLYK 654
Cdd:cd14921 481 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 655 ESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAGSIPK 734
Cdd:cd14921 561 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 1343958102 735 GFMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd14921 641 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
96-767 |
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: 1120.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTG 175
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 176 ESGAGKTENTKKVIQYLAVIASSHKPKKD-----INPGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSG 250
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDqssiaLSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 251 CLVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFLMGGHVEIPGLQDDELFEETLEAME 330
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 331 IMGFTQEERLGMLKVVSTVLQLGNIRFEKERNNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQTK 410
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 411 QQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIM 490
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 491 EQEEYKREGIEWNFIDFGLDLQPCIELIERPNNPPGILALLDEECWFPKATDTTFVEKLMNTHSAHAKFSKPKQHKDKLM 570
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 571 FTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDVDRVVGLDTINKMSQSSvPTSTKSKKGMFRTVG 650
Cdd:cd14932 481 FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESL-HGAFKTRKGMFRTVG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 651 QLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAG 730
Cdd:cd14932 560 QLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 639
|
650 660 670
....*....|....*....|....*....|....*..
gi 1343958102 731 SIPKGFMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd14932 640 AIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
84-767 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1072.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 84 VEDMAALTFLNEASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNML 163
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 164 QDREDQSILCTGESGAGKTENTKKVIQYLAVIASSHKPKkdiNPGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIK 243
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAG---NVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 244 LNFDVSGCLVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFL-MGGHVEIPGLQDDELF 322
Cdd:pfam00063 158 IQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLsQSGCYTIDGIDDSEEF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 323 EETLEAMEIMGFTQEERLGMLKVVSTVLQLGNIRFEKERNNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGRE 402
Cdd:pfam00063 238 KITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 403 VVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQL 482
Cdd:pfam00063 318 TVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 483 FNHTMFIMEQEEYKREGIEWNFIDFGlDLQPCIELIERPnnPPGILALLDEECWFPKATDTTFVEKLMNTHSAHAKFSKP 562
Cdd:pfam00063 398 FNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQKP 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 563 KQhKDKLMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDVDRVVGLDtinkMSQSSVPTSTKSK 642
Cdd:pfam00063 475 RL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAA----ANESGKSTPKRTK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 643 KGMFRTVGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 722
Cdd:pfam00063 550 KKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQ 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1343958102 723 RYEILAAGSIPKGFMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:pfam00063 630 RYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
96-767 |
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: 1071.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTG 175
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 176 ESGAGKTENTKKVIQYLAVIASSHKPKKDinPGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVGA 255
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKD--QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 256 FIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFLMGGHVEIPGLQDDELFEETLEAMEIMGFT 335
Cdd:cd14919 159 NIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 336 QEERLGMLKVVSTVLQLGNIRFEKERNNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQTKQQADF 415
Cdd:cd14919 239 EEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 416 AVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIMEQEEY 495
Cdd:cd14919 319 AIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 496 KREGIEWNFIDFGLDLQPCIELIERPNNPPGILALLDEECWFPKATDTTFVEKLMNTHSAHAKFSKPKQHKDKLMFTVLH 575
Cdd:cd14919 399 QREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCIIH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 576 YAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDVDRVVGLDTINKMSQSSVPTSTKSKKGMFRTVGQLYKE 655
Cdd:cd14919 479 YAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYKE 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 656 SLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAGSIPKG 735
Cdd:cd14919 559 QLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKG 638
|
650 660 670
....*....|....*....|....*....|..
gi 1343958102 736 FMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd14919 639 FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
96-767 |
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: 1063.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTG 175
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 176 ESGAGKTENTKKVIQYLAVIASShKPKKD-----------INPGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKL 244
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAAS-KPKGSgavphpavnpaVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 245 NFDVSGCLVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFLMGGHVEIPGLQDDELFEE 324
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 325 TLEAMEIMGFTQEERLGMLKVVSTVLQLGNIRFEKERNNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVV 404
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 405 QKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFN 484
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 485 HTMFIMEQEEYKREGIEWNFIDFGLDLQPCIELIERPNnppGILALLDEECWFPKATDTTFVEKLMNTHSAHAKFSKpKQ 564
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 565 HKDKLMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDVDrVVGLDTinkMSQSSVPTSTKSKKG 644
Cdd:cd14911 476 FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQ---QALTDTQFGARTRKG 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 645 MFRTVGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 724
Cdd:cd14911 552 MFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1343958102 725 EILAAGSIPKGFMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd14911 632 ELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
96-767 |
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: 1056.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTG 175
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 176 ESGAGKTENTKKVIQYLAVIASSHKPKKDINP-----GELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSG 250
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNSlalshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 251 CLVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFLMGGHVEIPGLQDDELFEETLEAME 330
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 331 IMGFTQEERLGMLKVVSTVLQLGNIRFEKERNNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQTK 410
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 411 QQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIM 490
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 491 EQEEYKREGIEWNFIDFGLDLQPCIELIERPNNPPGILALLDEECWFPKATDTTFVEKLMNTHSAHAKFSKPKQHKDKLM 570
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 571 FTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDVDRVVGLDTINKMSQssVPTSTKSKKGMFRTVG 650
Cdd:cd15896 481 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSE--MPGAFKTRKGMFRTVG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 651 QLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAG 730
Cdd:cd15896 559 QLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 638
|
650 660 670
....*....|....*....|....*....|....*..
gi 1343958102 731 SIPKGFMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd15896 639 AIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
96-767 |
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: 996.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTG 175
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 176 ESGAGKTENTKKVIQYLAVIASSHKPKKDIN-PGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVG 254
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGvPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 255 AFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFLMGGHVEIPGlQDDELFEETLEAMEIMGF 334
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLESLRVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 335 TQEERLGMLKVVSTVLQLGNIRFEKERNNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQTKQQAD 414
Cdd:cd14930 240 SHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 415 FAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIMEQEE 494
Cdd:cd14930 320 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 495 YKREGIEWNFIDFGLDLQPCIELIERPNNPPGILALLDEECWFPKATDTTFVEKLMNTHSAHAKFSKPKQHKDKLMFTVL 574
Cdd:cd14930 400 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 575 HYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDVDRVVGLDTINKMSQSsvPTSTKSKKGMFRTVGQLYK 654
Cdd:cd14930 480 HYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDG--PPGGRPRRGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 655 ESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAGSIPK 734
Cdd:cd14930 558 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 1343958102 735 GFMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd14930 638 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
77-779 |
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: 993.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 77 NPPKFSKVEDMAALTFLNEASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITD 156
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 157 NAYRNMLQDREDQSILCTGESGAGKTENTKKVIQYLAVIASSHKPKkdinpGELEKQLLQANPILEAFGNAKTIKNDNSS 236
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV-----GSVEDQILESNPILEAFGNAKTLRNNNSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 237 RFGKFIKLNFDVSGCLVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFL-MGGHVEIPG 315
Cdd:smart00242 156 RFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLnQGGCLTVDG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 316 LQDDELFEETLEAMEIMGFTQEERLGMLKVVSTVLQLGNIRFEKERNNEQATMPDNT-AAQKVCHLQGINVTDFSRAILT 394
Cdd:smart00242 236 IDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEELEKALTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 395 PKIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKsKRQSSSFLGILDIAGFEIFEDNSFEQLCINY 474
Cdd:smart00242 316 RKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSF-KDGSTYFIGVLDIYGFEIFEVNSFEQLCINY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 475 TNERLQQLFNHTMFIMEQEEYKREGIEWNFIDFGlDLQPCIELIErpNNPPGILALLDEECWFPKATDTTFVEKLMNTHS 554
Cdd:smart00242 395 ANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQTFLEKLNQHHK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 555 AHAKFSKPKQhKDKLMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDVdrvvgldtinkmsqss 634
Cdd:smart00242 472 KHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSG---------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 635 vpTSTKSKKGMFRTVGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNR 714
Cdd:smart00242 535 --VSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYR 612
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1343958102 715 IVFQEFRQRYEILAAGSIPKGFMDGKQACGLMVKHLDLDPNLYRIGQSKMFFRTGVLAQLEEERD 779
Cdd:smart00242 613 LPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
96-767 |
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: 878.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRH-EVPPHIYSITDNAYRNMLQDREDQSILCT 174
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 175 GESGAGKTENTKKVIQYLAVIASSHKPKKDINPGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVG 254
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 255 AFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFL-----MGGHVEIPGLQDDELFEETLEAM 329
Cdd:cd00124 161 ASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDDAEEFQELLDAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 330 EIMGFTQEERLGMLKVVSTVLQLGNIRFEKERNNE--QATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKA 407
Cdd:cd00124 241 DVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITKP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 408 QTKQQADFAVEALAKAMYERLFRWILARVNKTLD-KSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHT 486
Cdd:cd00124 321 LTVEQAEDARDALAKALYSRLFDWLVNRINAALSpTDAAESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 487 MFIMEQEEYKREGIEWNFIDFgLDLQPCIELIERPnnPPGILALLDEECWFPKATDTTFVEKLMNTHSAHAKFSKPKQhK 566
Cdd:cd00124 401 VFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKR-K 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 567 DKLMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSgfiqdlwkdvdrvvgldtinkmsqssvptstkskkgmf 646
Cdd:cd00124 477 AKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ-------------------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 647 rtvgqlYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 726
Cdd:cd00124 519 ------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRI 592
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1343958102 727 LAAGSIPKGFMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd00124 593 LAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
34-1396 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 874.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 34 VWVPSEREGFEAASIREEKGE----QVLVELSNGQKVTVSKDDIQ--KMNPPKFSKVEDMAALTFLNEASVLQNLRERYF 107
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNkgkvTEEGKKEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 108 SSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTGESGAGKTENTKK 187
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 188 VIQYLAVIASSHKPKKdinpGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVGAFIDTYLLEKSRC 267
Cdd:COG5022 172 IMQYLASVTSSSTVEI----SSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 268 IRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFL-MGGHVEIPGLQDDELFEETLEAMEIMGFTQEERLGMLKVV 346
Cdd:COG5022 248 VHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLsQGGCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKIL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 347 STVLQLGNIRFEKERnNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQTKQQADFAVEALAKAMYE 426
Cdd:COG5022 328 AAILHIGNIEFKEDR-NGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYS 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 427 RLFRWILARVNKTLDKSKRQsSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIMEQEEYKREGIEWNFID 506
Cdd:COG5022 407 NLFDWIVDRINKSLDHSAAA-SNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFID 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 507 FgLDLQPCIELIERpNNPPGILALLDEECWFPKATDTTFVEKLMNT--HSAHAKFSKPKQHKDKlmFTVLHYAGKVDYNA 584
Cdd:COG5022 486 Y-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQRlnKNSNPKFKKSRFRDNK--FVVKHYAGDVEYDV 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 585 ADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDvdrvvgldtinkmsqssvpTSTKSKKGMFRTVGQLYKESLGKLMATL 664
Cdd:COG5022 562 EGFLDKNKDPLNDDLLELLKASTNEFVSTLFDD-------------------EENIESKGRFPTLGSRFKESLNSLMSTL 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 665 HNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAA----GSIPKGFMDGK 740
Cdd:COG5022 623 NSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPskswTGEYTWKEDTK 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 741 QACGLMVKHLDLDPNLYRIGQSKMFFRTGVLAQLEEERDLKLTVVIIAFQARALGFLGRKAFSKRQQQLTAMKVIQRNCA 820
Cdd:COG5022 703 NAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFR 782
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 821 CYLRLRNWQWWRLFTKVKPLLQVTRQEeemgqkeeelkavreaaakaeadlKDITQKHSQLVEEQAMLEAKLQAeaelya 900
Cdd:COG5022 783 LRRLVDYELKWRLFIKLQPLLSLLGSR------------------------KEYRSYLACIIKLQKTIKREKKL------ 832
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 901 eaedmRVRLEAKKQELEEVLHEMEARLEEEEERSISLQQEKKeMEQELQLMeahivqeEDARQKLQLEKAAVEgRVKKLE 980
Cdd:COG5022 833 -----RETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETI-YLQSAQRV-------ELAERQLQELKIDVK-SISSLK 898
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 981 EnlllsedQNNKLQKErklleerLADMSSNLAEEE-EKSKNLSKLKSKHESMISELEVRLKKE-EKTRQDVEKAKRKVEA 1058
Cdd:COG5022 899 L-------VNLELESE-------IIELKKSLSSDLiENLEFKTELIARLKKLLNNIDLEEGPSiEYVKLPELNKLHEVES 964
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1059 ELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQACLDEESRQRGA---ALKRVRDLEALLAELQED------------- 1122
Cdd:COG5022 965 KLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGAlqeSTKQLKELPVEVAELQSAskiissestelsi 1044
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1123 -LEAEKVaRGKAEAARRDLGEELNSLRSELEDSLDTTAAQQELRVKREQEMAMLKKAMEDEGRSHETQIQELRQKHGQAV 1201
Cdd:COG5022 1045 lKPLQKL-KGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAQMI 1123
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1202 --EELREHLEQAKKVRAALEKAKQALEKEAADLS-----ADLRALSSTKQDVEQKKKKvEAQLNDLQLRFSESERQRNEL 1274
Cdd:COG5022 1124 klNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDglfweANLEALPSPPPFAALSEKR-LYQSALYDEKSKLSSSEVNDL 1202
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1275 SERVSKMTVEL--DSVTGLLN---EAEGRNIKLSKEASSISSQLQD----AQELLSEETRQKLNLSGRLRQLEEDKGcLM 1345
Cdd:COG5022 1203 KNELIALFSKIfsGWPRGDKLkklISEGWVPTEYSTSLKGFNNLNKkfdtPASMSNEKLLSLLNSIDNLLSSYKLEE-EV 1281
|
1370 1380 1390 1400 1410
....*....|....*....|....*....|....*....|....*....|..
gi 1343958102 1346 EQLEEEMEAKQAVERQASSLSVQLSDLK-KRLEELSAAVELLEEGKKRLQRE 1396
Cdd:COG5022 1282 LPATINSLLQYINVGLFNALRTKASSLRwKSATEVNYNSEELDDWCREFEIS 1333
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
96-767 |
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: 778.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTG 175
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 176 ESGAGKTENTKKVIQYLAVIAS-SHKPKKDINP------GELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDV 248
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAAlGDGPGKKAQFlatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 249 SGCLVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLE-DFNSYSFLMGGHVEIPGLQDDELFEETLE 327
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSmNPYDYHFCSQGVTTVDNMDDGEELMATDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 328 AMEIMGFTQEERLGMLKVVSTVLQLGNIRFEKERNNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKA 407
Cdd:cd14927 241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 408 QTKQQADFAVEALAKAMYERLFRWILARVNKTLDKS-KRQssSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHT 486
Cdd:cd14927 321 QSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKlPRQ--FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 487 MFIMEQEEYKREGIEWNFIDFGLDLQPCIELIERPNnppGILALLDEECWFPKATDTTFVEKLMNTHSAHA-KFSKP--- 562
Cdd:cd14927 399 MFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHLGKSpNFQKPrpd 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 563 KQHKDKLMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDvdrVVGLDTInkmSQSSVPTSTKSK 642
Cdd:cd14927 476 KKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYEN---YVGSDST---EDPKSGVKEKRK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 643 KGM-FRTVGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFR 721
Cdd:cd14927 550 KAAsFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFK 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1343958102 722 QRYEILAAGSIPK-GFMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd14927 630 QRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
97-767 |
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: 764.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTGE 176
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 177 SGAGKTENTKKVIQYLAVIASSHKPKKDINP---GELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLV 253
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGDLAKKKDSkmkGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 254 GAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLL-EDFNSYSFLMGGHVEIPGLQDDELFEETLEAMEIM 332
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLItTNPYDYPFISQGEILVASIDDAEELLATDSAIDIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 333 GFTQEERLGMLKVVSTVLQLGNIRFEKERNNEQATmPDNT-AAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQTKQ 411
Cdd:cd14913 242 GFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 412 QADFAVEALAKAMYERLFRWILARVNKTLDkSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIME 491
Cdd:cd14913 321 QVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 492 QEEYKREGIEWNFIDFGLDLQPCIELIERPNnppGILALLDEECWFPKATDTTFVEKLMNTH-SAHAKFSKPKQHKDK-- 568
Cdd:cd14913 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPKVVKGRae 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 569 LMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDVDRVVGLDTINKmsqssvptSTKSKKGMFRT 648
Cdd:cd14913 477 AHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKK--------VAKKKGSSFQT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 649 VGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILA 728
Cdd:cd14913 549 VSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLN 628
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1343958102 729 AGSIPKG-FMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd14913 629 ASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
96-767 |
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: 762.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTG 175
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 176 ESGAGKTENTKKVIQYLAVI-ASSHKPKKDINPGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVG 254
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVgASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 255 AFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLL-EDFNSYSFLMGGHVEIPGLQDDELFEETLEAMEIMG 333
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 334 FTQEERLGMLKVVSTVLQLGNIRFEKERNNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQTKQQA 413
Cdd:cd14909 241 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 414 DFAVEALAKAMYERLFRWILARVNKTLD-KSKRQssSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIMEQ 492
Cdd:cd14909 321 TNSIGALCKGVFDRLFKWLVKKCNETLDtQQKRQ--HFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 493 EEYKREGIEWNFIDFGLDLQPCIELIERPNnppGILALLDEECWFPKATDTTFVEKLMNTH-SAHAKFSKPKQHKDKLM- 570
Cdd:cd14909 399 EEYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKPPKPGQQa 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 571 --FTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDvdrvvgldtinKMSQSSVPTSTK----SKKG 644
Cdd:cd14909 476 ahFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAD-----------HAGQSGGGEQAKggrgKKGG 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 645 MFRTVGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 724
Cdd:cd14909 545 GFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRY 624
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1343958102 725 EILAAGSIpKGFMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd14909 625 KILNPAGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
96-767 |
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: 745.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTG 175
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 176 ESGAGKTENTKKVIQYLAVIASSHKPKKDiNPGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVGA 255
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSD-GKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 256 FIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLL-EDFNSYSFLMGGHVEIPGLQDDELFEETLEAMEIMGF 334
Cdd:cd14934 160 DIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 335 TQEERLGMLKVVSTVLQLGNIRFEKERNNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQTKQQAD 414
Cdd:cd14934 240 SAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQCN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 415 FAVEALAKAMYERLFRWILARVNKTLDkSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIMEQEE 494
Cdd:cd14934 320 NSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 495 YKREGIEWNFIDFGLDLQPCIELIERPNnppGILALLDEECWFPKATDTTFVEKLMNTH-SAHAKFSKPKQHKDK---LM 570
Cdd:cd14934 399 YKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKGGKGKgpeAH 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 571 FTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSsgfiqdlwkdvdrvVGLDTINKMSQSSVPTSTKSKKG-MFRTV 649
Cdd:cd14934 476 FELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSS--------------LGLLALLFKEEEAPAGSKKQKRGsSFMTV 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 650 GQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAA 729
Cdd:cd14934 542 SNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNP 621
|
650 660 670
....*....|....*....|....*....|....*...
gi 1343958102 730 GSIPKGFMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd14934 622 NVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
96-767 |
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: 706.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTG 175
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 176 ESGAGKTENTKKVIQYLAVIASSHKPKKDInpGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVGA 255
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKL--GALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 256 FIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKgKMRDELLL-EDFNSYSFLMGGHVEIPGLQDDELFEETLEAMEIMGF 334
Cdd:cd14929 159 DIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVsANPSDFHFCSCGAVAVESLDDAEELLATEQAMDILGF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 335 TQEERLGMLKVVSTVLQLGNIRFEKERNNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQTKQQAD 414
Cdd:cd14929 238 LPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 415 FAVEALAKAMYERLFRWILARVNKTLDkSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIMEQEE 494
Cdd:cd14929 318 YAVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 495 YKREGIEWNFIDFGLDLQPCIELIERPNnppGILALLDEECWFPKATDTTFVEKLMNTH---SAHAKFSKPKQHKDKLMF 571
Cdd:cd14929 397 YRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfgkSVHFQKPKPDKKKFEAHF 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 572 TVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKdvdrvvglDTINKMSQSSVPTSTKSKKGMFRTVGQ 651
Cdd:cd14929 474 ELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFE--------NYISTDSAIQFGEKKRKKGASFQTVAS 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 652 LYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAGS 731
Cdd:cd14929 546 LHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRT 625
|
650 660 670
....*....|....*....|....*....|....*..
gi 1343958102 732 IPKG-FMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd14929 626 FPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
97-767 |
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: 703.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTGE 176
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 177 SGAGKTENTKKVIQYLAVIAS-SHKPKKDINPGE--LEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLV 253
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAiGDRSKKDQTPGKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 254 GAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFN-SYSFLMGGHVEIPGLQDDELFEETLEAMEIM 332
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPyDYAFISQGETTVASIDDAEELMATDNAFDVL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 333 GFTQEERLGMLKVVSTVLQLGNIRFEKERNNEQATmPDNT-AAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQTKQ 411
Cdd:cd14917 242 GFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 412 QADFAVEALAKAMYERLFRWILARVNKTLDkSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIME 491
Cdd:cd14917 321 QVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 492 QEEYKREGIEWNFIDFGLDLQPCIELIERPNnppGILALLDEECWFPKATDTTFVEKLMNTH-SAHAKFSKPKQHKDK-- 568
Cdd:cd14917 400 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPRNIKGKpe 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 569 LMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDvdrVVGLDTINKMSQSsvptstKSKKG-MFR 647
Cdd:cd14917 477 AHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN---YAGADAPIEKGKG------KAKKGsSFQ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 648 TVGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 727
Cdd:cd14917 548 TVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 627
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1343958102 728 AAGSIPKG-FMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd14917 628 NPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
98-767 |
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: 693.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 98 VLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTGES 177
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 178 GAGKTENTKKVIQYLAVIASSHKPKKDIN---PGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVG 254
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEESgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 255 AFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLL-EDFNSYSFLMGGHVEIPGLQDDELFEETLEAMEIMG 333
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 334 FTQEERLGMLKVVSTVLQLGNIRFEKERNNEQATmPDNT-AAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQTKQQ 412
Cdd:cd14918 243 FTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 413 ADFAVEALAKAMYERLFRWILARVNKTLDkSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIMEQ 492
Cdd:cd14918 322 VYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 493 EEYKREGIEWNFIDFGLDLQPCIELIERpnnPPGILALLDEECWFPKATDTTFVEKLMNTH-SAHAKFSKPK--QHKDKL 569
Cdd:cd14918 401 EEYKKEGIEWTFIDFGMDLAACIELIEK---PLGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPKvvKGKAEA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 570 MFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDVdrvvgldtINKMSQSSVPTSTKSKKGMFRTV 649
Cdd:cd14918 478 HFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY--------ASAEADSGAKKGAKKKGSSFQTV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 650 GQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAA 729
Cdd:cd14918 550 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNA 629
|
650 660 670
....*....|....*....|....*....|....*....
gi 1343958102 730 GSIPKG-FMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd14918 630 SAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
97-767 |
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: 692.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 97 SVLQNLRERYF-SSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTG 175
Cdd:cd01380 2 AVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 176 ESGAGKTENTKKVIQYLAVIASSHKPKKDInpgelEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVGA 255
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSGETQV-----EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 256 FIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFL-MGGHVEIPGLQDDELFEETLEAMEIMGF 334
Cdd:cd01380 157 NMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTnQGGSPVIDGVDDAAEFEETRKALTLLGI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 335 TQEERLGMLKVVSTVLQLGNIRFEKERNNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQTKQQAD 414
Cdd:cd01380 237 SEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 415 FAVEALAKAMYERLFRWILARVNKTLD-KSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIMEQE 493
Cdd:cd01380 317 VARDALAKHIYAQLFDWIVDRINKALAsPVKEKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 494 EYKREGIEWNFIDFgLDLQPCIELIErpnNPPGILALLDEECWFPKATDTTFVEKLMNTHSAHAK--FSKPKQHKDKlmF 571
Cdd:cd01380 397 EYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPRFSNTA--F 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 572 TVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSssgfiqdlwkdvdrvvgldtinkmsqssvptstKSKKgmfRTVGQ 651
Cdd:cd01380 471 IVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKAS---------------------------------KNRK---KTVGS 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 652 LYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAGS 731
Cdd:cd01380 515 QFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSK 594
|
650 660 670
....*....|....*....|....*....|....*.
gi 1343958102 732 IPKGfMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd01380 595 EWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
97-767 |
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: 689.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTGE 176
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 177 SGAGKTENTKKVIQYLAVIAS-SHKPKKDI---NPGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCL 252
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKENpnaNKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 253 VGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFN-SYSFLMGGHVEIPGLQDDELFEETLEAMEI 331
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPyDYAFVSQGEVSVASIDDSEELLATDSAFDV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 332 MGFTQEERLGMLKVVSTVLQLGNIRFEKERNNEQATmPDNTA-AQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQTK 410
Cdd:cd14916 242 LGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 411 QQADFAVEALAKAMYERLFRWILARVNKTLDkSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIM 490
Cdd:cd14916 321 QQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 491 EQEEYKREGIEWNFIDFGLDLQPCIELIERPNnppGILALLDEECWFPKATDTTFVEKLMNTH-SAHAKFSKPKQHKDK- 568
Cdd:cd14916 400 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRNVKGKq 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 569 -LMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDvdrVVGLDTinkmSQSSVPTSTKSKKGMFR 647
Cdd:cd14916 477 eAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFST---YASADT----GDSGKGKGGKKKGSSFQ 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 648 TVGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 727
Cdd:cd14916 550 TVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 629
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1343958102 728 AAGSIPKG-FMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd14916 630 NPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
97-767 |
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: 687.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTGE 176
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 177 SGAGKTENTKKVIQYLAVIASSHKPKKDINP----GELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCL 252
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQQPgkmqGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 253 VGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDeLLLEDFNSYS--FLMGGHVEIPGLQDDELFEETLEAME 330
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELID-LLLISTNPFDfpFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 331 IMGFTQEERLGMLKVVSTVLQLGNIRFEKERNNEQATmPDNT-AAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQT 409
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 410 KQQADFAVEALAKAMYERLFRWILARVNKTLDkSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFI 489
Cdd:cd14923 320 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 490 MEQEEYKREGIEWNFIDFGLDLQPCIELIERPNnppGILALLDEECWFPKATDTTFVEKLMNTHSAHA-KFSKPKQHKDK 568
Cdd:cd14923 399 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYDQHLGKSnNFQKPKPAKGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 569 --LMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDVDRVVGLDTinkmsqSSVPTSTKSKKGMF 646
Cdd:cd14923 476 aeAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDS------GGSKKGGKKKGSSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 647 RTVGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 726
Cdd:cd14923 550 QTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1343958102 727 LAAGSIPKG-FMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd14923 630 LNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
97-767 |
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: 686.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTGE 176
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 177 SGAGKTENTKKVIQYLAVIA-SSHKPKKDINPGE----LEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGC 251
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAvTGEKKKEEATSGKmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 252 LVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLL-EDFNSYSFLMGGHVEIPGLQDDELFEETLEAME 330
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMATDSAIE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 331 IMGFTQEERLGMLKVVSTVLQLGNIRFEKERNNEQATmPDNT-AAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQT 409
Cdd:cd14910 242 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 410 KQQADFAVEALAKAMYERLFRWILARVNKTLDkSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFI 489
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 490 MEQEEYKREGIEWNFIDFGLDLQPCIELIERPNnppGILALLDEECWFPKATDTTFVEKLMNTHSAHA-KFSKPKQHKDK 568
Cdd:cd14910 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHLGKSnNFQKPKPAKGK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 569 L--MFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDVdrvvgldTINKMSQSSVPTSTKSKKGMF 646
Cdd:cd14910 477 VeaHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGA-------AAAEAEEGGGKKGGKKKGSSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 647 RTVGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 726
Cdd:cd14910 550 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1343958102 727 LAAGSIPKG-FMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd14910 630 LNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
97-767 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 682.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTGE 176
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 177 SGAGKTENTKKVIQYLAVIA-SSHKPKKDINPGE----LEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGC 251
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAvTGEKKKEEITSGKmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 252 LVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLL-EDFNSYSFLMGGHVEIPGLQDDELFEETLEAME 330
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDDQEELMATDSAID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 331 IMGFTQEERLGMLKVVSTVLQLGNIRFEKERNNEQATmPDNT-AAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQT 409
Cdd:cd14912 242 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 410 KQQADFAVEALAKAMYERLFRWILARVNKTLDkSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFI 489
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 490 MEQEEYKREGIEWNFIDFGLDLQPCIELIERPNnppGILALLDEECWFPKATDTTFVEKLMNTH-SAHAKFSKPK--QHK 566
Cdd:cd14912 400 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSANFQKPKvvKGK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 567 DKLMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDVDRVVGldtinKMSQSSVPTSTKSKKGMF 646
Cdd:cd14912 477 AEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEG-----ASAGGGAKKGGKKKGSSF 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 647 RTVGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 726
Cdd:cd14912 552 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 631
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1343958102 727 LAAGSIPKG-FMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd14912 632 LNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
97-767 |
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: 669.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTGE 176
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 177 SGAGKTENTKKVIQYLAVIASSHKPKKDINP-----GELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGC 251
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEAAsgkmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 252 LVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRdELLLEDFNSYSF--LMGGHVEIPGLQDDELFEETLEAM 329
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELI-EMLLITTNPYDFafVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 330 EIMGFTQEERLGMLKVVSTVLQLGNIRFEKERNNEQATmPDNT-AAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQ 408
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 409 TKQQADFAVEALAKAMYERLFRWILARVNKTLDkSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMF 488
Cdd:cd14915 320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 489 IMEQEEYKREGIEWNFIDFGLDLQPCIELIERPNnppGILALLDEECWFPKATDTTFVEKLMNTHSAHA-KFSKPKQHKD 567
Cdd:cd14915 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHLGKSnNFQKPKPAKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 568 K--LMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSssgfiqdlwkdvdrvvGLDTINKM---SQSSVPTSTKSK 642
Cdd:cd14915 476 KaeAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKS----------------GMKTLAFLfsgGQTAEAEGGGGK 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 643 KG------MFRTVGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIV 716
Cdd:cd14915 540 KGgkkkgsSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRIL 619
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1343958102 717 FQEFRQRYEILAAGSIPKG-FMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd14915 620 YADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
97-767 |
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: 651.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTGE 176
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 177 SGAGKTENTKKVIQYLAVIASSHkpkkDINPGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVGAF 256
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGS----ESEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 257 IDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLE-DFNSYSFLMGGHVEIPGLQDDELFEETLEAMEIMGFT 335
Cdd:cd01378 158 ITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQrPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 336 QEERLGMLKVVSTVLQLGNIRFeKERNNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVG---REVVQKAQTKQQ 412
Cdd:cd01378 238 EEEQDSIFRILAAILHLGNIQF-AEDEEGNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSVYEVPLNVEQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 413 ADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIMEQ 492
Cdd:cd01378 317 AAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 493 EEYKREGIEWNFIDFgLDLQPCIELIErpNNPPGILALLDEECWFP-KATDTTFVEKLMNTHSAHAKFSKPKQHKDKLM- 570
Cdd:cd01378 397 EEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSGHFELRRg 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 571 -FTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDvdrvvgldtinkmsqssvPTSTKSKKgmfR-- 647
Cdd:cd01378 474 eFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPE------------------GVDLDSKK---Rpp 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 648 TVGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 727
Cdd:cd01378 533 TAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLL 612
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1343958102 728 AAGSIPKGFMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd01378 613 SPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
97-767 |
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: 640.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTGE 176
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 177 SGAGKTENTKKVIQYLAVIASSHKpkkdinpgELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVGAF 256
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS--------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 257 IDTYLLEKSRCIRQANTERAFHIFYYMVSGAKG--KMRDELLLEDFNSYSFL-MGGHVEIPGLQDDELFEETLEAMEIMG 333
Cdd:cd14883 154 IQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLnQSGCIRIDNINDKKDFDHLRLAMNVLG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 334 FTQEERLGMLKVVSTVLQLGNIRFEK-ERNNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQTKQQ 412
Cdd:cd14883 234 IPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 413 ADFAVEALAKAMYERLFRWILARVNKTLDKSkRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIMEQ 492
Cdd:cd14883 314 ARDNRDAMAKALYSRTFAWLVNHINSCTNPG-QKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 493 EEYKREGIEWNFIDFGlDLQPCIELIERPnnPPGILALLDEECWFPKATDTTFVEKLMNTHSAHAKFSKPKQHKDKLMFT 572
Cdd:cd14883 393 EEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTEFG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 573 VLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDVDRVVGldTINKMSQSSVPTSTKSKKGMfRTVGQL 652
Cdd:cd14883 470 VKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDLLAL--TGLSISLGGDTTSRGTSKGK-PTVGDT 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 653 YKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAGSI 732
Cdd:cd14883 547 FKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRAR 626
|
650 660 670
....*....|....*....|....*....|....*
gi 1343958102 733 PKGFMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd14883 627 SADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
97-767 |
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: 626.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKgkKRHEVPPHIYSITDNAYRNMLQDREDQSILCTGE 176
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 177 SGAGKTENTKKVIQYLAVIASSHkpkkdinpGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVGAF 256
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGS--------SGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 257 IDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFLMG-GHVEIPGLQDDELFEETLEAMEIMGFT 335
Cdd:cd01383 152 IQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQsNCLTIDGVDDAKKFHELKEALDTVGIS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 336 QEERLGMLKVVSTVLQLGNIRFEKERNNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQTKQQADF 415
Cdd:cd01383 232 KEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAID 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 416 AVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIMEQEEY 495
Cdd:cd01383 312 ARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 496 KREGIEWNFIDFgLDLQPCIELIERpnNPPGILALLDEECWFPKATDTTFVEKLMNTHSAHAKFskpKQHKDKLmFTVLH 575
Cdd:cd01383 392 ELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCF---KGERGGA-FTIRH 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 576 YAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKdvdrvvgldTINKMSQSSVPTSTKSKKG-MFRTVGQLYK 654
Cdd:cd01383 465 YAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFAS---------KMLDASRKALPLTKASGSDsQKQSVATKFK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 655 ESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILaAGSIPK 734
Cdd:cd01383 536 GQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFL-LPEDVS 614
|
650 660 670
....*....|....*....|....*....|...
gi 1343958102 735 GFMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd01383 615 ASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
96-767 |
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: 618.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTG 175
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 176 ESGAGKTENTKKVIQYLAVIASSHKpkkdinpgELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVGA 255
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS--------WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 256 FIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFL-MGGHVEIPGLQDDELFEETLEAMEIMGF 334
Cdd:cd01381 153 KIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLtQGNCLTCEGRDDAAEFADIRSAMKVLMF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 335 TQEERLGMLKVVSTVLQLGNIRFE-KERNNEQAT-MPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQTKQQ 412
Cdd:cd01381 233 TDEEIWDIFKLLAAILHLGNIKFEaTVVDNLDASeVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 413 ADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFL--GILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIM 490
Cdd:cd01381 313 ALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSRTsiGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 491 EQEEYKREGIEWNFIDFgLDLQPCIELI-ERPNNppgILALLDEECWFPKATDTTFVEKLMNTHSAHAKFSKPKQHKDKL 569
Cdd:cd01381 393 EQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNTS 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 570 mFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWkDVDRVVGLDTINKMSqssvptstkskkgmfrTV 649
Cdd:cd01381 469 -FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLF-NEDISMGSETRKKSP----------------TL 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 650 GQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAA 729
Cdd:cd01381 531 SSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVP 610
|
650 660 670
....*....|....*....|....*....|....*...
gi 1343958102 730 GSIPKGFMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd01381 611 GIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
96-767 |
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 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCT 174
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 175 GESGAGKTENTKKVIQYLAviassHKPKKDINPGE-LEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLV 253
Cdd:cd01384 81 GESGAGKTETTKMLMQYLA-----YMGGRAVTEGRsVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRIS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 254 GAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFLMGGH-VEIPGLQDDELFEETLEAMEIM 332
Cdd:cd01384 156 GAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKcFELDGVDDAEEYRATRRAMDVV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 333 GFTQEERLGMLKVVSTVLQLGNIRFEKERNNEQATMPDNTAAQ--KVC-HLQGINVTDFSRAILTPKIKVGREVVQKAQT 409
Cdd:cd01384 236 GISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFhlKAAaELLMCDEKALEDALCKRVIVTPDGIITKPLD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 410 KQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRqSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFI 489
Cdd:cd01384 316 PDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPN-SKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 490 MEQEEYKREGIEWNFIDFgLDLQPCIELIERpnNPPGILALLDEECWFPKATDTTFVEKLMNTHSAHAKFSKPKqhKDKL 569
Cdd:cd01384 395 MEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPK--LSRT 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 570 MFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDVDRvvgldtinkmsqssvptSTKSKKGMFRTV 649
Cdd:cd01384 470 DFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR-----------------EGTSSSSKFSSI 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 650 GQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAA 729
Cdd:cd01384 533 GSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAP 612
|
650 660 670
....*....|....*....|....*....|....*...
gi 1343958102 730 gSIPKGFMDGKQACGLMVKHLDLDPnlYRIGQSKMFFR 767
Cdd:cd01384 613 -EVLKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
96-767 |
1.09e-176 |
|
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: 552.24 E-value: 1.09e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCT 174
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 175 GESGAGKTENTKKVIQYLAVIASSHKpkkdinpGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVG 254
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSGA-------GPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 255 AFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLledfnsysflmgghvEIPGLQDDELFEETLEAMEIMGF 334
Cdd:cd01382 154 GFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL---------------KDPLLDDVGDFIRMDKAMKKIGL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 335 TQEERLGMLKVVSTVLQLGNIRFEKERNNEQAT---MPDNTAAQKVC-HLQGINVTDF-----SRAILTPKIKVGREVVQ 405
Cdd:cd01382 219 SDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGGcnvKPKSEQSLEYAaELLGLDQDELrvsltTRVMQTTRGGAKGTVIK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 406 KAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKrqSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNH 485
Cdd:cd01382 299 VPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 486 TMFIMEQEEYKREGIEWNFIDFgLDLQPCIELIERPNNppGILALLDEECWFPKATDTTFVEKLMNTHSAHAKF-----S 560
Cdd:cd01382 377 RILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLsiprkS 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 561 KPKQHK---DKLMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKdvdrvvgldtinkmSQSSVPT 637
Cdd:cd01382 454 KLKIHRnlrDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFE--------------SSTNNNK 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 638 STKSKKG--MFRTVGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRI 715
Cdd:cd01382 520 DSKQKAGklSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRT 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1343958102 716 VFQEFRQRYEILAAGSIPKgfMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
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 ... |
96-767 |
2.00e-175 |
|
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: 548.61 E-value: 2.00e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTG 175
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 176 ESGAGKTENTKKVIQYLAVIASShkpkkdinPGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVGA 255
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGS--------TNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 256 FIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELllEDFNSYSFL-MGGHVEIPGLQDDELFEETLEAMEIMGF 334
Cdd:cd14872 153 STENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGW--GSSAAYGYLsLSGCIEVEGVDDVADFEEVVLAMEQLGF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 335 TQEERLGMLKVVSTVLQLGNIRFEKE---RNNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKV-GREVVQKAQTK 410
Cdd:cd14872 231 DDADINNVMSLIAAILKLGNIEFASGggkSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMEIkGCDPTRIPLTP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 411 QQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIM 490
Cdd:cd14872 311 AQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 491 EQEEYKREGIEWNFIDFgLDLQPCIELIErpNNPPGILALLDEECWFPKATDTTFVEKLMNTHSAHAKFSKPKQHKDKLM 570
Cdd:cd14872 391 EEALYQSEGVKFEHIDF-IDNQPVLDLIE--KKQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVRTSRTE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 571 FTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWkdvdrvvgldtinkmsqssvPTSTKSKKGMFRTVG 650
Cdd:cd14872 468 FIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF--------------------PPSEGDQKTSKVTLG 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 651 QLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAg 730
Cdd:cd14872 528 GQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVK- 606
|
650 660 670
....*....|....*....|....*....|....*...
gi 1343958102 731 SIPKGFM-DGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd14872 607 TIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
96-767 |
3.80e-174 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 545.53 E-value: 3.80e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQ----DREDQS 170
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 171 ILCTGESGAGKTENTKKVIQYLAVIASSHKPKKDIN-----------PGELEKQLLQANPILEAFGNAKTIKNDNSSRFG 239
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEgeaaseaieqtLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 240 KFIKLNFDVSGCLVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFLMGGHVEIPGLQDD 319
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 320 ELFEETLEAMEIMGFTQEERLGMLKVVSTVLQLGNIRFEKERNNEQATmpDNTAAQ---KVCHLQGINVTDFSRAILTPK 396
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQslkLAAELLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 397 IKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLdKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTN 476
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTI-SSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 477 ERLQQLFNHTMFIMEQEEYKREGIEWNFIDFGlDLQPCIELIE-RPNNPPGILALLDeECWFPKAT--DTTFVEKLMNTH 553
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLHASF 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 554 -------------SAHAKFSKPKQHKDKLmFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSgfiqdlwkdvdr 620
Cdd:cd14890 476 grksgsggtrrgsSQHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRR------------ 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 621 vvgldTINKMSqssvptstkskkgmfrtVGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGV 700
Cdd:cd14890 543 -----SIREVS-----------------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGM 600
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1343958102 701 LEGIRICRQGFPNRIVFQEFRQRYEILAAGSipkgfMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd14890 601 MEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
96-767 |
7.86e-172 |
|
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: 539.34 E-value: 7.86e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTG 175
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 176 ESGAGKTENTKKVIQYLAVIASShkpkkdiNPGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDvSGCLVGA 255
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQR-------RNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 256 FIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFL-MGGHVEIPGLQDDELFEETLEAMEIMGF 334
Cdd:cd01387 153 ITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLnQGGNCEIAGKSDADDFRRLLAAMQVLGF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 335 TQEERLGMLKVVSTVLQLGNIRFEK---ERNNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQTKQ 411
Cdd:cd01387 233 SSEEQDSIFRILASVLHLGNVYFHKrqlRHGQEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTID 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 412 QADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSfLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIME 491
Cdd:cd01387 313 QALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLS-IAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 492 QEEYKREGIEWNFIDFgLDLQPCIELIERpnNPPGILALLDEECWFPKATDTTFVEKLMNTHSAHAKFSKPKQHKDKlmF 571
Cdd:cd01387 392 QEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRMPLPE--F 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 572 TVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDVDRVVGLDTINKMSQSSVPTSTKSKkgmfrTVGQ 651
Cdd:cd01387 467 TIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDKAPPRLGKGRFVTMKPRTP-----TVAA 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 652 LYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAGS 731
Cdd:cd01387 542 RFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALK 621
|
650 660 670
....*....|....*....|....*....|....*..
gi 1343958102 732 IPKGfMDGKQACGLMVKHLDLDP-NLYRIGQSKMFFR 767
Cdd:cd01387 622 LPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
96-736 |
2.76e-171 |
|
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: 538.12 E-value: 2.76e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYKgKKRHEVPPHIYSITDNAYRNMLQDREDQSILCT 174
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 175 GESGAGKTENTKKVIQYLAVIASSHKPKKDInpgeLEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFD------- 247
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRSL----VEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSklkskrm 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 248 --VSGCLVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKG--------KMRDELL------------LEDFNSYSF 305
Cdd:cd14888 156 sgDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREakntglsyEENDEKLakgadakpisidMSSFEPHLK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 306 LMG----GHVEIPGLQDDELFEETLEAMEIMGFTQEERLGMLKVVSTVLQLGNIRFEKERNNEQATMPDNTAAQ---KVC 378
Cdd:cd14888 236 FRYltksSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDdleKVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 379 HLQGINVTDFSRAILTPKIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAG 458
Cdd:cd14888 316 SLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGVLDIFG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 459 FEIFEDNSFEQLCINYTNERLQQLFNHTMFIMEQEEYKREGIEWNFIDFGlDLQPCIELIErpNNPPGILALLDEECWFP 538
Cdd:cd14888 396 FECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFCMLDEECFVP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 539 KATDTTFVEKLMNTHSAHAKFSKPKqhKDKLMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLwkdv 618
Cdd:cd14888 473 GGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNL---- 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 619 drvvgldtINKMSQSSVPTSTKSKKgmFRTVGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCN 698
Cdd:cd14888 547 --------FSAYLRRGTDGNTKKKK--FVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYG 616
|
650 660 670
....*....|....*....|....*....|....*...
gi 1343958102 699 GVLEGIRICRQGFPNRIVFQEFRQRYEILAAGSIPKGF 736
Cdd:cd14888 617 GVLQAVQVSRAGYPVRLSHAEFYNDYRILLNGEGKKQL 654
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
96-767 |
1.23e-169 |
|
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: 532.34 E-value: 1.23e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKK-RHEVPPHIYSITDNAYRNMLQDREDQSILCT 174
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 175 GESGAGKTENTKKVIQYLAVIASSHKPkkdinpgELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVG 254
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDDS-------DLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 255 AFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKgkmRDELL---LEDFNSYSFLMGGHVEIPGLQDDE-------LFEE 324
Cdd:cd14897 154 AKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMS---RDRLLyyfLEDPDCHRILRDDNRNRPVFNDSEeleyyrqMFHD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 325 TLEAMEIMGFTQEERLGMLKVVSTVLQLGNIRFEKERNNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVV 404
Cdd:cd14897 231 LTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 405 QKAQTKQQADFAVEALAKAMYERLFRWILARVNKTL----DKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQ 480
Cdd:cd14897 311 QSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 481 QLFNHTMFIMEQEEYKREGIEWNFIDFGlDLQPCIELIERpnNPPGILALLDEECWFPKATDTTFVEKLMNTHSAHAKFS 560
Cdd:cd14897 391 QYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYV 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 561 KPKQhkDKLMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKdvdrvvgldtinkmsqssvptstk 640
Cdd:cd14897 468 ASPG--NRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT------------------------ 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 641 skkgmfrtvgQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEF 720
Cdd:cd14897 522 ----------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDF 591
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1343958102 721 RQRYEILAAGSiPKGFMDGKQACGLMVKHLDLDPnlYRIGQSKMFFR 767
Cdd:cd14897 592 VKRYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
96-767 |
1.79e-168 |
|
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: 531.18 E-value: 1.79e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTG 175
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 176 ESGAGKTENTKKVIQYLavIASSHKpkkDINPGeLEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVGA 255
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQK---GYGSG-VEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 256 FIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFLMGGHVEIpgLQDDEL---FEETLEAMEIM 332
Cdd:cd01385 155 VVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYT--LEGEDEkyeFERLKQAMEMV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 333 GFTQEERLGMLKVVSTVLQLGNIRFEKERNN--EQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQTK 410
Cdd:cd01385 233 GFLPETQRQIFSVLSAVLHLGNIEYKKKAYHrdESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 411 QQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSS---FLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTM 487
Cdd:cd01385 313 PEAIATRDAMAKCLYSALFDWIVLRINHALLNKKDLEEAkglSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 488 FIMEQEEYKREGIEWNFIDFgLDLQPCIELIERpnNPPGILALLDEECWFPKATDTTFVEKLMNTHSAHAKFSKPKqhKD 567
Cdd:cd01385 393 FKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQ--VM 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 568 KLMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDL----------WK---------DVDRVVGLDTIN 628
Cdd:cd01385 468 EPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELigidpvavfrWAvlrafframAAFREAGRRRAQ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 629 KMSQSSVPTSTKSKKGMFR--------TVGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGV 700
Cdd:cd01385 548 RTAGHSLTLHDRTTKSLLHlhkkkkppSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGM 627
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1343958102 701 LEGIRICRQGFPNRIVFQEFRQRYEILaagsIPKGFMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd01385 628 LETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
96-765 |
1.94e-166 |
|
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: 524.35 E-value: 1.94e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMY------KGKKRHEVPPHIYSITDNAYRNMLQDRE-- 167
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 168 --DQSILCTGESGAGKTENTKKVIQYLAVIASSHKPKKDINPGE-LEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKL 244
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATEREnVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 245 NFDVSGCLVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFL--MGGHVEIPGLQDDELF 322
Cdd:cd14901 161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQCYDRRDGVDDSVQY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 323 EETLEAMEIMGFTQEERLGMLKVVSTVLQLGNIRF-EKERNNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGR 401
Cdd:cd14901 241 AKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 402 EVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLD-KSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQ 480
Cdd:cd14901 321 EYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAySESTGASRFIGIVDIFGFEIFATNSLEQLCINFANEKLQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 481 QLFNHTMFIMEQEEYKREGIEWNFIDFgldlqP----CIELIERpnNPPGILALLDEECWFPKATDTTFVEKLMNTHSAH 556
Cdd:cd14901 401 QLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFEA--RPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 557 AKFSKPKQHKDKLMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFiqdlwkdvdrvvgldtinkmsqssVP 636
Cdd:cd14901 474 ASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAF------------------------LS 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 637 TSTKSKkgmfrtvgqlYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIV 716
Cdd:cd14901 530 STVVAK----------FKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFP 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1343958102 717 FQEFRQRYEILAAGSIPKGFMDGKQACGLMVKH-----LDLDPNLYRIGQSKMF 765
Cdd:cd14901 600 HDAFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselNIEHLPPFQVGKTKVF 653
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
96-767 |
3.25e-166 |
|
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: 523.96 E-value: 3.25e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCT 174
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 175 GESGAGKTENTKKVIQYLAVIASshkpkkDINPGELEKqLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVG 254
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG------GLNDSTIKK-IIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 255 AFIDTYLLEKSRCIRQANTERAFHIFYYMVSGakGKMRDELLLEDFNSYSFLMGGHV-EIPGLQDDELFEETLEAMEIMG 333
Cdd:cd14903 154 AKCRTYLLEKTRVISHERPERNYHIFYQLLAS--PDVEERLFLDSANECAYTGANKTiKIEGMSDRKHFARTKEALSLIG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 334 FTQEERLGMLKVVSTVLQLGNIRFEKERNNEQATM--PDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQTKQ 411
Cdd:cd14903 232 VSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 412 QADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSfLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIME 491
Cdd:cd14903 312 QAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANH-IGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 492 QEEYKREGIEWNFIDFgLDLQPCIELIErpnNPPGILALLDEECWFPKATDTTFVEKLMNTHSAHAKFSK-PKQHKDKlm 570
Cdd:cd14903 391 QIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEfPRTSRTQ-- 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 571 FTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKdvdrvVGLDTINKMSQSSVPTSTKSKKGMF--RT 648
Cdd:cd14903 465 FTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFK-----EKVESPAAASTSLARGARRRRGGALttTT 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 649 VGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILa 728
Cdd:cd14903 540 VGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLF- 618
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1343958102 729 agsIPKGF---MDGKQACGLMVKHLDLD-PNLYRIGQSKMFFR 767
Cdd:cd14903 619 ---LPEGRntdVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
96-767 |
1.33e-165 |
|
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: 522.40 E-value: 1.33e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEV---PPHIYSITDNAYRNMLQDR----ED 168
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 169 QSILCTGESGAGKTENTKKVIQYLAVI----ASSHKPKKDINPGE-LEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIK 243
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATAsklaKGASTSKGAANAHEsIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 244 LNFDVSGCLVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFLMGGH-VEIPGLQDDELF 322
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNcVEVDGVDDATEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 323 EETLEAMEIMGFTQEERLGMLKVVSTVLQLGNIRFEKERNNEQ--ATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVG 400
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDvfAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTSTA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 401 R-EVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNK---------TLDKSKRQSSSFLGILDIAGFEIFEDNSFEQL 470
Cdd:cd14892 321 RgSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINAchkqqtsgvTGGAASPTFSPFIGILDIFGFEIMPTNSFEQL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 471 CINYTNERLQQLFNHTMFIMEQEEYKREGIEWNFIDFGlDLQPCIELIERPnnPPGILALLDEECWFP-KATDTTFVEKL 549
Cdd:cd14892 401 CINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDKQLLTIY 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 550 MNTHSA-HAKFSKPKQHKDKlmFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSgfiqdlwkdvdrvvgldtin 628
Cdd:cd14892 478 HQTHLDkHPHYAKPRFECDE--FVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK-------------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 629 kmsqssvptstkskkgmFRTvgqlykeSLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICR 708
Cdd:cd14892 536 -----------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRR 591
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1343958102 709 QGFPNRIVFQEFRQRYEILAAGSI--------PKGFMDGKQACGLMVKHldLDPNLYRIGQSKMFFR 767
Cdd:cd14892 592 EGFPIRRQFEEFYEKFWPLARNKAgvaaspdaCDATTARKKCEEIVARA--LERENFQLGRTKVFLR 656
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
97-767 |
3.41e-163 |
|
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: 514.90 E-value: 3.41e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTGE 176
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 177 SGAGKTENTKKVIQYLAVIASShkpkkdiNPGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVGAF 256
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLGKA-------NNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 257 IDTYLLEKSRCIRQANTERAFHIFYYMVSG--AKGKMRDELLLEDFNSYSFLMGGHVEIPGLQDD---ELFEETLEAMEI 331
Cdd:cd01379 155 ISEYLLEKSRVVHQAIGERNFHIFYYIYAGlaEDKKLAKYKLPENKPPRYLQNDGLTVQDIVNNSgnrEKFEEIEQCFKV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 332 MGFTQEERLGMLKVVSTVLQLGNIRFEKERNNEQ----ATMPDNTAAQKVCHLQGINVTDFSRAiLTPKIKVGR-EVVQK 406
Cdd:cd01379 235 IGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEA-LTSHSVVTRgETIIR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 407 AQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFL--GILDIAGFEIFEDNSFEQLCINYTNERLQQLFN 484
Cdd:cd01379 314 NNTVEEATDARDAMAKALYGRLFSWIVNRINSLLKPDRSASDEPLsiGILDIFGFENFQKNSFEQLCINIANEQIQYYFN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 485 HTMFIMEQEEYKREGIEWNFIDFG-----LDLqpcieLIERPNnppGILALLDEECWFPKATDTTFVEKLMNtHSAHAKF 559
Cdd:cd01379 394 QHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPM---GLLALLDEESRFPKATDQTLVEKFHN-NIKSKYY 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 560 SKPKqhKDKLMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSsgfiqdlwkdvdrvvgldtiNKMSQSSVPTSt 639
Cdd:cd01379 465 WRPK--SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSE--------------------NPLVRQTVATY- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 640 kskkgmFRTvgqlykeSLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQE 719
Cdd:cd01379 522 ------FRY-------SLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFAD 588
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1343958102 720 FRQRYEILAAGSIPKGFMDgKQACGLMVKHLDLDPnlYRIGQSKMFFR 767
Cdd:cd01379 589 FLKRYYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
96-767 |
8.65e-163 |
|
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: 514.34 E-value: 8.65e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCT 174
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 175 GESGAGKTENTKKVIQYLAVIA-SSHKPKKDINPGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLV 253
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISqQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 254 GAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFL-MGGHVEIPGLQDDELFEETLEAMEIM 332
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLnQSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 333 GFTQEERLGMLKVVSTVLQLGNIRFekeRNNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQTKQQ 412
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEF---ITAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 413 ADFAVEALAKAMYERLFRWILARVNKTLdkSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIMEQ 492
Cdd:cd14873 318 AVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 493 EEYKREGIEWNFIDFgLDLQPCIELIERpnnPPGILALLDEECWFPKATDTTFVEKLMNTHSAHAKFSKPKQHKDklMFT 572
Cdd:cd14873 396 LEYSREGLVWEDIDW-IDNGECLDLIEK---KLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVN--NFG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 573 VLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDVDrvvgldtiNKMSQSSVPTSTKSKKgmfRTVGQL 652
Cdd:cd14873 470 VKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVS--------SRNNQDTLKCGSKHRR---PTVSSQ 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 653 YKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAGSI 732
Cdd:cd14873 539 FKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLA 618
|
650 660 670
....*....|....*....|....*....|....*
gi 1343958102 733 PKGFMDGKqaCGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd14873 619 LPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
98-767 |
4.66e-151 |
|
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: 482.48 E-value: 4.66e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 98 VLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNML----QDREDQSILC 173
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 174 TGESGAGKTENTKKVIQYLAVIASSHKpkkdinpgELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDvSGCLV 253
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELCRGNS--------QLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHVK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 254 GAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFLMGGH-----VEIPGLQDDELfeetLEA 328
Cdd:cd14889 154 GAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAgckreVQYWKKKYDEV----CNA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 329 MEIMGFTQEERLGMLKVVSTVLQLGNIRFEKERNNEQATMPDNTAAQKVCHLQ-GINVTDFSRAiLTPKIKVGR-EVVQK 406
Cdd:cd14889 230 MDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEALKVENDSNGWLKAAAGQfGVSEEDLLKT-LTCTVTFTRgEQIQR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 407 AQTKQQADFAVEALAKAMYERLFRWILARVNKTLdKSKRQSSSFL---GILDIAGFEIFEDNSFEQLCINYTNERLQQLF 483
Cdd:cd14889 309 HHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL-APKDDSSVELreiGILDIFGFENFAVNRFEQACINLANEQLQYFF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 484 NHTMFIMEQEEYKREGIEWNFIDFgLDLQPCIELIerPNNPPGILALLDEECWFPKATDTTFVEKLMNTHSAHAKFSKPK 563
Cdd:cd14889 388 NHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLF--LNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYYGKSR 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 564 QHKDKlmFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWK-DVDRVVGLDTINKMSQSSVPTSTKSK 642
Cdd:cd14889 465 SKSPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTaTRSRTGTLMPRAKLPQAGSDNFNSTR 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 643 KgmfRTVGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 722
Cdd:cd14889 543 K---QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAE 619
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1343958102 723 RYEILAagsIPKGFMDGKQACGLMVKHLDLDPnlYRIGQSKMFFR 767
Cdd:cd14889 620 RYKILL---CEPALPGTKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
96-727 |
3.08e-149 |
|
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: 477.99 E-value: 3.08e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYKGKKRH--------EVPPHIYSITDNAYRNMLQDR 166
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 167 EDQSILCTGESGAGKTENTKKVIQYLAVIaSSHKPKKDINPGE-------------LEKQLLQANPILEAFGNAKTIKND 233
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQL-SQQEQNSEEVLTLtssiratskstksIEQKILSCNPILEAFGNAKTVRND 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 234 NSSRFGKFIKLNFD-VSGCLVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLED----FNSYSFLMG 308
Cdd:cd14907 160 NSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNqlsgDRYDYLKKS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 309 GHVEIPGLQDDELFEETLEAMEIMGFTQEERLGMLKVVSTVLQLGNIRFEKER--NNEQATMPDNTAAQKVCHLQGINVT 386
Cdd:cd14907 240 NCYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 387 DFSRAILTPKIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTL-------DKSKRQSSSFLGILDIAGF 459
Cdd:cd14907 320 ELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 460 EIFEDNSFEQLCINYTNERLQQLFNHTMFIMEQEEYKREGIE--WNFIDFgLDLQPCIELIErpNNPPGILALLDEECWF 537
Cdd:cd14907 400 EVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLD--KPPIGIFNLLDDSCKL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 538 PKATDTTFVEKLMNTHSAHAKFSKPKqHKDKLMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKD 617
Cdd:cd14907 477 ATGTDEKLLNKIKKQHKNNSKLIFPN-KINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSG 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 618 VDRvvgldtinkmSQSSVPTSTKSKKGMFRTVGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRC 697
Cdd:cd14907 556 EDG----------SQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRY 625
|
650 660 670
....*....|....*....|....*....|
gi 1343958102 698 NGVLEGIRICRQGFPNRIVFQEFRQRYEIL 727
Cdd:cd14907 626 LGVLESIRVRKQGYPYRKSYEDFYKQYSLL 655
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
97-733 |
1.99e-138 |
|
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: 446.29 E-value: 1.99e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMY-----------KGKKRHEVPPHIYSITDNAYRNM-- 162
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 163 --LQDREDQSILCTGESGAGKTENTKKVIQYLAVIASSHKPKK---DINPGELEKQLLQANPILEAFGNAKTIKNDNSSR 237
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASvsmGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 238 FGKFIKLNFDVSGCLVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKgkmrdellledfnsysflmgghveiPGLQ 317
Cdd:cd14900 162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGAS-------------------------EAAR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 318 DDELFEETLEAMEIMGFTQEERLGMLKVVSTVLQLGNIRFEKERNNE-QATMPDNTAAQKV------CHLQGINVTDFSR 390
Cdd:cd14900 217 KRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLSVDATKLEK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 391 AILTPKIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVN---KTLDKSKRQSSS-FLGILDIAGFEIFEDNS 466
Cdd:cd14900 297 ALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNaflKMDDSSKSHGGLhFIGILDIFGFEVFPKNS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 467 FEQLCINYTNERLQQLFNHTMFIMEQEEYKREGIEWNFIDFGlDLQPCIELIERpnNPPGILALLDEECWFPKATDTTFV 546
Cdd:cd14900 377 FEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLISQ--RPTGILSLIDEECVMPKGSDTTLA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 547 EKLMNTHSAHAKFSKPKQHKDKLMFTVLHYAGKVDYNAADWLTKNMDPLNDNVtallnnsssgfiqdlwkdVDrvvgldt 626
Cdd:cd14900 454 SKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKDVLHQEA------------------VD------- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 627 inkmsqssvptstkskkgMFRTVGQlYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRI 706
Cdd:cd14900 509 ------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRV 569
|
650 660
....*....|....*....|....*..
gi 1343958102 707 CRQGFPNRIVFQEFRQRYEILAAGSIP 733
Cdd:cd14900 570 ARAGFPIRLLHDEFVARYFSLARAKNR 596
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
96-767 |
8.68e-137 |
|
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: 442.18 E-value: 8.68e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERyfSSLI----YTYSGLFCVVVNPYKMLPiysEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDRE---D 168
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 169 QSILCTGESGAGKTENTKKVIQYL---AVIASSHKP--------KKDINPGELEKQLLQANPILEAFGNAKTIKNDNSSR 237
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLttrAVGGKKASGqdieqsskKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 238 FGKFIKLNFDVSGC-LVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFL-MGGHVEIPG 315
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLnQSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 316 LQDDELFEETLEAMEIMGFTQEERLGMLKVVSTVLQLGNIRFEKERNNE----QATMPDNTAAQKVCHLQGINVTDFSRA 391
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEgeaeIASESDKEALATAAELLGVDEEALEKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 392 ILTPKIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKsKRQSSSFLGILDIAGFEIFE-DNSFEQL 470
Cdd:cd14891 316 ITQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFEtKNDFEQL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 471 CINYTNERLQQLFNHTMFIMEQEEYKREGIEWNFIDFGlDLQPCIELI-ERPNnppGILALLDEECWFPKATDTTFVEKL 549
Cdd:cd14891 395 LINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPN---GILPLLDNEARNPNPSDAKLNETL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 550 MNTHSAHAKFSKPKQHKDKLMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSssgfiqdlwkdvdrvvgldtink 629
Cdd:cd14891 471 HKTHKRHPCFPRPHPKDMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS----------------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 630 msqssvptstkskkgmfrtvgQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQ 709
Cdd:cd14891 528 ---------------------AKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKV 586
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1343958102 710 GFPNRIVFQEFRQRYEILAAGSIPKGFmdGKQACGL---MVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd14891 587 GLPTRVTYAELVDVYKPVLPPSVTRLF--AENDRTLtqaILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
96-767 |
2.16e-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: 435.91 E-value: 2.16e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYK-MLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCT 174
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKwIDNLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 175 GESGAGKTENTKKVIQYLAVIASSHKPKKdinpgelEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVG 254
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKDKT-------IAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 255 AFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFLMGG--HVEIPGLQDDELFEETLEAMEIM 332
Cdd:cd14904 154 AKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSlaQMQIPGLDDAKLFASTQKSLSLI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 333 GFTQEERLGMLKVVSTVLQLGNIRFEKERNNEQAtMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQTKQQ 412
Cdd:cd14904 234 GLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSR-ISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 413 ADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIMEQ 492
Cdd:cd14904 313 AEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 493 EEYKREGIEWNFIDFGlDLQPCIELIErpnNPPGILALLDEECWFPKATDTTFVEKLMNTHSA-----HAKFSKPKQHKd 567
Cdd:cd14904 393 EEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIRTNHQTkkdneSIDFPKVKRTQ- 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 568 klmFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDVDrvvgLDTINKMSQSSvpTSTKSKKgmfr 647
Cdd:cd14904 468 ---FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE----APSETKEGKSG--KGTKAPK---- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 648 TVGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 727
Cdd:cd14904 535 SLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIM 614
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1343958102 728 AAGSIPKGfmDGKQACGLMVKHLDL-DPNLYRIGQSKMFFR 767
Cdd:cd14904 615 FPPSMHSK--DVRRTCSVFMTAIGRkSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
96-724 |
5.72e-134 |
|
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: 437.02 E-value: 5.72e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYK--------GKKRHEVPPHIYSITDNAYRNMLQ-D 165
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 166 REDQSILCTGESGAGKTENTKKVIQYLAVIAS--SHKPKKDINPGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIK 243
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRdqSSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 244 LNFDVSGCLVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFLMG---GHVEIPGLQDD- 319
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSygpSFARKRAVADKy 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 320 -ELFEETLEAMEIMGFTQEERLGMLKVVSTVLQLGNIRFEKERNNEQATMPDNTAA---QKVCHLQGINVTDFSRAILTP 395
Cdd:cd14902 241 aQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRfhlAKCAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 396 KIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLD--------KSKRQSSSFLGILDIAGFEIFEDNSF 467
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFESLNRNGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 468 EQLCINYTNERLQQLFNHTMFIMEQEEYKREGIEWNFIDFGlDLQPCIELIErpNNPPGILALLDEECWFPKATDTTFVE 547
Cdd:cd14902 401 EQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFD--DKSNGLFSLLDQECLMPKGSNQALST 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 548 KLMNTHSAHAKfskpkqhkdklmFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSgfiqdlwkdvDRVVGLDTI 627
Cdd:cd14902 478 KFYRYHGGLGQ------------FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSN----------EVVVAIGAD 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 628 NKMSQSSVPTSTKSKK--GMFRT--VGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEG 703
Cdd:cd14902 536 ENRDSPGADNGAAGRRrySMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEA 615
|
650 660
....*....|....*....|.
gi 1343958102 704 IRICRQGFPNRIVFQEFRQRY 724
Cdd:cd14902 616 VRIARHGYSVRLAHASFIELF 636
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
96-753 |
7.59e-132 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 429.71 E-value: 7.59e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYK--GKKRHE-------VPPHIYSITDNAYRNMLQD- 165
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 166 REDQSILCTGESGAGKTENTKKVIQYLAVIASSHKPKKDINpGELEK-----QLLQANPILEAFGNAKTIKNDNSSRFGK 240
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEG-EELGKlsimdRVLQSNPILEAFGNARTLRNDNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 241 FIKLNFDVSGCLVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDF--------NSYSFL-MGGHV 311
Cdd:cd14908 160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGitgglqlpNEFHYTgQGGAP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 312 EIPGLQDDELFEETLEAMEIMGFTQEERLGMLKVVSTVLQLGNIRFEKERNN---EQATMPDNTAAQKVCHLQGINVTDF 388
Cdd:cd14908 240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDgaaEIAEEGNEKCLARVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 389 SRAILTPKIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQS-SSFLGILDIAGFEIFEDNSF 467
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDiRSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 468 EQLCINYTNERLQQLFNHTMFIMEQEEYKREGIEWNFIDFGlDLQPCIELIERPnnPPGILALLDEECWFP-KATDTTFV 546
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQAK--KKGILTMLDDECRLGiRGSDANYA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 547 EKLMN--------THSAHAKFSKPKQHKDKLMFTVLHYAGKVDYNA-ADWLTKNMDPLndnvtallnnsssgfiqdlwkd 617
Cdd:cd14908 477 SRLYEtylpeknqTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVeTTFCEKNKDEI---------------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 618 vdrvvgldtinkmsqssvPTSTKSkkgMFRTvGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRC 697
Cdd:cd14908 535 ------------------PLTADS---LFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRY 592
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 698 NGVLEGIRICRQGFPNRIVFQEFRQRYEILAAgSIPK----GFMDGKQACGLMVKHLDLD 753
Cdd:cd14908 593 GGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlsWSMERLDPQKLCVKKMCKD 651
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
46-824 |
3.55e-131 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 432.53 E-value: 3.55e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 46 ASIREEKGEQVLVELSNGQKVTVSKDDIQKMNPP-KFSKVEDMAALTFLNEASVLQNLRERYFSSLIYTYSGLFCVVVNP 124
Cdd:PTZ00014 59 PGSTGEKLTLKQIDPPTNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 125 YKMLPIYSEKIIEMYKGKKRHE-VPPHIYSITDNAYRNMLQDREDQSILCTGESGAGKTENTKKVIQYLAviaSShkpKK 203
Cdd:PTZ00014 139 FKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFA---SS---KS 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 204 DINPGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVGAFIDTYLLEKSRCIRQANTERAFHIFYYM 283
Cdd:PTZ00014 213 GNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 284 VSGAKGKMRDELLLEDFNSYSFLMGGHVEIPGLQDDELFEETLEAMEIMGFTQEERLGMLKVVSTVLQLGNIRFE-KERN 362
Cdd:PTZ00014 293 LKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEgKEEG 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 363 ---NEQATMPDNTAA-QKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNK 438
Cdd:PTZ00014 373 gltDAAAISDESLEVfNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNA 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 439 TLDKSKrQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIMEQEEYKREGIEWNFIDFgLDLQPCIELI 518
Cdd:PTZ00014 453 TIEPPG-GFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLL 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 519 ERPNNppGILALLDEECWFPKATDTTFVEKLMNTHSAHAKFSKPKQHKDKlMFTVLHYAGKVDYNAADWLTKNMDPLNDN 598
Cdd:PTZ00014 531 CGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKVDSNK-NFVIKHTIGDIQYCASGFLFKNKDVLRPE 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 599 VTALLNNSSSGFIQDLWKDVdrvvgldtinkmsqssVPTSTKSKKGMFrtVGQLYKESLGKLMATLHNTQPNFVRCIIPN 678
Cdd:PTZ00014 608 LVEVVKASPNPLVRDLFEGV----------------EVEKGKLAKGQL--IGSQFLNQLDSLMSLINSTEPHFIRCIKPN 669
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 679 HEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAGSIPKGFMDGKQACGLMVKHLDLDPNLYR 758
Cdd:PTZ00014 670 ENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYA 749
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1343958102 759 IGQSKMFF-RTGV--LAQLEEERDLKLTVVIIAFQARALGFLGRKAFSKRqqqltaMKVIQRNCAcYLR 824
Cdd:PTZ00014 750 IGKTMVFLkKDAAkeLTQIQREKLAAWEPLVSVLEALILKIKKKRKVRKN------IKSLVRIQA-HLR 811
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
102-767 |
3.89e-130 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 425.91 E-value: 3.89e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 102 LRERYFSSLIYTYSGLFCVVVNPYKMLPiysekiiEMYKGKKRHE-------VPPHIYSITDNAYRNMLQ-------DRE 167
Cdd:cd14895 7 LAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhepgaSKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 168 DQSILCTGESGAGKTENTKKVIQYLAVIA------SSHKPKKDINPGELekqlLQANPILEAFGNAKTIKNDNSSRFGKF 241
Cdd:cd14895 80 NQTILVSGESGAGKTETTKFIMNYLAESSkhttatSSSKRRRAISGSEL----LSANPILESFGNARTLRNDNSSRFGKF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 242 IKLNF-----DVSGCLVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNS--YSFLMGG--HVE 312
Cdd:cd14895 156 VRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAqeFQYISGGqcYQR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 313 IPGLQDDELFEETLEAMEIMGFTQEERLGMLKVVSTVLQLGNIRFEKERNNE---------------QATMPDNTAAQK- 376
Cdd:cd14895 236 NDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSSLTVQQHl 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 377 --VCHLQGINVTDFSRAILTPKIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSK---------- 444
Cdd:cd14895 316 diVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQfalnpnkaan 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 445 RQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIMEQEEYKREGIEWNFIDFGLDlQPCIELIERpnNP 524
Cdd:cd14895 396 KDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLEQ--RP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 525 PGILALLDEECWFPKATDTTFVEKLMNTHSAHAKFSKPKQHKDKLMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLN 604
Cdd:cd14895 473 SGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASRTDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLG 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 605 NSSSGFIQDLWKDVDRVVGldtiNKMSQSSVPTSTKSKKGMFRTVGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAG 684
Cdd:cd14895 553 KTSDAHLRELFEFFKASES----AELSLGQPKLRRRSSVLSSVGIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASD 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 685 KMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAGSIPKGFMDGKQACGLMVKHLDLdpnlyriGQSKM 764
Cdd:cd14895 629 QFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASALIETLKVDHAEL-------GKTRV 701
|
...
gi 1343958102 765 FFR 767
Cdd:cd14895 702 FLR 704
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
96-767 |
5.21e-129 |
|
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: 420.34 E-value: 5.21e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTG 175
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 176 ESGAGKTENTKKVIQYLaviaSSHKPKKDINPGeleKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDvSGCLVGA 255
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL----SSLYQDQTEDRL---RQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 256 FIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFL-MGGHVEIPGLQDDELFEETLEAMEIMGF 334
Cdd:cd14896 153 SVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLnQGGACRLQGKEDAQDFEGLLKALQGLGL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 335 TQEERLGMLKVVSTVLQLGNIRF---EKErNNEQATMPDNTAAQKVCHLQGINvTDFSRAILTPKIKV---GRevVQKAQ 408
Cdd:cd14896 233 CAEELTAIWAVLAAILQLGNICFsssERE-SQEVAAVSSWAEIHTAARLLQVP-PERLEGAVTHRVTEtpyGR--VSRPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 409 TKQQADFAVEALAKAMYERLFRWILARVNKTLD-KSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTM 487
Cdd:cd14896 309 PVEGAIDARDALAKTLYSRLFTWLLKRINAWLApPGEAESDATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 488 FIMEQEEYKREGIEWNFIDfGLDLQPCIELIErpNNPPGILALLDEECWFPKATDTTFVEKLMNTHSAHAKFSKPKQHKD 567
Cdd:cd14896 389 LAQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQLPLP 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 568 klMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDVDRVVGLDTinkmsqssvPTSTKSKKgmfr 647
Cdd:cd14896 466 --VFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQ---------GKPTLASR---- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 648 tvgqlYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 727
Cdd:cd14896 531 -----FQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGAL 605
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1343958102 728 AAGSIPKgfMDGKQACGLMVKH-LDLDPNLYRIGQSKMFFR 767
Cdd:cd14896 606 GSERQEA--LSDRERCGAILSQvLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
96-765 |
1.40e-125 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 410.92 E-value: 1.40e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRH-EVPPHIYSITDNAYRNMLQDREDQSILCT 174
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 175 GESGAGKTENTKKVIQYLAViasshkPKKDINPGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLnfDVS---GC 251
Cdd:cd14876 81 GESGAGKTEATKQIMRYFAS------AKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQL--DVAsegGI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 252 LVGAfIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFLMGGHVEIPGLQDDELFEETLEAMEI 331
Cdd:cd14876 153 RYGS-VVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFEEVLESLKS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 332 MGFTQEERLGMLKVVSTVLQLGNIRFEKErnnEQATMPDntAA----------QKVCHLQGINVTDFSRAILTPKIKVGR 401
Cdd:cd14876 232 MGLTEEQIDTVFSIVSGVLLLGNVKITGK---TEQGVDD--AAaisneslevfKEACSLLFLDPEALKRELTVKVTKAGG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 402 EVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDkSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQ 481
Cdd:cd14876 307 QEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE-PPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 482 LFNHTMFIMEQEEYKREGIEWNFIDFgLDLQPCIELIERPNNppGILALLDEECWFPKATDTTFVEKLMNTHSAHAKFSK 561
Cdd:cd14876 386 NFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFKP 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 562 PKQHKDkLMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDVdrvvgldtinkmsqssVPTSTKS 641
Cdd:cd14876 463 AKVDSN-INFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGV----------------VVEKGKI 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 642 KKGMFrtVGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFR 721
Cdd:cd14876 526 AKGSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFL 603
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1343958102 722 QRYEILAAGSIPKGFMDGKQACGLMVKHLDLDPNLYRIGQSKMF 765
Cdd:cd14876 604 YQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
96-767 |
2.30e-123 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 405.93 E-value: 2.30e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTG 175
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 176 ESGAGKTENTKKVIQYLAVIASShkPKKDINPGELEKqllqANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVGA 255
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGS--VGGVLSVEKLNA----ALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 256 FIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFN-SYSFLMGGHVEIPGLQDDEL-FEETLEAMEIMG 333
Cdd:cd01386 155 SIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAeSNSFGIVPLQKPEDKQKAAAaFSKLQAAMKTLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 334 FTQEERLGMLKVVSTVLQLGNIRFEKERNNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIK-------VGREVVQK 406
Cdd:cd01386 235 ISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIFKHHLSggpqqstTSSGQESP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 407 AQ-----TKQQADFAVEALAKAMYERLFRWILARVNKTLdKSKRQSSSFLGILDIAGFeifeDN----------SFEQLC 471
Cdd:cd01386 315 ARsssggPKLTGVEALEGFAAGLYSELFAAVVSLINRSL-SSSHHSTSSITIVDTPGF----QNpahsgsqrgaTFEDLC 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 472 INYTNERLQQLFNHTMFIMEQEEYKREGIEWNFIDFGLDLQPCIELIERPN------------NPPGILALLDEECWFPK 539
Cdd:cd01386 390 HNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPqqalvrsdlrdeDRRGLLWLLDEEALYPG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 540 ATDTTFVEKLMNTH--SAHAKFSKPKQHKDK-LMFTVLHYAGK--VDYNAADWLTK-NMDPLNDNVTALLnnsssgfiqd 613
Cdd:cd01386 470 SSDDTFLERLFSHYgdKEGGKGHSLLRRSEGpLQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLL---------- 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 614 lwkdvdrvvgldtinkmSQSSVPTSTKSKKGMFRTVgqlyKESLGKLMATLHNTQPNFVRCIIPNH--EKRAGK------ 685
Cdd:cd01386 540 -----------------QESQKETAAVKRKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQHnaGKDERStsspaa 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 686 ----MDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAGSIPKGF-----MDGKQACGLMVKHLDLDPNL 756
Cdd:cd01386 599 gdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEELLEELDLEKSS 678
|
730
....*....|.
gi 1343958102 757 YRIGQSKMFFR 767
Cdd:cd01386 679 YRIGLSQVFFR 689
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
96-728 |
1.99e-122 |
|
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: 402.31 E-value: 1.99e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYKGKKR-HEVPPHIYSITDNAYRNMLQDRE--DQSI 171
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 172 LCTGESGAGKTENTKKVIQYLAVIASSHKPKKDINPGE-LEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSG 250
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAErIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 251 CLVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFLMGGHVEIpglqDDELFEETLEAME 330
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNL----EEDCFEVTREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 331 IMGFTQEERLGMLKVVSTVLQLGNIRFEKERNNEQATMPDNTAAQKV---CHLQGINVTDFSRAILTPKIKVGRE--VVQ 405
Cdd:cd14880 237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTKESVrtsALLLKLPEDHLLETLQIRTIRAGKQqqVFK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 406 KAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNH 485
Cdd:cd14880 317 KPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 486 TMFIMEQEEYKREGIEWNFIDFGlDLQPCIELIErpNNPPGILALLDEECWFPKATDT----TFVEKLMNTHS--AHAKF 559
Cdd:cd14880 397 HYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAaqlqTRIESALAGNPclGHNKL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 560 SKpkqhkdKLMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDvdrvvgldtiNKMSQSSVPTST 639
Cdd:cd14880 474 SR------EPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPA----------NPEEKTQEEPSG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 640 KSKKGMFrTVGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQE 719
Cdd:cd14880 538 QSRAPVL-TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQN 616
|
....*....
gi 1343958102 720 FRQRYEILA 728
Cdd:cd14880 617 FVERYKLLR 625
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
96-727 |
4.57e-120 |
|
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: 397.43 E-value: 4.57e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYKGKKR-HEVPPHIYSITDNAYRNMLQDREDQSILC 173
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 174 TGESGAGKTENTKKVIQYLAVIASSHKPKK---DINPGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVS- 249
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQNnnnNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 250 GCLVGAFIDTYLLEKSRCI-RQANTERAFHIFYYMVSGAKGKMRDELLLE-DFNSYSFL--------------MGGHVEI 313
Cdd:cd14906 161 GKIDGASIETYLLEKSRIShRPDNINLSYHIFYYLVYGASKDERSKWGLNnDPSKYRYLdarddvissfksqsSNKNSNH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 314 PGLQD-DELFEETLEAMEIMGFTQEERLGMLKVVSTVLQLGNIRFEKERNNEQAT--MPDNTAA-QKVCHLQGINVTDFS 389
Cdd:cd14906 241 NNKTEsIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 390 RAILTPKIKVG---------REVVQKAQTKqqadfavEALAKAMYERLFRWILARVNKTLDK----------SKRQSSSF 450
Cdd:cd14906 321 QALLNRNLKAGgrgsvycrpMEVAQSEQTR-------DALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 451 LGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIMEQEEYKREGIEWNFIDFgLDLQPCIELIERPNNppGILAL 530
Cdd:cd14906 394 IGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 531 LDEECWFPKATDTTFVEKLMNTHsaHAKFSKPKQHKDKLMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGF 610
Cdd:cd14906 471 LDDECIMPKGSEQSLLEKYNKQY--HNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFL 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 611 IQDLWKdvdrvvgldtinkmSQSSVPTSTKSKKGMFRTVGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHL 690
Cdd:cd14906 549 KKSLFQ--------------QQITSTTNTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVH 614
|
650 660 670
....*....|....*....|....*....|....*..
gi 1343958102 691 VLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 727
Cdd:cd14906 615 VLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCI 651
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
96-767 |
5.71e-118 |
|
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: 389.25 E-value: 5.71e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYKGKKRH-----EVPPHIYSITDNAYRNMLQDREDQ 169
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 170 SILCTGESGAGKTENTKKVIQYLAVIASShkpkkdiNPGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVS 249
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHST-------SSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 250 GCLVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFLMGGHV-EIPGLQDDELFEETLEA 328
Cdd:cd14886 154 GGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGIDDQKEFAPVRSQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 329 MEIMgFTQEERLGMLKVVSTVLQLGNIRFEKERNN--EQATMPDNTAA-QKVCHLQGINVTDFSRAILTPKIKVGREVVQ 405
Cdd:cd14886 234 LEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDMgvINAAKISNDEDfGKMCELLGIESSKAAQAIITKVVVINNETII 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 406 KAQTKQQADFAVEALAKAMYERLFRWILARVNKTLdKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNH 485
Cdd:cd14886 313 SPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEII-QFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFIN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 486 TMFIMEQEEYKREGIEWNFIDFGlDLQPCIELIERPNNppGILALLDEECWFPKATDTTFVEKLmNTHSAHAKFSKPKqh 565
Cdd:cd14886 392 QVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFTSSC-KSKIKNNSFIPGK-- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 566 KDKLMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIqdlwkdvdrvvgldtinKMSQSSVPTSTKSKKGM 645
Cdd:cd14886 466 GSQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIV-----------------NKAFSDIPNEDGNMKGK 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 646 FrtVGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 725
Cdd:cd14886 529 F--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNK 606
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1343958102 726 ILA--AGSIPKGFMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd14886 607 ILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
96-767 |
5.22e-111 |
|
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: 369.52 E-value: 5.22e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERyFSSLIYTYS--GLFCVVVNPYKMLPIYSEKIIEMY-KGKKRHEVPPHIYSITDNAYRNM-LQDREDQSI 171
Cdd:cd14875 1 ATLLHCIKER-FEKLHQQYSlmGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 172 LCTGESGAGKTENTKKVIQYLAVIA---SSHKPKKDInPGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFD- 247
Cdd:cd14875 80 VISGESGSGKTENAKMLIAYLGQLSymhSSNTSQRSI-ADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 248 VSGCLVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDEL-LLEDFNSYSFLMGGH------VEIPGLQDDE 320
Cdd:cd14875 159 TSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNtfvrrgVDGKTLDDAH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 321 LFEETLEAMEIMGFTQEERLGMLKVVSTVLQLGNIRFEKErNNEQATMPDNTAAQKVCHLQGINVTDFSRAILtpkIKVG 400
Cdd:cd14875 239 EFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESD-QNDKAQIADETPFLTACRLLQLDPAKLRECFL---VKSK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 401 REVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSS-SFLGILDIAGFEIFEDNSFEQLCINYTNERL 479
Cdd:cd14875 315 TSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDCSGcKYIGLLDIFGFENFTRNSFEQLCINYANESL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 480 QQLFNHTMFIMEQEEYKREGIEWNFIDFGlDLQPCIELIERPNNppGILALLDEECWFPKATDTTFVEKLMNTHSAHAK- 558
Cdd:cd14875 395 QNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDQKRT--GIFSMLDEECNFKGGTTERFTTNLWDQWANKSPy 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 559 FSKPKQHKDKlMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWkdvdrvvgldtinkmsqSSVPTS 638
Cdd:cd14875 472 FVLPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLL-----------------STEKGL 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 639 TKSKKgmfrTVGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQ 718
Cdd:cd14875 534 ARRKQ----TVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIE 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1343958102 719 EFRQRYEILAAGSIPKGFMDGK---QACGLMVKHLDL----DPNlYRIGQSKMFFR 767
Cdd:cd14875 610 QFCRYFYLIMPRSTASLFKQEKyseAAKDFLAYYQRLygwaKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
93-766 |
3.07e-104 |
|
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: 349.54 E-value: 3.07e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 93 LNEASVLQNLRERYFSSLIYTY---SGLfcVVVNPYKMLPIYSE----KIIEMYKG---KKRHEVPPHIYSITDNAYRNM 162
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDaslgEYGSEYYDttsGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 163 LQDREDQSILCTGESGAGKTEN----TKKVIQYlaviaSSHKPKkdinPGELEKQLLQANPILEAFGNAKTIKNDNSSRF 238
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESrrllLRQLLRL-----SSHSKK----GTKLSSQISAAEFVLDSFGNAKTLTNPNASRF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 239 GKFIKLNFDVSGCLVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFL--MGGH--VEIP 314
Cdd:cd14879 150 GRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasYGCHplPLGP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 315 GLQDDELFEETLEAMEIMGFTQEERLGMLKVVSTVLQLGNIRFEKER-NNEQATMPDNTAA-QKVCHLQGINVTDFsRAI 392
Cdd:cd14879 230 GSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHeGGEESAVVKNTDVlDIVAAFLGVSPEDL-ETS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 393 LTPKIK-VGREVV----QKAQTKQQADfaveALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAGFEIF---ED 464
Cdd:cd14879 309 LTYKTKlVRKELCtvflDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQNRsstGG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 465 NSFEQLCINYTNERLQQLFNHTMFIMEQEEYKREGIEWNFIDFgLDLQPCIELIERPnnPPGILALLDEEC-WFPKATDT 543
Cdd:cd14879 385 NSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLRGK--PGGLLGILDDQTrRMPKKTDE 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 544 TFVEKLMNTHSAHAKFS---KPKQHKDKLMFTVLHYAGKVDYNAADWLTKNMDPLndnvtallnnsSSGFIQdlwkdvdr 620
Cdd:cd14879 462 QMLEALRKRFGNHSSFIavgNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVL-----------SPDFVN-------- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 621 vvgldtinkmsqssvptstkskkgMFRTVGQLyKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGV 700
Cdd:cd14879 523 ------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGL 577
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1343958102 701 LEGIRICRQGFPNRIVFQEFRQRYEILAAGsipkgfMDGKQACGLMVKHLDLDPNLYRIGQSKMFF 766
Cdd:cd14879 578 PELAARLRVEYVVSLEHAEFCERYKSTLRG------SAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
96-752 |
2.00e-102 |
|
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: 346.70 E-value: 2.00e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYKgkKRHEVP------------PHIYSITDNAYRNM 162
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYA--YDHNSQfgdrvtstdprePHLFAVARAAYIDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 163 LQDREDQSILCTGESGAGKTENTKKVIQYLAVIASSHKPKKDINPGE----------LEKQLLQANPILEAFGNAKTIKN 232
Cdd:cd14899 79 VQNGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESIsppaspsrttIEEQVLQSNPILEAFGNARTVRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 233 DNSSRFGKFIKLNF-DVSGCLVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAK---GKMRDELLLEDFNSYSFLMG 308
Cdd:cd14899 159 DNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADNncvSKEQKQVLALSGGPQSFRLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 309 GHV----EIPGLQDDELFEETLEAMEIMGFTQEERLGMLKVVSTVLQLGNIRFEK-----ERN---NEQATMPDNTAA-- 374
Cdd:cd14899 239 NQSlcskRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQiphkgDDTvfaDEARVMSSTTGAfd 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 375 --QKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTL------------ 440
Cdd:cd14899 319 hfTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgade 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 441 --DKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIMEQEEYKREGIEWNFIDFGlDLQPCIELI 518
Cdd:cd14899 399 sdVDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 519 ErpNNPPGILALLDEECWFPKATDTTFVEKL---MNTHSAHAKFSKPKQHKDKLMFTVLHYAGKVDYNAADWLTKNMDPL 595
Cdd:cd14899 478 E--HRPIGIFSLTDQECVFPQGTDRALVAKYyleFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 596 NDNVTALLNNSSSGFIQDL-----WKDVDRVVGLDTINKMSQSSVPTSTKSKkgmfrTVGQLYKESLGKLMATLHNTQPN 670
Cdd:cd14899 556 CESAAQLLAGSSNPLIQALaagsnDEDANGDSELDGFGGRTRRRAKSAIAAV-----SVGTQFKIQLNELLSTVRATTPR 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 671 FVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE--ILAAGSIPKGFMDGKQACGLMVK 748
Cdd:cd14899 631 YVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYRrvLLSLYKWGDNDFERQMRCGVSLG 710
|
....
gi 1343958102 749 HLDL 752
Cdd:cd14899 711 KTRV 714
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
97-727 |
3.95e-100 |
|
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: 335.33 E-value: 3.95e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKmlPIYSEKIIEMYKGKKRHeVPPHIYSITDNAYRNMLQdREDQSILCTGE 176
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 177 SGAGKTENTKKVIQYLAVIASSHKpkkdinpgELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDvsGCLVGAF 256
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTT--------SIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 257 IDTYLLEKSRCIRQANTERAFHIFYyMVSGAKGKMrdelLLEDFNSYSFLMGGHVEIPGLQddELFEETLEAMEIMGFTQ 336
Cdd:cd14898 148 FETYLLEKSRVTHHEKGERNFHIFY-QFCASKRLN----IKNDFIDTSSTAGNKESIVQLS--EKYKMTCSAMKSLGIAN 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 337 EERLGMLKVvsTVLQLGNIRFekerNNEQAT-MPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQTKQQADF 415
Cdd:cd14898 221 FKSIEDCLL--GILYLGSIQF----VNDGILkLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQART 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 416 AVEALAKAMYERLFRWILARVNKTLDKSKRQSSSflgILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIMEQEEY 495
Cdd:cd14898 295 IRNSMARLLYSNVFNYITASINNCLEGSGERSIS---VLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMY 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 496 KREGIEWNFIDFgLDLQPCIELIERPNnppGILALLDEECWFPKATdttfVEKL-MNTHSAHAKFSKPKQhKDKLMftVL 574
Cdd:cd14898 372 KEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGN----VKNLlVKIKKYLNGFINTKA-RDKIK--VS 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 575 HYAGKVDYNAADWLTKNMDplndnvtallnnsssgfiqdlwKDVDRVVGLDTINkmsqssvptsTKSKKgmfRTVGQLYK 654
Cdd:cd14898 441 HYAGDVEYDLRDFLDKNRE----------------------KGQLLIFKNLLIN----------DEGSK---EDLVKYFK 485
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1343958102 655 ESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 727
Cdd:cd14898 486 DSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRIL 558
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
96-767 |
1.85e-99 |
|
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: 338.16 E-value: 1.85e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFS--------SLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDRE 167
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 168 DQSILCTGESGAGKTENTKKVIQYLAVIASShkpKKDINPGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFD 247
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDR---RHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 248 VSGCLVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLledfnsysflmgghveiPGLQDDELFE--ET 325
Cdd:cd14887 158 GRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSS-----------------AGEGDPESTDlrRI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 326 LEAMEIMGFTQEERLGMLKVVSTVLQLGNIRFEKERNNEQATMPDNTA--------AQKVCHL-------QGINVTDFSR 390
Cdd:cd14887 221 TAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSsevkclsSGLKVTEASR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 391 AILT--------PKIKVGREVV------------QKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSS- 449
Cdd:cd14887 301 KHLKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKPSESd 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 450 ------------FLGILDIAGFEIFED---NSFEQLCINYTNERLQQLFNHTMFIMEQEEYKREGIEWNFI--DFGLDLQ 512
Cdd:cd14887 381 sdedtpsttgtqTIGILDLFGFEDLRNhskNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsAFPFSFP 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 513 PCIELIERPNN---------------------PPGILALLDE------ECWFPKATDTTFVEKLMNTHSAHAKFSK--PK 563
Cdd:cd14887 461 LASTLTSSPSStspfsptpsfrsssafatspsLPSSLSSLSSslssspPVWEGRDNSDLFYEKLNKNIINSAKYKNitPA 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 564 QHKDKLMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLnNSSSGFIqdlwkdvdRVVGLDtinkmsQSSVPTSTKSKK 643
Cdd:cd14887 541 LSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYT--------RLVGSK------KNSGVRAISSRR 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 644 gmfRTVGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 723
Cdd:cd14887 606 ---STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRR 682
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1343958102 724 YEilaaGSIP---KGFMDGKQACGLMVKHLDLDPNLYRIGQSKMFFR 767
Cdd:cd14887 683 YE----TKLPmalREALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
96-767 |
4.51e-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: 329.08 E-value: 4.51e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMY---KGKKRHEVPPHIYSITDNAYRNMLQDREDQSIL 172
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 173 CTGESGAGKTENTKKVIQYLAVIASSHKPKkdinpgeLEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNF-DVSGC 251
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTT-------FDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 252 LVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFLMGGHVEIPGLQDDELFEETL----E 327
Cdd:cd14878 154 LTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMREDVSTAERSLNREKLavlkQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 328 AMEIMGFTQEERLGMLKVVSTVLQLGNIRFEKERNNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKA 407
Cdd:cd14878 234 ALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 408 QTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSS---FLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFN 484
Cdd:cd14878 314 HTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMqtlDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYIN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 485 HTMFIMEQEEYKREGIewnfidfgldlqpCIELIERPNN-----------PPGILALLDEECWFPKATDTTFVEKL---M 550
Cdd:cd14878 394 EVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLLDEESQMIWSVEPNLPKKLqslL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 551 NTHSAHAKFSKPKQHKDKL-------MFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSssgfiqdlwkdvDRVVg 623
Cdd:cd14878 461 ESSNTNAVYSPMKDGNGNValkdqgtAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTS------------ENVV- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 624 ldtINKMSQSSVPTstkskkgmfrTVGQLYKeSLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEG 703
Cdd:cd14878 528 ---INHLFQSKLVT----------IASQLRK-SLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEM 593
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1343958102 704 IRICRQGFPNRIVFQEFRQRYEILAAGSI-PKGFMDGKQACGLMVKHLDLDPnlYRIGQSKMFFR 767
Cdd:cd14878 594 VKIFRYGYPVRLSFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
96-767 |
1.26e-91 |
|
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: 312.33 E-value: 1.26e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYsekiIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTG 175
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 176 ESGAGKTENTKKVIQ-YLAVIasshkpKKDinpGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVG 254
Cdd:cd14937 77 ESGSGKTEASKLVIKyYLSGV------KED---NEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 255 AFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFLMGGHVEIPGLQDDELFEETLEAMEIMGF 334
Cdd:cd14937 148 SSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMNM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 335 TqEERLGMLKVVSTVLQLGNIRF---EKERNNEQATMPDNT--AAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAQT 409
Cdd:cd14937 228 H-DMKDDLFLTLSGLLLLGNVEYqeiEKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 410 KQQADFAVEALAKAMYERLFRWILARVNKTLDKSKrQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFI 489
Cdd:cd14937 307 VEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 490 MEQEEYKREGIEWNFIDFGLDlQPCIELIeRPNNppGILALLDEECWFPKATDTTFVEKLMNTHSAHAKFSKPKQHKDKl 569
Cdd:cd14937 386 KETELYKAEDILIESVKYTTN-ESIIDLL-RGKT--SIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINK- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 570 MFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDVDRVVGLDTINKMSqssvptstkskkgmFRtv 649
Cdd:cd14937 461 NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRKNLIT--------------FK-- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 650 gqlYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRIcRQGFPNRIVFQEFRQRYEILAA 729
Cdd:cd14937 525 ---YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDY 600
|
650 660 670
....*....|....*....|....*....|....*...
gi 1343958102 730 GSIPKGFMDGKQACGLMVKHlDLDPNLYRIGQSKMFFR 767
Cdd:cd14937 601 STSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
96-719 |
1.34e-85 |
|
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: 296.43 E-value: 1.34e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYKGKKRHE-------VPPHIYSITDNAYRNMLQDRE 167
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 168 DQSILCTGESGAGKTENTKKVIQYLaviassHKPKKDINPGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFD 247
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYF------HYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 248 ---------VSGCLVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGK-------MRD----ELLLEDFNSYSFLM 307
Cdd:cd14884 155 eventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEdlarrnlVRNcgvyGLLNPDESHQKRSV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 308 GGHVEIPGL----------QDDELFEETLEAMEIMGFTQEERLGMLKVVSTVLQLGNIRFekernneqatmpdntaaQKV 377
Cdd:cd14884 235 KGTLRLGSDsldpseeekaKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAY-----------------KAA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 378 CHLQGINVTDFSRAILTPKIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTL--DKSKRQS-------- 447
Cdd:cd14884 298 AECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkCKEKDESdnediysi 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 448 -SSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIMEQEEYKREGIEWNFIDFGlDLQPCIELIERpnnppg 526
Cdd:cd14884 378 nEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFIAK------ 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 527 ILALLDEECWFP----KATDTTFVEKLMNT---------HSA------HAKFSKPKQHKDKLMFTVLHYAGKVDYNAADW 587
Cdd:cd14884 451 IFRRLDDITKLKnqgqKKTDDHFFRYLLNNerqqqlegkVSYgfvlnhDADGTAKKQNIKKNIFFIRHYAGLVTYRINNW 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 588 LTKNMDPLNDNVTALLNNSSSGFIQDlwkdvdrvvgldtinkmsqssvpTSTKSKKGMFRTVGQLYKESLGKLMATLHNT 667
Cdd:cd14884 531 IDKNSDKIETSIETLISCSSNRFLRE-----------------------ANNGGNKGNFLSVSKKYIKELDNLFTQLQST 587
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1343958102 668 QPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQE 719
Cdd:cd14884 588 DMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
96-732 |
5.71e-75 |
|
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: 263.27 E-value: 5.71e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYkgkkrhevppHIYSITDNAYRNMLQDRED-QSILCT 174
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 175 GESGAGKTENTKKVIQYLaviasSHKPKKDINpgelEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVG 254
Cdd:cd14874 71 GESGSGKSYNAFQVFKYL-----TSQPKSKVT----TKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYKRNVLTGL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 255 AFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFLMGGHVEIPGLQDDELFEETLEAMEIMGF 334
Cdd:cd14874 142 NLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLEDALHVLGF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 335 TQEERLGMLKVVSTVLQLGNIRFEKERN---NEQATMPDNTAAQK-VCHLQGINVTDFSrAILTPKIKVGREVvqkaqTK 410
Cdd:cd14874 222 SDDHCISIYKIISTILHIGNIYFRTKRNpnvEQDVVEIGNMSEVKwVAFLLEVDFDQLV-NFLLPKSEDGTTI-----DL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 411 QQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSsfLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIM 490
Cdd:cd14874 296 NAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 491 EQEEYKREGIEWNF-IDFGLDLQPCIELIERpnNPPGILALLDEECWFPKATDTTFVEKLMNTHSAHAKFSKPKQhKDKL 569
Cdd:cd14874 374 QLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARN-KERL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 570 MFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLwkdvdrvvgldtinkmsqssVPTSTKSKKGMFRTV 649
Cdd:cd14874 451 EFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLL--------------------FESYSSNTSDMIVSQ 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 650 GQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAA 729
Cdd:cd14874 511 AQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLP 590
|
...
gi 1343958102 730 GSI 732
Cdd:cd14874 591 GDI 593
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
97-720 |
3.36e-73 |
|
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: 259.64 E-value: 3.36e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYKgkKRHEVPPHIYSITDNAYRNMLQDREDQSILCTG 175
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 176 ESGAGKTENTKKVIQYLAVIASSHKPKkdinpgeLEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVGA 255
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTDLSRSKY-------LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 256 FIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFL-MGGHVEIPGLQDDELFEETLEAMEIMGF 334
Cdd:cd14905 153 KLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLnQGGSISVESIDDNRVFDRLKMSFVFFDF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 335 TQEERLGMLKVVSTVLQLGNIRFEKErnNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVVQKAqtkqqad 414
Cdd:cd14905 233 PSEKIDLIFKTLSFIIILGNVTFFQK--NGKTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENR------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 415 favEALAKAMYERLFRWILARVNKTLDKSkrQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIMEQEE 494
Cdd:cd14905 304 ---DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQRE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 495 YKREGIEW-NFIDFGlDLQPCIELIERpnnppgILALLDEECWFPKATDTTFVEKLMNTHSAHAKFSKpKQHKdklmFTV 573
Cdd:cd14905 379 YQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFGK-KPNK----FGI 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 574 LHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFI--QDLWKDVDRVVGldTINKMSQSSvPTSTKSKKGMFRTV-- 649
Cdd:cd14905 447 EHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLfsRDGVFNINATVA--ELNQMFDAK-NTAKKSPLSIVKVLls 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 650 --------------------------------GQLYK--ESLGKLMATlHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQL 695
Cdd:cd14905 524 cgsnnpnnvnnpnnnsgggggggnsgggsgsgGSTYTtySSTNKAINN-SNCDFHFIRCIKPNSKKTHLTFDVKSVNEQI 602
|
650 660
....*....|....*....|....*....
gi 1343958102 696 RCNGVLEGIRICRQGFP----NRIVFQEF 720
Cdd:cd14905 603 KSLCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
97-728 |
1.08e-71 |
|
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: 253.88 E-value: 1.08e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYkmlpiysekiieMYKGKKRHEVP-------PHIYSITDNAYRNMLQDREDQ 169
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTLTStrssplaPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 170 SILCTGESGAGKTENTKKVIQYLAVIASshkpkkdinpGELE----KQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLN 245
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAG----------GGPEtdafKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 246 FdVSGCLVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFN--SYSFLMGGHVEIPGLQDDELFE 323
Cdd:cd14881 140 V-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAEDAARFQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 324 ETLEAMEIMG--FtqeerLGMLKVVSTVLQLGNIRFeKERNNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGR 401
Cdd:cd14881 219 AWKACLGILGipF-----LDVVRVLAAVLLLGNVQF-IDGGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTHNARG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 402 EVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTL----DKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNE 477
Cdd:cd14881 293 QLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANSLKrlgsTLGTHATDGFIGILDMFGFEDPKPSQLEHLCINLCAE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 478 RLQQLFNHTMFIMEQEEYKREGIEWNF-IDFgLDLQPCIELIErpNNPPGILALLDEECwFPKATDTTFVEKLMNTHSAH 556
Cdd:cd14881 373 TMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKIKVQHRQN 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 557 AKFSKPKQHKDKlMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFiqdlwkdvdrvvgldtinkmsqssvp 636
Cdd:cd14881 449 PRLFEAKPQDDR-MFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNF-------------------------- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 637 tstkskkgMFRTVGQLYKESLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIV 716
Cdd:cd14881 502 --------GFATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMR 573
|
650
....*....|..
gi 1343958102 717 FQEFRQRYEILA 728
Cdd:cd14881 574 FKAFNARYRLLA 585
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
99-725 |
8.96e-70 |
|
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: 251.04 E-value: 8.96e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 99 LQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIY----------SEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDRED 168
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYtpdhmqaynkSREQTPLYEKDTVNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 169 QSILCTGESGAGKTENTKKVIQYLAVIASSHKPKKDiNPGE------LEKQLLQANPILEAFGNAKTIKNDNSSRFGKFI 242
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPD-SEGAsgvlhpIGQQILHAFTILEAFGNAATRQNRNSSRFAKMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 243 KLNFDVSGCLVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKG--KMRDELLL-EDFNSYSFLMGGHVEIPGLQ-D 318
Cdd:cd14893 163 SVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdpTLRDSLEMnKCVNEFVMLKQADPLATNFAlD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 319 DELFEETLEAMEIMGFTQEERLGMLKVVSTVLQLGNIRFekernneqatMPDNTAAQK--------VCHLQGINVTDFSR 390
Cdd:cd14893 243 ARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDF----------VPDPEGGKSvggansttVSDAQSCALKDPAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 391 AILTPKI-------------------KVGREVVQ--KAQTKQQADFAVEALAKAMYERLFRWILARVNKTL----DKSKR 445
Cdd:cd14893 313 ILLAAKLlevepvvldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 446 QS----SSFLGILDIAGFEIFED--NSFEQLCINYTNERLQQLF-NHTMFIMEQE-EYKREGIEWNF-----IDFGLDLQ 512
Cdd:cd14893 393 SNivinSQGVHVLDMVGFENLTPsqNSFDQLCFNYWSEKVHHFYvQNTLAINFSFlEDESQQVENRLtvnsnVDITSEQE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 513 PCIELIERPnnPPGILALLDEECWFPKATDTTFVEKLMNTHSAHAKFSKPKQHKD------------KLMFTVLHYAGKV 580
Cdd:cd14893 473 KCLQLFEDK--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADttneylapskdwRLLFIVQHHCGKV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 581 DYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDVDRVVGLDTINKMSQSSVPTSTKSKKGMFR----------TVG 650
Cdd:cd14893 551 TYNGKGLSSKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKAAKQTEERGSTSSKFRKSASSaresknitdsAAT 630
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1343958102 651 QLYKESlGKLMATLHNTQPNFVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 725
Cdd:cd14893 631 DVYNQA-DALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
97-728 |
9.08e-68 |
|
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: 242.72 E-value: 9.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTGE 176
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 177 SGAGKTENTKKVIQYLAVIASShkpkkdiNPGELEKqLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSGCLVGAF 256
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDG-------NRGATGR-VESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 257 IDTYLLEKSRCIRQANTERAFHIFYYMVSG--AKGKMRDELLLEDFNsYSFLMgGHVEIPG-----LQDD-----ELFEE 324
Cdd:cd14882 154 FWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLKEYNLKAGRN-YRYLR-IPPEVPPsklkyRRDDpegnvERYKE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 325 TLEAMEIMGFTQEERLGMLKVVSTVLQLGNIRFEKerNNEQATMPDNTAAQKVCHLQGINVTDFSRAILTPKIKVGREVV 404
Cdd:cd14882 232 FEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 405 QKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLD--KSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQL 482
Cdd:cd14882 310 RRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSfpRAVFGDKYSISIHDMFGFECFHRNRLEQLMVNTLNEQMQYH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 483 FNHTMFIMEQEEYKREGI---EWNFIDFGLDLQpciELIERPNnppGILALLDEECwfPKATDTTFVekLMNTHSAHAKF 559
Cdd:cd14882 390 YNQRIFISEMLEMEEEDIptiNLRFYDNKTAVD---QLMTKPD---GLFYIIDDAS--RSCQDQNYI--MDRIKEKHSQF 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 560 SKPKQHKDklmFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFIQDLWKDvdrvvglDTINKMsqssvptst 639
Cdd:cd14882 460 VKKHSAHE---FSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVRNM--------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 640 kskkgmfRTVGQLYKESLGKLMATLHNTQPN----FVRCIIPNHEKRAGKMDAHLVLEQLRCNGVLEGIRICRQGFPNRI 715
Cdd:cd14882 521 -------RTLAATFRATSLELLKMLSIGANSggthFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRI 593
|
650
....*....|...
gi 1343958102 716 VFQEFRQRYEILA 728
Cdd:cd14882 594 PFQEFLRRYQFLA 606
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
118-250 |
1.55e-58 |
|
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: 199.49 E-value: 1.55e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 118 FCVVVNPYKMLPIYSE-KIIEMYKGKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTGESGAGKTENTKKVIQYLAVIA 196
Cdd:cd01363 1 VLVRVNPFKELPIYRDsKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1343958102 197 SSHKPKKDIN--------PGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVSG 250
Cdd:cd01363 81 FNGINKGETEgwvylteiTVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAG 142
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
97-765 |
3.75e-55 |
|
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: 206.61 E-value: 3.75e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYK-GKKRHEVPPHIYSITDNAYRNMLQDREDQSILCTG 175
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 176 ESGAGKTENTKKVIQYLA--VIASSHKPKKDINPGELEKQ--------------LLQANPILEAFGNAKTIKNDNSSRFG 239
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAyqVKGSRRLPTNLNDQEEDNIHneentdyqfnmsemLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 240 KFIKLNFDVSGcLVGAFIDTYLLEKSRCIRQANTERAFHIFYYMVSGAKGKMRDELLLEDFNSYSFLMGGHVEIPGLQDD 319
Cdd:cd14938 162 KFCTIHIENEE-IKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 320 ELFEETLEAMEIMGFTQEERLGMLKVVSTVLQLGNIRFEK-------------------------ERNNEQATMPDNTAA 374
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVKafrkksllmgknqcgqninyetilsELENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 375 QKV--CHLQGINVTDFSRAILTPKIkVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKR--QSSSF 450
Cdd:cd14938 321 NLLlaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 451 LGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFIMEQEEYKREGIEWNFIDFGLDLQPCIELIERPNNppGILAL 530
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 531 LDEECWFPKATD-TTFVEKLMNTHSAHAKFSKPKQHK-DKLMFTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSS 608
Cdd:cd14938 478 LLENVSTKTIFDkSNLHSSIIRKFSRNSKYIKKDDITgNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 609 GFIQDLWKDVDRVVGLDTINKMSQSSVPTSTKSKKGMFRTVGQ----LYKESLGKLMATLHNTQPNFVRCIIPNHEKRA- 683
Cdd:cd14938 558 EYMRQFCMFYNYDNSGNIVEEKRRYSIQSALKLFKRRYDTKNQmavsLLRNNLTELEKLQETTFCHFIVCMKPNESKREl 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 684 GKMDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAgsipkgfmDGKQACGLMVKHLDLDPNLYRIGQSK 763
Cdd:cd14938 638 CSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISNYEWMIGNNM 709
|
..
gi 1343958102 764 MF 765
Cdd:cd14938 710 IF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
933-1714 |
1.74e-32 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 138.65 E-value: 1.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 933 RSISLQQEKKEMEQELQLMEahIVQEEDARQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLLEERLADMSSNLa 1012
Cdd:TIGR02168 214 RYKELKAELRELELALLVLR--LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1013 eeeeksKNLSKLKSKHESMISELEVRLkkeektrqdvekakRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQ 1092
Cdd:TIGR02168 291 ------YALANEISRLEQQKQILRERL--------------ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1093 ACLDEESRQRGAALKRVRDLEALLAELQEDLEAEKvargkaeAARRDLGEELNSLRSELEdSLDTTAAQQELRVKREQE- 1171
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELEEQLETLR-------SKVAQLELQIASLNNEIE-RLEARLERLEDRRERLQQe 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1172 -MAMLKKAMEDEGRSHETQIQELRQKHGQAVEELREHLEQAKKVRAALEKAKQAL---EKEAADLSADLRALSSTKQDVE 1247
Cdd:TIGR02168 423 iEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALdaaERELAQLQARLDSLERLQENLE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1248 QKKKKVEA------QLNDLQLRFSESERQRNE--------LSERVSKMTVE------------------------LDSVT 1289
Cdd:TIGR02168 503 GFSEGVKAllknqsGLSGILGVLSELISVDEGyeaaieaaLGGRLQAVVVEnlnaakkaiaflkqnelgrvtflpLDSIK 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1290 GLLNEAEGRNIKLSKEA-------------------------SSISSQLQDAQELLSeetrqKLNLSGRLRQLEEDKgcl 1344
Cdd:TIGR02168 583 GTEIQGNDREILKNIEGflgvakdlvkfdpklrkalsyllggVLVVDDLDNALELAK-----KLRPGYRIVTLDGDL--- 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1345 meQLEEEMEAKQAVERQASSLSVqlsdlKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQE 1424
Cdd:TIGR02168 655 --VRPGGVITGGSAKTNSSILER-----RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1425 LEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSAKSAEERDRAEAELREKETKVLALMKMLEDKQEALQEAERTVKA 1504
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE 807
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1505 LRVEMEDLisskddvGKSVHDLERAKRGLEAFVEEMKTQMEELEDELQVAEDAKLRLEVNSQALRAQHERELQAREEQGE 1584
Cdd:TIGR02168 808 LRAELTLL-------NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1585 EKRRQLLKQVRELEAELEEERKQRTLASaARKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQGQLKELHR-ELEEGRAA 1663
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELES-KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEAL 959
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1343958102 1664 HKEILASAREAERRCKNLEAEILQMQEMLAAAERARKQAETERDELSEEVA 1714
Cdd:TIGR02168 960 ENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKE 1010
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1039-1878 |
1.60e-31 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 135.57 E-value: 1.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1039 LKKEEKTRQD---VEKAKRKVEAELVDLQeQQADLQAQLAELRAQLAAKEEELQTTQ-----ACLDEESRQRGAALKRVR 1110
Cdd:TIGR02168 178 ERKLERTRENldrLEDILNELERQLKSLE-RQAEKAERYKELKAELRELELALLVLRleelrEELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1111 DLEALLAELQEDLEAEKVARGKAEAARRDLGEELNSLRSELEDsldttaAQQELRVKREQemamlKKAMEDEGRSHETQI 1190
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR------LEQQKQILRER-----LANLERQLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1191 QELRQKHGQAVEELrehleqakkvrAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQ 1270
Cdd:TIGR02168 326 EELESKLDELAEEL-----------AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1271 RNELSERVSKMTVELDSVTGLLNEAEGRNIKLSKEASSisSQLQDAQELLSEETRQKLNLSGRLRQLEEDKGCLMEQLEE 1350
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1351 EMEAKQAVERQASSLSVQLSDLKKRLEELS----AAVELLEEGKK------RLQRELEAASGDYEEKAAAydkleksrgr 1420
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSLERLQENLEgfseGVKALLKNQSGlsgilgVLSELISVDEGYEAAIEAA---------- 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1421 LQQELEDVLM-DLDSQRQLVSNLEKKQKKF----------DQMLAEERAVSAKSAEERDRAEAELREKETKV-------L 1482
Cdd:TIGR02168 543 LGGRLQAVVVeNLNAAKKAIAFLKQNELGRvtflpldsikGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLrkalsylL 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1483 ALMKMLEDKQEALQ------------------------------EAERTVKALRVEMEDLISSKDDVGKSVHDLERAKRG 1532
Cdd:TIGR02168 623 GGVLVVDDLDNALElakklrpgyrivtldgdlvrpggvitggsaKTNSSILERRREIEELEEKIEELEEKIAELEKALAE 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1533 LEAFVEEMKTQMEELEDELQVAEDAKLRLEVNSQALRAQHERELQAREEQGEEkRRQLLKQVRELEAELEEERKQRTLAS 1612
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE-LTELEAEIEELEERLEEAEEELAEAE 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1613 AARKKLEGEVKNTEEQLEAASRgrdealkQLRKNQGQLKELHRELEEGRAAHKEILASAREAERRCKNLEAEILQMQEML 1692
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALRE-------ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1693 AAAERARKQAETERDELSEEVAGgssgrslLSDEKRRLEAKISQLEEELEEEQANVETLNERLRKSQQLVDQLGAELTAE 1772
Cdd:TIGR02168 855 ESLAAEIEELEELIEELESELEA-------LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1773 RASSQNREGSRLQLEKQTRDLKAKLQDVESQARSKLKSSVAALEAKLREAEEQLEVESRERQASAKNLRQKEKKLKDLTA 1852
Cdd:TIGR02168 928 ELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTA 1007
|
890 900
....*....|....*....|....*.
gi 1343958102 1853 QMEDERKQAQDYKDQMEKSSARMKQL 1878
Cdd:TIGR02168 1008 QKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
102-708 |
1.40e-29 |
|
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: 128.32 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 102 LRERYFSSLIYTYSGLFCV-VVNPYKML------PIYSEKIIEMYKGKKRHE--VPPHIYSITDNAYRNMLQDRED---- 168
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKQSLVRLFFDNEHtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 169 ---------------QSILCTGESGAGKTENTKKVIQYLAVIA----------------SSHKPK--------------- 202
Cdd:cd14894 87 pstissnrsmtegrgQSLFLCGESGSGKTELAKDLLKYLVLVAqpalskgseetckvsgSTRQPKiklftsstkstiqmr 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 203 ----------------------KDINPG---------------------------------ELEKQL------------- 214
Cdd:cd14894 167 teeartialleakgvekyeivlLDLHPErwdemtsvsrskrlpqvhvdglffgfyeklehlEDEEQLrmyfknphaakkl 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 215 ---LQANPILEAFGNAKTIKNDNSSRFGKFIKLN---------FDVSGCLVGAFidtyLLEKSRCIRQANTERA------ 276
Cdd:cd14894 247 sivLDSNIVLEAFGHATTSMNLNSSRFGKMTTLQvafglhpweFQICGCHISPF----LLEKSRVTSERGRESGdqneln 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 277 FHIFYYMVSGAKG-----KMRDELLLE--DFNSYSFLMGGHVEIPGL--------QDDELFEETLEAMEIMGFTQEERLG 341
Cdd:cd14894 323 FHILYAMVAGVNAfpfmrLLAKELHLDgiDCSALTYLGRSDHKLAGFvskedtwkKDVERWQQVIDGLDELNVSPDEQKT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 342 MLKVVSTVLQLGNIRFEKERNNEQATMPDN---TAAQKVCHLQGI-NVTDFSRAILTPKIKV--GREVVQKAQTKQQADF 415
Cdd:cd14894 403 IFKVLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELgSVEKLERMLMTKSVSLqsTSETFEVTLEKGQVNH 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 416 AVEALAKAMYERLFRWILARVNK-------TLDKSKRQ---------SSSFLGILDIAGFEIFEDNSFEQLCINYTNERL 479
Cdd:cd14894 483 VRDTLARLLYQLAFNYVVFVMNEatkmsalSTDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 480 qqlfnhtmfimeqeeYKREGiewNFIDFGLDLQPciELIERPN---------NPPGILALLDEECWFPKATDTT------ 544
Cdd:cd14894 563 ---------------YAREE---QVIAVAYSSRP--HLTARDSekdvlfiyeHPLGVFASLEELTILHQSENMNaqqeek 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 545 ----FVEKLMNTHSAHAK-----FSKPKQHKDKLM----FTVLHYAGKVDYNAADWLTKNMDPLNDNVTALLNNSSSGFI 611
Cdd:cd14894 623 rnklFVRNIYDRNSSRLPepprvLSNAKRHTPVLLnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHF 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 612 QDLWKDVDRVVGLDTINKM---SQSSVPTSTKSKKGMFRTvgqlykeSLGKLMATLHNTQPNFVRCIIPNHEKRAGKMDA 688
Cdd:cd14894 703 CRMLNESSQLGWSPNTNRSmlgSAESRLSGTKSFVGQFRS-------HVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNN 775
|
810 820
....*....|....*....|
gi 1343958102 689 HLVLEQLRCNGVLEGIRICR 708
Cdd:cd14894 776 DLVEQQCRSQRLIRQMEICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1184-1926 |
3.43e-29 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 127.87 E-value: 3.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1184 RSHETQIQ-ELRQKHGQAVEELREHLE-QAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLQ 1261
Cdd:TIGR02168 173 RRKETERKlERTRENLDRLEDILNELErQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1262 LRFSESERQRNELSERVSKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQELLSEETRQKLNLSGRLRQLEEDK 1341
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1342 GClmeqleeEMEAKQAVERQASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRL 1421
Cdd:TIGR02168 333 DE-------LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1422 QQELEDVLMDLDSQRQLVSNLEKKQKKFDqmLAEERAVSAKSAEERDRAEAELREKETKVLALMKMLEDKQEALQEAERT 1501
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1502 VKALRVE---MEDLISSKDDVGKSVHDLERAKRGLEAFVEEMKTQME-ELEDELQVAEDAKLRL-----EVNSQALRAQh 1572
Cdd:TIGR02168 484 LAQLQARldsLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISvDEGYEAAIEAALGGRLqavvvENLNAAKKAI- 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1573 erELQAREEQG---------------EEKRRQLLKQVRELEAELEEERKQRTLASAA--------------------RKK 1617
Cdd:TIGR02168 563 --AFLKQNELGrvtflpldsikgteiQGNDREILKNIEGFLGVAKDLVKFDPKLRKAlsyllggvlvvddldnalelAKK 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1618 LEGEVKNTEEQLEAASRG----------------RDEALKQLRKN----QGQLKELHRELEEGRAAHKEILASAREAERR 1677
Cdd:TIGR02168 641 LRPGYRIVTLDGDLVRPGgvitggsaktnssileRRREIEELEEKieelEEKIAELEKALAELRKELEELEEELEQLRKE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1678 CKNLEAEILQMQEMLAAAERARKQAETERDELSEEVAGGSSGRSLLSDEKRRLEAKISQLEEELEEEQANVETLNERLRK 1757
Cdd:TIGR02168 721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1758 SQQLVDQLGAELTAERASSQNREGSRLQLEKQTRDLKAKLQDVESQAR------SKLKSSVAALEAKLREAEEQLEVESR 1831
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEelsediESLAAEIEELEELIEELESELEALLN 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1832 ERQASAKNLRQKEKKLKDLTAQMEDERKQAQDYKDQMEKSSARMKQLKHQLEEAEEEAQRVAAA-RRKLQRELDEALEAN 1910
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALE 960
|
810
....*....|....*.
gi 1343958102 1911 DALSREVSSLRSKLRR 1926
Cdd:TIGR02168 961 NKIEDDEEEARRRLKR 976
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1201-1833 |
4.91e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 126.98 E-value: 4.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1201 VEELREHLEQAKKVRAALEKAkQALEKEAADLSADLRALSstKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSK 1280
Cdd:COG1196 195 LGELERQLEPLERQAEKAERY-RELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1281 MTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQELLSEETRQKLNLSGRLRQLEEDKGCLMEQLEEEMEAKQAVER 1360
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1361 QASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVS 1440
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1441 NLEKKQKKFDQMLAEERAVSAKSAEERDRAEAELREKETKVLALMKMLEDKQEALQEAeRTVKALRVEMEDLISSKDDVG 1520
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA-AARLLLLLEAEADYEGFLEGV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1521 KSVHDLERAKRGLEAFVEEMKTQmEELEDELQVAEDAKLRLEVNSQALRAQHERELQAREEQGEEKRRQLLKQVRELEAE 1600
Cdd:COG1196 511 KAALLLAGLRGLAGAVAVLIGVE-AAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALA 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1601 LEEERKQRTLASAARKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQGQLKELHRELEEGRAAHKEILASAREAERRCKN 1680
Cdd:COG1196 590 AALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1681 LEAEILQMQEMLAAAERARKQAETERDELSEEvaggssgrslLSDEKRRLEAKISQLEEELEEEQANVETLNERLRKSQQ 1760
Cdd:COG1196 670 LLAALLEAEAELEELAERLAEEELELEEALLA----------EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1761 LVDQLGAELTAERASSQNREGSRLQLEKQTRDLKAKLQD------------VESQAR-----SKLKSSVAALEaKLREAE 1823
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllaieeyEELEERydflsEQREDLEEARE-TLEEAI 818
|
650
....*....|
gi 1343958102 1824 EQLEVESRER 1833
Cdd:COG1196 819 EEIDRETRER 828
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
857-1590 |
2.81e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 124.78 E-value: 2.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 857 LKAVREAAAKAEADLKDITQKHSQLVEEQAMLEAKLQAEAELyaeaedmRVRLEAKKQELEEVLHEMEARLEEEEERSIS 936
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE-------VSELEEEIEELQKELYALANEISRLEQQKQI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 937 LQQEKKEMEQELQLMEAHIVQEEDARQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLLEERLAD-------MSS 1009
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEleeqletLRS 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1010 NLAEEEEKSKNLSKLKSKHESMISELEVRLKK-----EEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAK 1084
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLEARLERLEDRRERlqqeiEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1085 EEELQTTQACLDEESRQRGAALKRVRDLEALLAELQEDLEAEK--VARGKAEAARRDLGEELNSLRSELEDSLDTT--AA 1160
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKalLKNQSGLSGILGVLSELISVDEGYEAAIEAAlgGR 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1161 QQELRVKREQEmAMLKKAMEDEGRSHETQIQELRQKHGQAVE----ELREHLEQAKKVRAALEKAKQALEKEAADLSADL 1236
Cdd:TIGR02168 547 LQAVVVENLNA-AKKAIAFLKQNELGRVTFLPLDSIKGTEIQgndrEILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGV 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1237 RALSSTKQDVEQKKKKVEAQ----LNDLQLRFS-----ESERQRNELSERvskmTVELDSVTGLLNEAEGRNIKLSKEAS 1307
Cdd:TIGR02168 626 LVVDDLDNALELAKKLRPGYrivtLDGDLVRPGgvitgGSAKTNSSILER----RREIEELEEKIEELEEKIAELEKALA 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1308 SISSQLQDAQELLSEETRQKLNLSGRLRQLEEDKgclmeqlEEEMEAKQAVERQASSLSVQLSDLKKRLEELSAAVELLE 1387
Cdd:TIGR02168 702 ELRKELEELEEELEQLRKELEELSRQISALRKDL-------ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1388 EGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSAKSAEER 1467
Cdd:TIGR02168 775 EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1468 DRAEAELREKETKVLALMKMLEDKQEALQEAERTVKALRVEMEDLISSKDDVGKSVHDLERAKRGLEAFVEEMKTQMEEL 1547
Cdd:TIGR02168 855 ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1548 EDELQ-----VAEDAKLRLEV--NSQALRAQHERELQAREEQGEEKRRQL 1590
Cdd:TIGR02168 935 EVRIDnlqerLSEEYSLTLEEaeALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
992-1757 |
4.99e-28 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 124.02 E-value: 4.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 992 KLQKERKLLEERLADMSSNLAEEEEKSKNLSKLKSKHESMISELEVRLKKEE-------KTRQDVEKAKRKVEAELVDLQ 1064
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREyegyellKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1065 EQQADLQAQLAELRAQLAAKEEELQTTQACLDEESRQRGAALK-RVRDLEALLAELQEDLEAEKVARGKAEAARRDLGEE 1143
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKeKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1144 LNSLRSELEDSldtTAAQQELRVKREQEMAMLKKAmEDEGRSHETQIQELRQKHGQAVEEL---REHLEQAKKVRAALEK 1220
Cdd:TIGR02169 331 IDKLLAEIEEL---EREIEEERKRRDKLTEEYAEL-KEELEDLRAELEEVDKEFAETRDELkdyREKLEKLKREINELKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1221 AKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVELDSVTGLLNEAEGRNI 1300
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1301 KLSKEASSISSQLQ----------DAQELLSEETRQKLNLSGRLRQLEEDKGCLMEQL----------EEEMEAKQAVE- 1359
Cdd:TIGR02169 487 KLQRELAEAEAQARaseervrggrAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAagnrlnnvvvEDDAVAKEAIEl 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1360 ---RQASSLS-VQLSDLKKRLEELSA---------AVELLEEGKKR------------LQRELEAA------------SG 1402
Cdd:TIGR02169 567 lkrRKAGRATfLPLNKMRDERRDLSIlsedgvigfAVDLVEFDPKYepafkyvfgdtlVVEDIEAArrlmgkyrmvtlEG 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1403 DYEEKAAA----YDKLEKSRGRLQQELEDVLM---DLDSQRQLVSNLEKKQKKFDQMLAEERAvsaksaeERDRAEAELR 1475
Cdd:TIGR02169 647 ELFEKSGAmtggSRAPRGGILFSRSEPAELQRlreRLEGLKRELSSLQSELRRIENRLDELSQ-------ELSDASRKIG 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1476 EKETKVLALMKMLEDKQEALQEAERTVKALRVEMEDLISSKDDVGKSVHDLERAKrgleafvEEMKTQMEELEDELqvae 1555
Cdd:TIGR02169 720 EIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL-------HKLEEALNDLEARL---- 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1556 daklrlevnsqalRAQHERELQAREEQGEEKRRQLLKQVRELEAELEEERKQRTLASAARKKLEGEVKNTEEQleaasrg 1635
Cdd:TIGR02169 789 -------------SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ------- 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1636 RDEALKQLRKNQGQLKELHRELEEGRAAhkeilasAREAERRCKNLEAEILQMQEMLAAAERARKQAETERDELSEEVAG 1715
Cdd:TIGR02169 849 IKSIEKEIENLNGKKEELEEELEELEAA-------LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 1343958102 1716 GSSGRSLLSDEKRRLEAKISQLEEELEEE------QANVETLNERLRK 1757
Cdd:TIGR02169 922 LKAKLEALEEELSEIEDPKGEDEEIPEEElsledvQAELQRVEEEIRA 969
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1355-1869 |
5.34e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 123.51 E-value: 5.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1355 KQAVERQASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLM---- 1430
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAelar 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1431 ---DLDSQRQLVSNLEKKQKKFDQMLAEERAVSAKSAEERDRAEAELREKETKVLALMKMLEDKQEALQEAERTVKALRV 1507
Cdd:COG1196 300 leqDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1508 EMEDLISSKDDVGKSVHDLERAKRGLEAFVEEMKTQMEELEDELQVAEDAKLRLEVNSQALRaQHERELQAREEQGEEKR 1587
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE-EALEEAAEEEAELEEEE 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1588 RQLLKQVRELEAELEEERKQRTLASAARKKLEgEVKNTEEQLEAASRGRDEALKQLRKNQGQLK-----ELHRELEEGRA 1662
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAA-ARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavAVLIGVEAAYE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1663 AHKEILASAREAERRCKNLEAEILQMQEML------AAAERARKQAETERDELSEEVAGGSSGRSLLSDEKRRLEAKISQ 1736
Cdd:COG1196 538 AALEAALAAALQNIVVEDDEVAAAAIEYLKaakagrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1737 LEEELEEEQANVETLNERLRKSQQLVDQLGAELTAERASSQNREGSRLQLEKQTRDLKAKLQDVESQARSKLKSSVAALE 1816
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE 697
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1343958102 1817 AKLREAEEQLEVESRERQASAKNLRQKEKKLKDLTAQMEDERKQAQDYKDQME 1869
Cdd:COG1196 698 ALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1050-1736 |
1.13e-26 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 119.27 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1050 EKAKRK---VEAELVDLQEQQADLQAQLAELRAQlAAKEEELQTTQACLDEesRQRGAALKRVRDLEALLAELQEDLEAE 1126
Cdd:COG1196 175 EEAERKleaTEENLERLEDILGELERQLEPLERQ-AEKAERYRELKEELKE--LEAELLLLKLRELEAELEELEAELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1127 KVARGKAEAARRDLGEELNSLRSELEdsldttAAQQELRVKREQEMAMLKKAMEDEGRshETQIQELRQKHGQAVEELRE 1206
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELE------ELELELEEAQAEEYELLAELARLEQD--IARLEERRRELEERLEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1207 HLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVELD 1286
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1287 SVTGLLNEAEGRNIKLSKEASSISSQLQDAQELLSEETRQKLNLSGRLRQLEEDKgclmeqlEEEMEAKQAVERQASSLS 1366
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE-------EALLELLAELLEEAALLE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1367 VQLSDLKKRLEELSAAVELLEEgkkrlqrelEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEkkq 1446
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLE---------AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL--- 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1447 kkfDQMLAEERAVSAKSAEERDRAEAELREKETKVLALMKMLEDKQEALQEAERTVKALRVEMEDLISSKDDVGKSVHDL 1526
Cdd:COG1196 545 ---AAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1527 ERAKRGLEAFVEEMKTQMEELEDELQVAEDAKLRLEVNSQALRAQHERELQAREEQGEEKRRQLLKQVRELEAELEEERK 1606
Cdd:COG1196 622 LLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1607 QRTLASAARKKLEGEVKNTEEQLEAASRGRDEALKQLRknqgQLKELHRELEEGRAAHKEILASAREAERRCKNLEAEIL 1686
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE----ELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1343958102 1687 QMQE--MLAAAERARkqAETERDELSEEvaggssgRSLLSDEKRRLEAKISQ 1736
Cdd:COG1196 778 ALGPvnLLAIEEYEE--LEERYDFLSEQ-------REDLEEARETLEEAIEE 820
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
908-1547 |
1.85e-26 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 118.50 E-value: 1.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 908 RLEAKKQELEEvlhemearleeeeeRSISLQQEKKEMEQELQLMEAHIVQEEDARQKLQLEKAAVEGRVKKLEENLLLSE 987
Cdd:COG1196 243 ELEAELEELEA--------------ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 988 DQNNKLQKERKLLEERLADMSSNLAEEEEKSKNLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQ 1067
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1068 ADLQAQLAELRAQLAAKEEELQTTQACLDEESRQRGAALKRVRDLEALLAELQEDLEAEKVARGKAEAARRDLGEELNSL 1147
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1148 RSELEDSLDTTAAQQELRVKREQEMAMLKKAMED-EGRSHETQIQELRQKHGQAVEELREHLEQAKKVRAALEKAKQALE 1226
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADyEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1227 KEAAdlsadLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERvskmtveldsvtGLLNEAEGRNIKLSKEA 1306
Cdd:COG1196 549 QNIV-----VEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALAR------------GAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1307 SSISSQLQDAQELLSEETRQKLNLSGRLRQLEEDKGCLMEQLEEEMEAKQAVERQAsslsvqlsdlKKRLEELSAAVELL 1386
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSR----------RELLAALLEAEAEL 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1387 EEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSAKSAEE 1466
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1467 RDRAEAELREKETKvlalMKMLED-KQEALQEAErtvkALRVEMEDLISSKDdvgksvhDLERAKRGLEAFVEEMKTQME 1545
Cdd:COG1196 762 LEELERELERLERE----IEALGPvNLLAIEEYE----ELEERYDFLSEQRE-------DLEEARETLEEAIEEIDRETR 826
|
..
gi 1343958102 1546 EL 1547
Cdd:COG1196 827 ER 828
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
857-1423 |
2.52e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 115.03 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 857 LKAVREAAAKAEADLKDITQKHSQLVEEQAMLEAKLQAEAELYAEAEDMRVRLEAKKQELEEVLHEMEARLEEEEERSIS 936
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 937 LQQEKKEMEQELQLMEAHIVQEEDARQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLLEERLADMSSNLAEEEE 1016
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1017 KSKNLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQACLD 1096
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1097 EESRQRGAALKRVRDLEALLAELQEDLEAEKVARGKA----------------EAARRDLGEELNSLRSELEDSLDTTAA 1160
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAglrglagavavligveAAYEAALEAALAAALQNIVVEDDEVAA 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1161 QQELRVKREQEMAMLKKAMEDEGRSHETQIQELRQKHGQAVEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALS 1240
Cdd:COG1196 561 AAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1241 STKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQELL 1320
Cdd:COG1196 641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1321 SEETRQKLNLSGRLRQLEEDKGCLMEQLEEEMEAKQAVERQASSLSVQLSDLKKRLEELSA----AVElleegkkrlqrE 1396
Cdd:COG1196 721 LEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPvnllAIE-----------E 789
|
570 580
....*....|....*....|....*..
gi 1343958102 1397 LEAASGDYEEKAAAYDKLEKSRGRLQQ 1423
Cdd:COG1196 790 YEELEERYDFLSEQREDLEEARETLEE 816
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
824-1547 |
3.66e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 114.77 E-value: 3.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 824 RLRNWQWWRLftkvkpLLQVTRQEEEMGQKEEELKAVREAAAKAEADLKDITQKHSQLVEEQAMLEAKLQAEAELYAEAE 903
Cdd:TIGR02168 221 ELRELELALL------VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 904 DMRVRLEAKKQELEEVLHEMEARLEEEEERSISLQQEKKEMEQELQLMEAhivQEEDARQKLQLEKAAVEGRVKKLEENL 983
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE---KLEELKEELESLEAELEELEAELEELE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 984 LLSEDQNNKLQKERKLLEERLADMSSNLAEEEEKSKNLSKLKSKHESMISELEVRLKK-EEKTRQDVEKAKRKVEAELVD 1062
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1063 LQEQQADLQAQLAELRAQLAAKEEELQTTQACLdEESRQRGAALKRVR------------------DLEALLAELQEDLE 1124
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAEREL-AQLQARLDSLERLQenlegfsegvkallknqsGLSGILGVLSELIS 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1125 AEKVARGKAEAArrdLGEELNSLRSE-----------LEDSLDTTAAQQELRVKREQEMAMLKKAMEDEGRSHETQIQEL 1193
Cdd:TIGR02168 531 VDEGYEAAIEAA---LGGRLQAVVVEnlnaakkaiafLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDL 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1194 RQKHGQA-------------VEELREHLEQAKKVRAA-------------------------------------LEKAKQ 1223
Cdd:TIGR02168 608 VKFDPKLrkalsyllggvlvVDDLDNALELAKKLRPGyrivtldgdlvrpggvitggsaktnssilerrreieeLEEKIE 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1224 ALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVELDSVTGLLNEAEGRNIKLS 1303
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1304 KEASSISSQLQDAQELLSEETRQKLNLSGRLRQLEEDKGCLMEQLEEEMEAKQAVERQASSLSVQLSDLKKRLEELSAAV 1383
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1384 ELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSAKS 1463
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1464 AEERDRAEAELREKETKVLALMKMLEDKQEAL--------QEAERTVKALRV--------------EMEDLISSKDDVGK 1521
Cdd:TIGR02168 928 ELRLEGLEVRIDNLQERLSEEYSLTLEEAEALenkieddeEEARRRLKRLENkikelgpvnlaaieEYEELKERYDFLTA 1007
|
810 820
....*....|....*....|....*.
gi 1343958102 1522 SVHDLERAKRGLEAFVEEMKTQMEEL 1547
Cdd:TIGR02168 1008 QKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1202-1855 |
7.75e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 113.49 E-value: 7.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1202 EELREHLEQAKKVRAALEKAKQALEKEAAdlsadlRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERvskm 1281
Cdd:COG1196 182 EATEENLERLEDILGELERQLEPLERQAE------KAERYRELKEELKELEAELLLLKLRELEAELEELEAELEEL---- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1282 TVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQELLSEETRQKLNLSGRLRQLEEDKgclmeqleeemeakQAVERQ 1361
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR--------------RELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1362 ASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVSN 1441
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1442 LEKKQKKFDQMLAEERAVSAKSAEERDRAEAELREKETKVLALMKMLEDKQEALQEAERTVKALRVEMEDLISSKDDVGK 1521
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1522 SVHDLERAKRGLEAfVEEMKTQMEELEDELqvAEDAKLRLEVNSQALRAQHERELQAREEQGEEKRRQLLKQVRELEAEL 1601
Cdd:COG1196 478 ALAELLEELAEAAA-RLLLLLEAEADYEGF--LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1602 EEERKQRTLASAARKKLEgevKNTEEQLEAASRGRDEALKQLRknqgqlkelhRELEEGRAAHKEILASAREAERRCKNL 1681
Cdd:COG1196 555 DDEVAAAAIEYLKAAKAG---RATFLPLDKIRARAALAAALAR----------GAIGAAVDLVASDLREADARYYVLGDT 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1682 EAEILQMQEMLAAAERARKQAETERDELSEEVAGGSSGRSLLSDEKRRLEAKIsqleeeleeeqanvetlnERLRKSQQL 1761
Cdd:COG1196 622 LLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL------------------LEAEAELEE 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1762 VDQLGAELTAERASSQNREGSRLQLEKQTRDLKAKLQDVESQARSKLKSSVAALEAKLREAEEQLEVESRERQASAKNLR 1841
Cdd:COG1196 684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
|
650
....*....|....
gi 1343958102 1842 QKEKKLKDLTAQME 1855
Cdd:COG1196 764 ELERELERLEREIE 777
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1155-1922 |
1.74e-23 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 109.00 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1155 LDTTAAQQELRVKREQEMAMLKKAMEDEGRShETQIQELRQKHGQAVEElREHLEQAKKVRAALEKAKQ-ALEKEAADLS 1233
Cdd:TIGR02169 159 IDEIAGVAEFDRKKEKALEELEEVEENIERL-DLIIDEKRQQLERLRRE-REKAERYQALLKEKREYEGyELLKEKEALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1234 ADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTveldsvtgllneaEGRNIKLSKEASSISSQL 1313
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG-------------EEEQLRVKEKIGELEAEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1314 QDAQELLSEETRQKLNLSGRLRQLEEDKGCLMEQLEEEMEAKQAVERQASSLSVQLSDLKK-------RLEELSAAVELL 1386
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEeledlraELEEVDKEFAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1387 EEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSAKSAEE 1466
Cdd:TIGR02169 384 RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1467 RDRAEAELREKETKVLALMKMLEDKQEALQEAERTVKALRVEMED-------LISSKDDVGKSVHDLERAKRGLEAFVEE 1539
Cdd:TIGR02169 464 LSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGgraveevLKASIQGVHGTVAQLGSVGERYATAIEV 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1540 M---KTQMEELEDELQVAEDAKLRLEVNSQALR-------AQHERELQAREEQG-----------EEKRRQLLKQVRELE 1598
Cdd:TIGR02169 544 AagnRLNNVVVEDDAVAKEAIELLKRRKAGRATflplnkmRDERRDLSILSEDGvigfavdlvefDPKYEPAFKYVFGDT 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1599 AELEEERKQRTLASAARK-KLEGEV----------KNTEEQLEAASRGRDEALKQLRKNQGQLKE----LHRELEEGRAA 1663
Cdd:TIGR02169 624 LVVEDIEAARRLMGKYRMvTLEGELfeksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRelssLQSELRRIENR 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1664 HKEILASAREAERRCKNLEAEILQMQEMLAAAERARKQAETERDELSEEVAGgssgrslLSDEKRRLEAKISQLEEELEE 1743
Cdd:TIGR02169 704 LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN-------VKSELKELEARIEELEEDLHK 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1744 EQANVETLNERLRKSQqlVDQLGAELtaeraSSQNREGSRlqLEKQTRDLKAKLQDVEsQARSKLKSSVAALEAKLREAE 1823
Cdd:TIGR02169 777 LEEALNDLEARLSHSR--IPEIQAEL-----SKLEEEVSR--IEARLREIEQKLNRLT-LEKEYLEKEIQELQEQRIDLK 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1824 EQLEVESRERQASAKNLRQKEKKLKDLTAQMEDERKQAQDYKDQMEKSSARMKQLKHQLEEAEEEAQRVAAARRKLQREL 1903
Cdd:TIGR02169 847 EQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
810
....*....|....*....
gi 1343958102 1904 DEALEANDALSREVSSLRS 1922
Cdd:TIGR02169 927 EALEEELSEIEDPKGEDEE 945
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
940-1736 |
4.02e-22 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 104.76 E-value: 4.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 940 EKKEMEQELQLMEAHIVQEEDARQKLQLEKAavegrvKKLEENLLLSEDQNNKLQKERKLLEERLADMSSNLAEEEEKSK 1019
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLRRERE------KAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1020 NLSKLKSKhesmISELEVRLKKEEKTRQDV-EKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTtqacLDEE 1098
Cdd:TIGR02169 252 ELEKLTEE----ISELEKRLEEIEQLLEELnKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELED----AEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1099 SRQrgaALKRVRDLEALLAELQEDLEAEKVARGKAEAARRDLGEELNSLRSELEDSLDTTAAQQELRVKREQEMAMLKKA 1178
Cdd:TIGR02169 324 LAK---LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1179 MEDEGRSHETQIQELRQKHGQaVEELREHLEQAKKVRAALEKAKQAL-------EKEAADLSADLRALSSTKQDVEQKKK 1251
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEE-LADLNAAIAGIEAKINELEEEKEDKaleikkqEWKLEQLAADLSKYEQELYDLKEEYD 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1252 KVEAQLNDLQLRFSESERQRNELSERV--SKMTVEL-----DSVTGLLNE--------------AEG------------- 1297
Cdd:TIGR02169 480 RVEKELSKLQRELAEAEAQARASEERVrgGRAVEEVlkasiQGVHGTVAQlgsvgeryataievAAGnrlnnvvveddav 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1298 --RNIKLSKE-------------------------------------------ASSISSQLQDAQELLSEETRQKLNLSG 1332
Cdd:TIGR02169 560 akEAIELLKRrkagratflplnkmrderrdlsilsedgvigfavdlvefdpkyEPAFKYVFGDTLVVEDIEAARRLMGKY 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1333 RLRQLEED-------------KGCLMEQLEEEMEAK--------QAVERQASSLSVQLSDLKKRLEELSAA-------VE 1384
Cdd:TIGR02169 640 RMVTLEGElfeksgamtggsrAPRGGILFSRSEPAElqrlrerlEGLKRELSSLQSELRRIENRLDELSQElsdasrkIG 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1385 LLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAvsAKSA 1464
Cdd:TIGR02169 720 EIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI--PEIQ 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1465 EERDRAEAELREKETKVLALMKMLEDKQEALQEAERTVKALRVEMEDLISSKDDVGKSVHDLERAKRGLEAFVEEMKTQM 1544
Cdd:TIGR02169 798 AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1545 EELEDELqvaedAKLRLEVnsqalraqheRELQAREEQGEEKRRQLlkqvreleaeleeerkqrtlaSAARKKLEGEVKN 1624
Cdd:TIGR02169 878 RDLESRL-----GDLKKER----------DELEAQLRELERKIEEL---------------------EAQIEKKRKRLSE 921
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1625 TEEQLEAAsrgrdealkqlrknQGQLKELHRELEEGRAAHKEILaSAREAERRCKNLEAEILQMQEMLAAAERARKQAET 1704
Cdd:TIGR02169 922 LKAKLEAL--------------EEELSEIEDPKGEDEEIPEEEL-SLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLK 986
|
890 900 910
....*....|....*....|....*....|..
gi 1343958102 1705 ERDELSEEvaggssgRSLLSDEKRRLEAKISQ 1736
Cdd:TIGR02169 987 RLDELKEK-------RAKLEEERKAILERIEE 1011
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1398-1926 |
4.11e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 104.63 E-value: 4.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1398 EAA--SGDYEEKAAAYDKLEKSRGRLQqELEDVLMDLDSQRQlvsNLEK---KQKKFDQMLAEERAVSAKSA-------- 1464
Cdd:COG1196 163 EAAgiSKYKERKEEAERKLEATEENLE-RLEDILGELERQLE---PLERqaeKAERYRELKEELKELEAELLllklrele 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1465 EERDRAEAELREKETKVLALMKMLEDKQEALQEAERTVKALRVEMEDLISSKDDVGKSVHDLERAKRGLEAFVEEMKTQM 1544
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1545 EELEDELQVAEDAKLRLEVNSQALRAQHErELQAREEQGEEKRRQLLKQVRELEAELEEERKQRTLASAARKKLEGEVKN 1624
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELE-EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1625 TEEQLEAASRGRDEALKQLRKNQGQLKELHRELEEGRAAHKEILASAREAERRCKNLEAEILQMQEMLAAAERARKQAET 1704
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1705 ERDELSEEVA-------------------GGSSGRSLLSDEKRRLEAKISQLEEELEEEQANVETLNERLRKsQQLVDQL 1765
Cdd:COG1196 478 ALAELLEELAeaaarllllleaeadyegfLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ-NIVVEDD 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1766 GAELTAERASSQNREG--SRLQLEKQtRDLKAKLQDVESQARSKLKSSVAALEAKLREAEEQLEVESRERQASAKNLRQK 1843
Cdd:COG1196 557 EVAAAAIEYLKAAKAGraTFLPLDKI-RARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1844 EKKLKDLTAQMEDERKQAQDYKDQMEKSSARMKQLKHQLEEAEEEAQRVAAARRKLQRELDEALEANDALSREVSSLRSK 1923
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
...
gi 1343958102 1924 LRR 1926
Cdd:COG1196 716 RLE 718
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1170-1882 |
1.57e-21 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 102.50 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1170 QEMAMLKKAMEDegrshetqiqeLRQKHGQAVEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQK 1249
Cdd:pfam15921 120 QEMQMERDAMAD-----------IRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1250 KKKV-----EAQLNDLQLRFSESERQRNELSERVSKMTVELDSVTGLLneaEGRNIKLSKEASSISSQLQDAQELLSEE- 1323
Cdd:pfam15921 189 IRSIlvdfeEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYL---KGRIFPVEDQLEALKSESQNKIELLLQQh 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1324 --------TRQKLNLSGRLRQLEEDKGCLMEQLEEEMEAKQAVERQASSLSVQLSDLKKRLE----ELSAAVELLEEGKK 1391
Cdd:pfam15921 266 qdrieqliSEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSqlrsELREAKRMYEDKIE 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1392 RLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVSnLEKKQKKfdqmLAEERAVSAKSAEERDRAE 1471
Cdd:pfam15921 346 ELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELS-LEKEQNK----RLWDRDTGNSITIDHLRRE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1472 AELREKETKVL-ALMKMLedKQEALQEAERTVKALRVEMEDLisskDDVGKSVHDLERAKRGLEAFVEEMKTQMEELEDE 1550
Cdd:pfam15921 421 LDDRNMEVQRLeALLKAM--KSECQGQMERQMAAIQGKNESL----EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1551 LQVAEDAKLRLEVNSQALRAQHERELQAREEQGEEkrrqlLKQVRELEAELEEERKQRTLASAARKKLEGEVKNTE---E 1627
Cdd:pfam15921 495 ERTVSDLTASLQEKERAIEATNAEITKLRSRVDLK-----LQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEilrQ 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1628 QLE-----AASRGRDEALKQLRKNQ--GQLKELHRELEEGRAAHKEILASAREAERRCKNLEAEILQMQEMLAAAERARK 1700
Cdd:pfam15921 570 QIEnmtqlVGQHGRTAGAMQVEKAQleKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVK 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1701 QAETERDELSEEVAGGSSGRSLLSDEKRRLEAKISQleeELEEEQANVETLNERLRKSQQLVDQLGAELTAERASSQNRE 1780
Cdd:pfam15921 650 DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRN---KSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAM 726
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1781 GSRLQLEKQTRDLKAKLQDVESQAR---------SKLKSSVAALEAKLREAEEQLEVESRERQASAKNLRQKEKKLKDLT 1851
Cdd:pfam15921 727 KVAMGMQKQITAKRGQIDALQSKIQfleeamtnaNKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKV 806
|
730 740 750
....*....|....*....|....*....|....*...
gi 1343958102 1852 AQMEDERKQA-------QDYKDQMEKSSARMKqLKHQL 1882
Cdd:pfam15921 807 ANMEVALDKAslqfaecQDIIQRQEQESVRLK-LQHTL 843
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1121-1878 |
2.46e-21 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 102.07 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1121 EDLEAEKVARGKAEAARRDLGEELNSLRSELEDSLDTTAAQQELRVKREQEMAMLKKAME----------DEGRSHETQI 1190
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALErqkeaierqlASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1191 QELRQKHGQAVEELREHLEQ-AKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESER 1269
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1270 QRNELSERVSKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQELLSEETRQKLNLSGRLRQLEEDKGCLMEQLE 1349
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1350 EEMEAKQAVERQASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELedvl 1429
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL---- 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1430 mdldsqrqlvsnlekkqkkfDQMLAEERAVSAKSAEERDrAEAELREKETKVLALMKMLEDKQEALQEAERTVKALRveM 1509
Cdd:TIGR02169 493 --------------------AEAEAQARASEERVRGGRA-VEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNR--L 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1510 EDLISSKDDVGKSVHDLERAKRGLEA-FVEEMKTQMEELEDELqVAEDAKLRLEVN------------SQALRAQ--HER 1574
Cdd:TIGR02169 550 NNVVVEDDAVAKEAIELLKRRKAGRAtFLPLNKMRDERRDLSI-LSEDGVIGFAVDlvefdpkyepafKYVFGDTlvVED 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1575 ELQAREEQGEEKRRQLLKQVRELEAELEEERKQRTLASAARKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQGQLKELH 1654
Cdd:TIGR02169 629 IEAARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELS 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1655 RELEEGRAAHKEILASAREAERRCKNLEAEILQMQEMLAAAERARKQAETERDELSEEVAGGSSGRSLLSDEKRRLEAKI 1734
Cdd:TIGR02169 709 QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1735 SQLEEELEEEQAN-VETLNERLRKSQQLVDQLGAELTAERA----SSQNREGSRLQLEKQTRDLKAKLQDVESQARsKLK 1809
Cdd:TIGR02169 789 SHSRIPEIQAELSkLEEEVSRIEARLREIEQKLNRLTLEKEylekEIQELQEQRIDLKEQIKSIEKEIENLNGKKE-ELE 867
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1343958102 1810 SSVAALEAKLREAEEQLEVESRERQASAKNLRQKEKKLKDLTAQMEDERKQAQDYKDQMEKSSARMKQL 1878
Cdd:TIGR02169 868 EELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
935-1329 |
1.80e-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: 99.36 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 935 ISLQQEKKEMEQELQLMEAhivQEEDARQKLQlekaavegrvkKLEENLLLSEDQNNKLQKERKLLEERLADMSSNLAEE 1014
Cdd:TIGR02168 673 LERRREIEELEEKIEELEE---KIAELEKALA-----------ELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1015 EEKSKNLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQAC 1094
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1095 LDEESRQRGAALKRVRDLEALLAELQEDLEAEKVARGKAEAARRDLGEELNSLRSELEDSLDTTAAQQELRVKREQEMAm 1174
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE- 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1175 lkkAMEDEGRSHETQIQELRQKHgqavEELREHLEQakkVRAALEKAKQALEKEAADLSADLRAlssTKQDVEQKKKKVE 1254
Cdd:TIGR02168 898 ---ELSEELRELESKRSELRREL----EELREKLAQ---LELRLEGLEVRIDNLQERLSEEYSL---TLEEAEALENKIE 964
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1343958102 1255 AQLNDLQLRFSESERQRNELSErvskmtVELDSVTGlLNEAEGRNIKLSKEASSISS---QLQDAQELLSEETRQKLN 1329
Cdd:TIGR02168 965 DDEEEARRRLKRLENKIKELGP------VNLAAIEE-YEELKERYDFLTAQKEDLTEakeTLEEAIEEIDREARERFK 1035
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1270-1938 |
2.07e-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: 98.98 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1270 QRNELSERVSKMTVELDSVTGLLNEAEGRNIKLSKEASsissQLQDAQELLSEETRQKLNLSG-RLRQLEEdkgclmeql 1348
Cdd:TIGR02168 173 RRKETERKLERTRENLDRLEDILNELERQLKSLERQAE----KAERYKELKAELRELELALLVlRLEELRE--------- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1349 eeemeAKQAVERQASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEdv 1428
Cdd:TIGR02168 240 -----ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA-- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1429 lmdldsqrqlvsNLEKKQKKFDQMLAEERAVSAKSAEERDRAEAELREKETKVLALMKMLEDKQEALQEAERTVKALRVE 1508
Cdd:TIGR02168 313 ------------NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1509 MEDLISSkddvgksVHDLERAKRGLEAFVEEMKTQMEELEDELQVAEDaklRLEVNSQALRAQHERELQAREEQGEEKRR 1588
Cdd:TIGR02168 381 LETLRSK-------VAQLELQIASLNNEIERLEARLERLEDRRERLQQ---EIEELLKKLEEAELKELQAELEELEEELE 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1589 QLLKQVRELEAELEEERKQRTLASAARKKLEGEV------KNTEEQLEAASRGRDEALKQLRKNQGQLKELHR------E 1656
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAERELaqlqarLDSLERLQENLEGFSEGVKALLKNQSGLSGILGvlseliS 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1657 LEEGRAAHKEILASAREAERRCKNLEAeILQMQEMLAAAERAR-------KQAETERDELSEEVAGGSSGRSLLSDEKRR 1729
Cdd:TIGR02168 531 VDEGYEAAIEAALGGRLQAVVVENLNA-AKKAIAFLKQNELGRvtflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVK 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1730 LEAKISQLEEELEEEQANVETLNERLRKSQQL------VDQLGAELTAERAS---SQNREGSRLQLEKQTRDLKAKLQDV 1800
Cdd:TIGR02168 610 FDPKLRKALSYLLGGVLVVDDLDNALELAKKLrpgyriVTLDGDLVRPGGVItggSAKTNSSILERRREIEELEEKIEEL 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1801 ESQARSkLKSSVAALEAKLREAEEQLEVESRERQASAKNLRQKEKKLKDLTAQMEDERKQAQDYKDQMEKSSARMKQLKH 1880
Cdd:TIGR02168 690 EEKIAE-LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1343958102 1881 QLEEAEEEAQRVAAARRKLQRELDEALEANDALSREVSSLRSKLRRGGGEVLTSGQRV 1938
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
858-1586 |
8.78e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 97.52 E-value: 8.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 858 KAVREAAAKAEADLKDITQKHSQLVE-EQAMLEAKLQAEAELYAEAEDMRVRLEAKKQELEEVLHEMEARLEEEEERSIS 936
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKaEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEAR 1170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 937 LQQEKKEMEQELQLMEAHIVQE----EDARqklQLEKAAVEGRVKKLEENLLLSEDQnnKLQKERKLLEERLADMSSNLA 1012
Cdd:PTZ00121 1171 KAEDAKKAEAARKAEEVRKAEElrkaEDAR---KAEAARKAEEERKAEEARKAEDAK--KAEAVKKAEEAKKDAEEAKKA 1245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1013 EEEEKSKNLSKLKSKHESMISELEVRLKKEEKTRQD-VEKAKRKVEAElvDLQEQQADLQAQLAELRAQLAAKEEELQTT 1091
Cdd:PTZ00121 1246 EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADeLKKAEEKKKAD--EAKKAEEKKKADEAKKKAEEAKKADEAKKK 1323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1092 QacldEESRQRGAALKRvrdleallaELQEDLEAEKVARGKAEAARRDL-----GEELNSLRSELEDSLDTTAAQQELRV 1166
Cdd:PTZ00121 1324 A----EEAKKKADAAKK---------KAEEAKKAAEAAKAEAEAAADEAeaaeeKAEAAEKKKEEAKKKADAAKKKAEEK 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1167 KREQEMAmlKKAMEDEGRSHETQIQELRQKHGqavEELREHLEQAKKVRAALEKAKQALEKEAADLSA-DLRALSSTKQD 1245
Cdd:PTZ00121 1391 KKADEAK--KKAEEDKKKADELKKAAAAKKKA---DEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAeEAKKAEEAKKK 1465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1246 VEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQELLSEETR 1325
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1326 QKlnlSGRLRQLEEDKgcLMEQLEEEMEAKQAVERQASSLsvqlsdlkKRLEELSAAvelleeGKKRLQRELEAASGDYE 1405
Cdd:PTZ00121 1546 KK---ADELKKAEELK--KAEEKKKAEEAKKAEEDKNMAL--------RKAEEAKKA------EEARIEEVMKLYEEEKK 1606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1406 EKAAAYDKLEKSRGRlQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSAKSAEERDRAEAELREKEtkvlALM 1485
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIK-AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE----EAK 1681
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1486 KMLEDKQEALQEAERTVKALRvEMEDLISSKDDVGKSVHDLERAKRGLEAFVEEMKTQMEEledELQVAEDAKLRLEVNS 1565
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAK-KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE---DKKKAEEAKKDEEEKK 1757
|
730 740
....*....|....*....|.
gi 1343958102 1566 QALRAQHERELQAREEQGEEK 1586
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEEIRKEKE 1778
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1356-1926 |
4.02e-19 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 94.86 E-value: 4.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1356 QAVERQASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKaaaydklEKSRGRL---QQELEDVLMDL 1432
Cdd:pfam01576 8 QAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEA-------EEMRARLaarKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1433 DSQ--------RQLVSNLEKKQ---KKFDQMLAEERAVSAKSAEERDRAEAELREKETKVLalmkMLEDKQEALQeaeRT 1501
Cdd:pfam01576 81 ESRleeeeersQQLQNEKKKMQqhiQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDIL----LLEDQNSKLS---KE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1502 VKALRVEMEDLISSKDDVGKSVHDLERAKRGLEAFVEEMKTQMEELEDELQVAEDAKLRLEVNSQALRAQHErELQAree 1581
Cdd:pfam01576 154 RKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIA-ELQA--- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1582 QGEEKRRQLLK---QVRELEAELEEERKQRTLASAARKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQGQLKELHRELE 1658
Cdd:pfam01576 230 QIAELRAQLAKkeeELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1659 E--GRAAHKEILASAREAE---------RRCKNLEAEILQM-----------QEMLAAAERAR------KQA-ETERDEL 1709
Cdd:pfam01576 310 DtlDTTAAQQELRSKREQEvtelkkaleEETRSHEAQLQEMrqkhtqaleelTEQLEQAKRNKanlekaKQAlESENAEL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1710 SEEVAGGSSGRSLLSDEKRRLEAKISQLEEELEEEQANVETLNERLRKSQQLVDQLGAELTAERASSQNREGSRLQLEKQ 1789
Cdd:pfam01576 390 QAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQ 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1790 TRDLKAKLQDvESQARSKLKSSVAALEAKLREAEEQLEVESRERQASAKNLRQKEKKLKDLTAQMEDERKQAQDYKDQME 1869
Cdd:pfam01576 470 LQDTQELLQE-ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKK 548
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1343958102 1870 KSSARMKQLKHQLEEAEEEAQRVAAARRKLQRELDEALEANDALSREVSSLRSKLRR 1926
Cdd:pfam01576 549 RLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKK 605
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1002-1485 |
1.17e-18 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 93.44 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1002 ERLADMSSNLAEEEEKSKNLSKLKSKHESMIS-ELEVRLKKEEKTRQDVEKAKRKV---EAELVDLQEQQADLQAQLAEL 1077
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERYAAaRERLAELEYLRAALRLWFAQRRLellEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1078 RAQLAAKEEELQTTQAcldeesRQRGAALKRVRDLEALLAELQEDLEAEKVARGKAEAARRDLG-------EELNSLRSE 1150
Cdd:COG4913 315 EARLDALREELDELEA------QIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGlplpasaEEFAALRAE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1151 LEDSLDTTAAQQELRVKREQEMAMLKKAMEDEGRSHETQIQELRQKHG---QAVEELREHLEQAKK-------------- 1213
Cdd:COG4913 389 AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSnipARLLALRDALAEALGldeaelpfvgelie 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1214 VRAALEKAKQALEK-----------EAADLSADLRAlsstkqdVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMT 1282
Cdd:COG4913 469 VRPEEERWRGAIERvlggfaltllvPPEHYAAALRW-------VNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1283 VELDSVTGLLNEAEGRNIK---------LSKEASSISS-----------QLQDAQELLSE-----ETRQKLN-LSGRLRQ 1336
Cdd:COG4913 542 FKPHPFRAWLEAELGRRFDyvcvdspeeLRRHPRAITRagqvkgngtrhEKDDRRRIRSRyvlgfDNRAKLAaLEAELAE 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1337 LEEDKGCLMEQLEEEMEAKQAVERQASSLS---------VQLSDLKKRLEELSAAVELLEEGK---KRLQRELEAASGDY 1404
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERREALQrlaeyswdeIDVASAEREIAELEAELERLDASSddlAALEEQLEELEAEL 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1405 EEKAAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKK-----FDQMLAE------ERAVSAKSAEERDRAEAE 1473
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelralLEERFAAalgdavERELRENLEERIDALRAR 781
|
570
....*....|..
gi 1343958102 1474 LREKETKVLALM 1485
Cdd:COG4913 782 LNRAEEELERAM 793
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
910-1712 |
1.89e-18 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 92.73 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 910 EAKKQELEEVLHEMEARLEEEEERSISLQQEKKEMEQELQLMEAH----IVQEEDARQKLQLEKAAVEGRVKKLEENLLL 985
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYqlkeKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 986 SEDQNNKLQKERKLLEERLADMSSNLAEEEEKSKNLSKLKSKHESMISE-------LEVRLKKEEKTRQDVEKAKRKVEA 1058
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEElksellkLERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1059 ELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQACLDEESRQRGAALKRVRDLEALLAELQEDLEAEKVARGKAEAARR 1138
Cdd:pfam02463 329 ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQ 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1139 DLGEELNSLRSELEDsldttAAQQELRVKREQEMAMLKKAMEDEGRSHETQIQELRQKHGQAVEELREHLEQAKKVRAAL 1218
Cdd:pfam02463 409 LLLELARQLEDLLKE-----EKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQ 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1219 EKAKQALE--KEAADLSADLRALSSTK------QDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVELDSVTG 1290
Cdd:pfam02463 484 EQLELLLSrqKLEERSQKESKARSGLKvllaliKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEER 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1291 LLNEAEGRNIKLSK-----EASSISSQLQDAQELLSEETRQKLNLSGRLRQLEEDKGCLMEQLEEEMEAKQAVE-----R 1360
Cdd:pfam02463 564 QKLVRALTELPLGArklrlLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLkesakA 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1361 QASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVS 1440
Cdd:pfam02463 644 KESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELL 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1441 NLEKKQKKFDQMLAEERAVSAKSAEERDRAEAELREKETKVLALMKMLEDKQEALQEAERTVKALRVEMEDLISSKDDVG 1520
Cdd:pfam02463 724 ADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1521 KSVHDLERAKRGLEAFVEEMKTQMEELEDELQVAEDAKLRLEVNSQALRAQHERELQAREEQGEEKRRQLLKQVRELEAE 1600
Cdd:pfam02463 804 RALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQK 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1601 LEEERKQRTLASAARKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQGQLKELHRELEEGRAAHKEILASAREAERR--- 1677
Cdd:pfam02463 884 LKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEErnk 963
|
810 820 830
....*....|....*....|....*....|....*
gi 1343958102 1678 CKNLEAEILQMQEMLAAAERARKQAETERDELSEE 1712
Cdd:pfam02463 964 RLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKE 998
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1105-1870 |
2.54e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 92.51 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1105 ALKRVRDLEALLAELQEDLEAEKVARGKAEAARRDlgeelNSLRSELEDSLDTTAAQQELRVKREQEMamlKKAMEDEGR 1184
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKA-----EEAKKKAEDARKAEEARKAEDARKAEEA---RKAEDAKRV 1154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1185 SHETQIQELRQ-KHGQAVEELR--EHLEQAKKVRAALE--KAKQALEKEAADLSADLRALSSTKQ-----DVEQKKKKVE 1254
Cdd:PTZ00121 1155 EIARKAEDARKaEEARKAEDAKkaEAARKAEEVRKAEElrKAEDARKAEAARKAEEERKAEEARKaedakKAEAVKKAEE 1234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1255 AQLNDLQLRFSESERQRNELSERVSKMTVELDSVTGLLNEAEGRNiklskeassiSSQLQDAQELLSEETRQKlnlSGRL 1334
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK----------ADELKKAEEKKKADEAKK---AEEK 1301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1335 RQLEEDKGCLMEQLEEEMEAKQAVERQASSlsvqlSDLKKRLEELSAAVELLEEGKKRLQRELEAAsgdyEEKAAAYDKL 1414
Cdd:PTZ00121 1302 KKADEAKKKAEEAKKADEAKKKAEEAKKKA-----DAAKKKAEEAKKAAEAAKAEAEAAADEAEAA----EEKAEAAEKK 1372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1415 EKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMlaEERAVSAKSAEERDRAEAELREKETkvlaLMKMLEDKQ-- 1492
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADEL--KKAAAAKKKADEAKKKAEEKKKADE----AKKKAEEAKka 1446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1493 -EALQEAERTVKAlrvemEDLISSKDDVGKSVHDLERAKRGLEAfvEEMKTQMEELE---DELQVAEDAKLRLEVNSQAL 1568
Cdd:PTZ00121 1447 dEAKKKAEEAKKA-----EEAKKKAEEAKKADEAKKKAEEAKKA--DEAKKKAEEAKkkaDEAKKAAEAKKKADEAKKAE 1519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1569 RAQHERELQAREEQGEEKRRQLLKQVRELEAEleeeRKQRTLASAARKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQG 1648
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAKKAEEKKKADEL----KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE 1595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1649 QLKELHRELEEGRAAHKEILASAR-EAERRCKNLEAEILQMQEMLAAAERARKQAETERDELSEEVAGGSSGRSLLSDEK 1727
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK 1675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1728 RRLEAKISQLEEELEEEQANVETlnERLRKSQQLvdqlgaeltAERASSQNREGSRLQLEKQTRDLKAKlqdvesqarsk 1807
Cdd:PTZ00121 1676 KAEEAKKAEEDEKKAAEALKKEA--EEAKKAEEL---------KKKEAEEKKKAEELKKAEEENKIKAE----------- 1733
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1343958102 1808 lkssvaalEAKLREAE-----EQLEVESRERQASAKNLRQKEKKLKDLTAQMEDERKQAQDYKDQMEK 1870
Cdd:PTZ00121 1734 --------EAKKEAEEdkkkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRR 1793
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
811-1509 |
3.36e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 91.67 E-value: 3.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 811 AMKVIQRNCACYLRLRNWQwwrlfTKVKPLLQVTRQEEEMGQKEEELKAVREAAAK----AEADLKDITQKHSQLVEEQA 886
Cdd:TIGR02169 215 ALLKEKREYEGYELLKEKE-----ALERQKEAIERQLASLEEELEKLTEEISELEKrleeIEQLLEELNKKIKDLGEEEQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 887 M--------LEAKLQAEAELYAEAEDMRVRLEAKKQELEEVLHEMEARL-------EEEEERSISLQQEKKEMEQELQLM 951
Cdd:TIGR02169 290 LrvkekigeLEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIeelereiEEERKRRDKLTEEYAELKEELEDL 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 952 EAHIVQEEDARQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLLEERLADMSSNLAEEEEKSKNLSKLKSKHESM 1031
Cdd:TIGR02169 370 RAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1032 ISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQACLDEESRQRGAALKRVRD 1111
Cdd:TIGR02169 450 IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQ 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1112 LEALLAELQEDLEAEKVARGKA---------------------------------------------------------- 1133
Cdd:TIGR02169 530 LGSVGERYATAIEVAAGNRLNNvvveddavakeaiellkrrkagratflplnkmrderrdlsilsedgvigfavdlvefd 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1134 --------------------EAARRDLGE--------EL-----------NSLRSELEDSLDTTAAQQELRvKREQEMAM 1174
Cdd:TIGR02169 610 pkyepafkyvfgdtlvvediEAARRLMGKyrmvtlegELfeksgamtggsRAPRGGILFSRSEPAELQRLR-ERLEGLKR 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1175 LKKAMEDEGRSHETQIQELRQKhgqaVEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKVE 1254
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQE----LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1255 AQLNDLQLRFSESERQRNELSERVSKMtvELDSVTGLLNeaegrniKLSKEASSISSQLQDAQELLSEETRQKlnlsgrl 1334
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLEARLSHS--RIPEIQAELS-------KLEEEVSRIEARLREIEQKLNRLTLEK------- 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1335 RQLEEDKGCLMEQLEEEMEAKQAVERQASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKL 1414
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1415 EKSRGRLQQELEDVLMDLDSQRQLVSNLEkKQKKFDQMLAEERAVSAKSAEERDRAEAELREKET----------KVLAL 1484
Cdd:TIGR02169 909 EAQIEKKRKRLSELKAKLEALEEELSEIE-DPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPvnmlaiqeyeEVLKR 987
|
810 820
....*....|....*....|....*
gi 1343958102 1485 MKMLEDKQEALQEaERTVKALRVEM 1509
Cdd:TIGR02169 988 LDELKEKRAKLEE-ERKAILERIEE 1011
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
975-1860 |
5.68e-18 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 91.19 E-value: 5.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 975 RVKKLEENLLLSEDQNNKLQKERKLLEERLADMS-SNLAEEEEKSKNLSKLKSKHEsmiSELEVRLKKEEKTRQdvekaK 1053
Cdd:pfam02463 154 RRLEIEEEAAGSRLKRKKKEALKKLIEETENLAElIIDLEELKLQELKLKEQAKKA---LEYYQLKEKLELEEE-----Y 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1054 RKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQACLDEESRQRGAALKRVRDLEALLAELQEDLEAEKVARGKA 1133
Cdd:pfam02463 226 LLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1134 EAARRDLGEELNSLRSELEDSLDTTAAQQELRVKREQEMAMLKKAMEdegrSHETQIQELRQKHGQAVEELREHLEQAKK 1213
Cdd:pfam02463 306 ERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKRE----AEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1214 VRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVELDSVTGLLN 1293
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1294 eaegrniKLSKEASSISSQLQDAQELLSEETRQKLNLSGRLRQLeedkgcLMEQLEEEMEAKQAVERQASSLSVQLSDLK 1373
Cdd:pfam02463 462 -------KDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEER------SQKESKARSGLKVLLALIKDGVGGRIISAH 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1374 KRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAA----AYDKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKKF 1449
Cdd:pfam02463 529 GRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQklvrALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQL 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1450 DQ--MLAEERAVSAKSAEERDRAEAELREKETKVLALMKMLEDKQEALQEAER-TVKALRVEMEDLISSKDDVGKSVHDL 1526
Cdd:pfam02463 609 DKatLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKsEVKASLSELTKELLEIQELQEKAESE 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1527 ERAKRGLEAFVEEMKTQMEELEDELQVAEDAKLRLEVNSQAL--RAQHERELQAREEQGEEKRRQLLKQVRELEAELEEE 1604
Cdd:pfam02463 689 LAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAqdKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1605 RKQRTLASAARKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQGQLKELHRELEEgraahKEILASAREAERRCKNLEAE 1684
Cdd:pfam02463 769 LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLL-----IEQEEKIKEEELEELALELK 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1685 ILQMQEMLAAAERARKQAETERDELSEEvaggssgrsllSDEKRRLEAKISQLEEELEEEQANVETLNERLRKSQQLVDQ 1764
Cdd:pfam02463 844 EEQKLEKLAEEELERLEEEITKEELLQE-----------LLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLL 912
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1765 LGAELTAERASSQNREGSRLQLEKQTRDLKAKLQDVESQARSKLKSSVAALEAKLREAEEQLEVESRERQASAKNLRQKE 1844
Cdd:pfam02463 913 EEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNK 992
|
890
....*....|....*.
gi 1343958102 1845 KKLKDLTAQMEDERKQ 1860
Cdd:pfam02463 993 DELEKERLEEEKKKLI 1008
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
860-1541 |
7.00e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 90.51 E-value: 7.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 860 VREAAAKAEADLKDITQKHSQLVEEQAMLEAKLQAEAELYAEAEDMRVRLEAKKQELEEVLHEMEARLEEEeersISLQQ 939
Cdd:PRK03918 146 SREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSEL----PELRE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 940 EKKEMEQELQLMEAHIVQEEdarqKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLLEERLADMSSnLAEEEEKSK 1019
Cdd:PRK03918 222 ELEKLEKEVKELEELKEEIE----ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1020 NLSKLKSKHesmiselevrlkkeektrqdvEKAKRKVEAELVDLQEQQADLQAQLAElraqLAAKEEELQTTQacldees 1099
Cdd:PRK03918 297 KLSEFYEEY---------------------LDELREIEKRLSRLEEEINGIEERIKE----LEEKEERLEELK------- 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1100 rqrgaalKRVRDLEALLAELQEDLEAEKVARGKAeaarrdlgEELNSLRSELEDSldttaaQQELRVKREQEMAMLKKAM 1179
Cdd:PRK03918 345 -------KKLKELEKRLEELEERHELYEEAKAKK--------EELERLKKRLTGL------TPEKLEKELEELEKAKEEI 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1180 EDEGRSHETQIQELRQKhgqaVEELREHLEQAKKVRAALEKAKQAL-EKEAADLsadLRALSSTKQDVEQKKKKVEAQLN 1258
Cdd:PRK03918 404 EEEISKITARIGELKKE----IKELKKAIEELKKAKGKCPVCGRELtEEHRKEL---LEEYTAELKRIEKELKEIEEKER 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1259 DLQLRFSESERQRNELSeRVSKMTVELDSVTGLLNEAEGRNIKLSKEASSissqlqdaqelLSEETRQKLN-LSGRLRQL 1337
Cdd:PRK03918 477 KLRKELRELEKVLKKES-ELIKLKELAEQLKELEEKLKKYNLEELEKKAE-----------EYEKLKEKLIkLKGEIKSL 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1338 EEDkgclMEQLEEEMEAKQAVERQASSLSVQLSDLKKRLEELsaAVELLEEGKKRLQrELEAASGDYEEKAAAYDKLEKS 1417
Cdd:PRK03918 545 KKE----LEKLEELKKKLAELEKKLDELEEELAELLKELEEL--GFESVEELEERLK-ELEPFYNEYLELKDAEKELERE 617
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1418 RGRLQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEeravsaKSAEERDRAEAELREKETKVLALMKMLEDKQEALQE 1497
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK------YSEEEYEELREEYLELSRELAGLRAELEELEKRREE 691
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1343958102 1498 AERTVKALRVEMEDLISSKddvgKSVHDLERAKRGLEAFVEEMK 1541
Cdd:PRK03918 692 IKKTLEKLKEELEEREKAK----KELEKLEKALERVEELREKVK 731
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
858-1511 |
3.10e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 89.04 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 858 KAVREAAAKAEADLKDITQKHSQLVEEQAMLEAKLQAEAELYAEAEDMRVRLEAKKQELEEVLHEMEARLEEEEERSISL 937
Cdd:PTZ00121 1152 KRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKK 1231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 938 QQEKKEMEQELQLME-----AHIVQEEDARQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLLEERLADMSSNLA 1012
Cdd:PTZ00121 1232 AEEAKKDAEEAKKAEeernnEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1013 EEEEKSKNLSK-----------LKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAElvDLQEQQADLQAQLAELRAQL 1081
Cdd:PTZ00121 1312 EEAKKADEAKKkaeeakkkadaAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA--EKKKEEAKKKADAAKKKAEE 1389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1082 AAKEEELQTTQacldEESRQRGAALKRVRDLEALLAELQEDLEAEKVA---RGKAEAARRdlgeelnslrseledsldtt 1158
Cdd:PTZ00121 1390 KKKADEAKKKA----EEDKKKADELKKAAAAKKKADEAKKKAEEKKKAdeaKKKAEEAKK-------------------- 1445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1159 aaQQELRVKREQEmamlKKAMEDEGRSHET-QIQELRQKhgqaVEELREHLEQAKKVRAALEKAKQALEKEAADLSADLR 1237
Cdd:PTZ00121 1446 --ADEAKKKAEEA----KKAEEAKKKAEEAkKADEAKKK----AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA 1515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1238 ALSSTKQDVEQKKKKVEAQLNDlQLRFSESERQRNEL--SERVSKMTvELDSVTGLLNEAEGRNIKLSKEASSISSQLQD 1315
Cdd:PTZ00121 1516 KKAEEAKKADEAKKAEEAKKAD-EAKKAEEKKKADELkkAEELKKAE-EKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1316 AQELLSEETRQKLNLSGRLRQLEEDKgclmeQLEEEMEAKQAVERQASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQR 1395
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAK-----IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1396 ELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVlmdlDSQRQLVSNLEKKQKKFDQMLAEE-----RAVSAKSAEERDRA 1470
Cdd:PTZ00121 1669 KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA----KKAEELKKKEAEEKKKAEELKKAEeenkiKAEEAKKEAEEDKK 1744
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1343958102 1471 EAELREKE----TKVLALMKMLEDKQEALQEAERTVKALRVEMED 1511
Cdd:PTZ00121 1745 KAEEAKKDeeekKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1043-1705 |
9.04e-17 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 86.89 E-value: 9.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1043 EKTRQDVEKAKRKVEA--ELVDLQEQQADLQAQLAELRAQLAAkeeelqttqacldeesRQRGAALKRVRDLEALLAELQ 1120
Cdd:COG4913 238 ERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAA----------------LRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1121 EDLEAEKVARGKAEAARRDLGEELNSLRSELEDSldttaaqqelrvkreqemamlkkamedEGRshetQIQELRQKHGQA 1200
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGN---------------------------GGD----RLEQLEREIERL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1201 VEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSErvsk 1280
Cdd:COG4913 351 ERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA---- 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1281 mtvELDSvtgllneaegrnikLSKEASSISSQLQDAQELLSEETRQK---LNLSGRLRQLEEDkgclmeqleeEMEAKQA 1357
Cdd:COG4913 427 ---EIAS--------------LERRKSNIPARLLALRDALAEALGLDeaeLPFVGELIEVRPE----------EERWRGA 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1358 VER----QASSLSVQLSDLKK-----------------RLEELSAAVELLEEGKKRLQRELEAASGDYEekAAAYDKLEK 1416
Cdd:COG4913 480 IERvlggFALTLLVPPEHYAAalrwvnrlhlrgrlvyeRVRTGLPDPERPRLDPDSLAGKLDFKPHPFR--AWLEAELGR 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1417 SRGRL----QQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSAKSAEERDRAEAELREKETKVLALMKMLEDKQ 1492
Cdd:COG4913 558 RFDYVcvdsPEELRRHPRAITRAGQVKGNGTRHEKDDRRRIRSRYVLGFDNRAKLAALEAELAELEEELAEAEERLEALE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1493 EALQEAERTVKALRvEMEDLISSKDDVG---KSVHDLERAKRGLEAF---VEEMKTQMEELEDELQVAEDAKLRLEVNSQ 1566
Cdd:COG4913 638 AELDALQERREALQ-RLAEYSWDEIDVAsaeREIAELEAELERLDASsddLAALEEQLEELEAELEELEEELDELKGEIG 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1567 ALRAQHEReLQAREEQGEEKRRQLLKQVRELEAELEEERKQRTLASAARKKLegeVKNTEEQLEAASRGRDEALKQLRKn 1646
Cdd:COG4913 717 RLEKELEQ-AEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL---RENLEERIDALRARLNRAEEELER- 791
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1343958102 1647 qgQLKELHRELEEGRAAHKEILASAREAERRCKNLEAEILQMQEmlAAAERARKQAETE 1705
Cdd:COG4913 792 --AMRAFNREWPAETADLDADLESLPEYLALLDRLEEDGLPEYE--ERFKELLNENSIE 846
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1048-1775 |
1.99e-16 |
|
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: 86.16 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1048 DVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQACLD---EESRQRGAALKRVRDLEAL---LAELQE 1121
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNlvqTALRQQEKIERYQEDLEELterLEEQEE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1122 DLEAEKVARGKAEAARRDLGEELNSLRSELED---SLDT--TAA---QQELRVKRE-QEMAMLKKAMEDEGRSHETQIQE 1192
Cdd:COG3096 369 VVEEAAEQLAEAEARLEAAEEEVDSLKSQLADyqqALDVqqTRAiqyQQAVQALEKaRALCGLPDLTPENAEDYLAAFRA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1193 LRQKHGQAVEELREHLEQAKKVRAALEKAKQALEKEAADLSADlRALSSTKQDVE---------QKKKKVEAQLNDLQLR 1263
Cdd:COG3096 449 KEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERS-QAWQTARELLRryrsqqalaQRLQQLRAQLAELEQR 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1264 FS---ESERQRNELSERVSKMTVELDSVTGLLNEAEGRNIKLSKEASSIS---SQLQDAQELLS---EETRQK----LNL 1330
Cdd:COG3096 528 LRqqqNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVeqrSELRQQLEQLRariKELAARapawLAA 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1331 SGRLRQLEEDKGCLMEQLEEEMEAKQAV---ERQASSLSVQLSDLKKRLEelSAAVELLEEG---KKRLQRELEAASGD- 1403
Cdd:COG3096 608 QDALERLREQSGEALADSQEVTAAMQQLlerEREATVERDELAARKQALE--SQIERLSQPGgaeDPRLLALAERLGGVl 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1404 ----YEEKA---AAY--------------DKLEKSRGRLQQeLEDVLMDL---------------------------DSQ 1435
Cdd:COG3096 686 lseiYDDVTledAPYfsalygparhaivvPDLSAVKEQLAG-LEDCPEDLyliegdpdsfddsvfdaeeledavvvkLSD 764
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1436 RQL-VS---------------NLEKKQKKFDQmLAEERAVSAKSAEERDRAEAELREKETKVLALM------KMLEDKQE 1493
Cdd:COG3096 765 RQWrYSrfpevplfgraarekRLEELRAERDE-LAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAfapdpeAELAALRQ 843
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1494 ALQEAERTVKALRVEMEDLISSKDDVGKSVHDLERAKRGLEAFVEEMKTQ-MEELEDELQVAEDAKLRLEVNSQALR--- 1569
Cdd:COG3096 844 RRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADrLEELREELDAAQEAQAFIQQHGKALAqle 923
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1570 ----------AQHErELQAREEQGEEKRRQL------LKQVRELEAELEEERKQRTLA--SAARKKLEgevknteEQLEA 1631
Cdd:COG3096 924 plvavlqsdpEQFE-QLQADYLQAKEQQRRLkqqifaLSEVVQRRPHFSYEDAVGLLGenSDLNEKLR-------ARLEQ 995
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1632 ASRGRDEALKQLRKNQGQLKELHRELEEGRAAHKEILASAREAERRcknleaeilqMQEM-LAAAERARKQAETERDELS 1710
Cdd:COG3096 996 AEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQE----------LEELgVQADAEAEERARIRRDELH 1065
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1343958102 1711 EEVAGGSSGRSLLSDEKRRLEAKISQleeeleeeqanvetLNERLRKSQQLVDQLGAELTAERAS 1775
Cdd:COG3096 1066 EELSQNRSRRSQLEKQLTRCEAEMDS--------------LQKRLRKAERDYKQEREQVVQAKAG 1116
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1168-1906 |
6.68e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.42 E-value: 6.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1168 REQEMAMLKKAMEDEGRSHETQIQElrqkhgQAVEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVE 1247
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEEAFGKAE------EAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAED 1150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1248 QKKKKVEAQLNDLQlRFSESERQRNELSERVSKMTVELDSVTGLLNEAEGRNIklskEASSISSQLQDAQELLSEETRQK 1327
Cdd:PTZ00121 1151 AKRVEIARKAEDAR-KAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKA----EAARKAEEERKAEEARKAEDAKK 1225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1328 LNlsgRLRQLEEDKgclmeqlEEEMEAKQAVERQASSLSVQLSDLKKRLEELSAAVELLEEgkKRLQRELEAAsgdyEEK 1407
Cdd:PTZ00121 1226 AE---AVKKAEEAK-------KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE--ARKADELKKA----EEK 1289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1408 AAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKKFDQmlAEERAVSAKSAEERDRAEAELREKETKvlALMKM 1487
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA--AKKKAEEAKKAAEAAKAEAEAAADEAE--AAEEK 1365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1488 LEDKQEALQEAERTVKALRVEMEDLISSKDDVGKSVHDLERAKRGLEAfvEEMKTQMEELE---DELQVAEDAKLRLEVN 1564
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKA--AAAKKKADEAKkkaEEKKKADEAKKKAEEA 1443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1565 SQALRAQHERElQAREEQGEEKRRQLLKQVRELEAELEEERKqrtlASAARKKLEgEVKNTEEQLEAASRGRDEALKQLR 1644
Cdd:PTZ00121 1444 KKADEAKKKAE-EAKKAEEAKKKAEEAKKADEAKKKAEEAKK----ADEAKKKAE-EAKKKADEAKKAAEAKKKADEAKK 1517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1645 KNQGQLKELHRELEEGRAAHKeilasAREAERRCKnleAEILQMQEMLAAAERARKQAETERDELSEEVAggssgrslls 1724
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADE-----AKKAEEKKK---ADELKKAEELKKAEEKKKAEEAKKAEEDKNMA---------- 1579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1725 deKRRleAKISQLEEELEEEQANVETLNERLRKSQQLVDQLGAELTAERASSQNREgsrlqlEKQTRDLKAKLQDVESQA 1804
Cdd:PTZ00121 1580 --LRK--AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE------KKKVEQLKKKEAEEKKKA 1649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1805 RSKLKssvAALEAKLREAEEQLEVESRERQA-SAKNLRQKEKKLKDLTAQMEDERKQAQDYKDQMEKSSARMKQLKHQLE 1883
Cdd:PTZ00121 1650 EELKK---AEEENKIKAAEEAKKAEEDKKKAeEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726
|
730 740
....*....|....*....|...
gi 1343958102 1884 EAEEEAQRVAAARRKLQRELDEA 1906
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKKKAEEA 1749
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1082-1448 |
1.05e-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: 83.58 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1082 AAKEEELQTTQACLDEESRQRGAALKRVRDLEALLAELQEDLEAEKVARGKAEAARRDLGEELNSLRSELEDSLDTTAAQ 1161
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1162 QELRVKREQEMAMLKK---AMEDEGRSHETQIQELRQKHGQA-VEELREHLEQAKKVRAALEKAKQALEKEaadlsadLR 1237
Cdd:TIGR02169 750 EQEIENVKSELKELEArieELEEDLHKLEEALNDLEARLSHSrIPEIQAELSKLEEEVSRIEARLREIEQK-------LN 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1238 ALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQ 1317
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1318 EllseetrqklnlsgRLRQLEEDKGCLMEQLEEEMEAKQAVERQASslsvQLSDLKKRLEELSAAV---ELLEEGKKRLQ 1394
Cdd:TIGR02169 903 R--------------KIEELEAQIEKKRKRLSELKAKLEALEEELS----EIEDPKGEDEEIPEEElslEDVQAELQRVE 964
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1343958102 1395 RELEA-------ASGDYEEKAAAYDKLEKSRGRLQQELEDVLmdldsqrQLVSNLEKKQKK 1448
Cdd:TIGR02169 965 EEIRAlepvnmlAIQEYEEVLKRLDELKEKRAKLEEERKAIL-------ERIEEYEKKKRE 1018
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
858-1476 |
2.54e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 82.27 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 858 KAVREAAAKAEADLKDITQKHSQLVEEQAMLEAkLQAEAELYAEAEDMRVRLEAKKQELEEV-LHEMEARLEEEEERSIS 936
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREQIEL-LEPIRELAERYAAARERLAELEYLRAALrLWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 937 LQQEKKEMEQELQLMEAHIVQEEDARQKLQLEKAAVEG-RVKKLEENLLLSEDQNNKLQKERKLLEERLADMSSNLAEEE 1015
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIRGNGGdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1016 E----KSKNLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAA----KEEE 1087
Cdd:COG4913 380 EefaaLRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEalglDEAE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1088 LQTtqAC-----LDEESRQRGAA-----------LKRVRDLEALLA-----ELQEDLEAEKVARGKAEAARRDLGEelNS 1146
Cdd:COG4913 460 LPF--VGelievRPEEERWRGAIervlggfaltlLVPPEHYAAALRwvnrlHLRGRLVYERVRTGLPDPERPRLDP--DS 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1147 LRSELEdsLDTTAAQQELR-----------VKREQEMAMLKKAMEDEG------RSHE------------------TQIQ 1191
Cdd:COG4913 536 LAGKLD--FKPHPFRAWLEaelgrrfdyvcVDSPEELRRHPRAITRAGqvkgngTRHEkddrrrirsryvlgfdnrAKLA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1192 ELRQKhgqaVEELREHLEQAKKVRAALEKAKQALEKEAADLSAdLRALSSTKQDVEQkkkkVEAQLNDLqlrfsesERQR 1271
Cdd:COG4913 614 ALEAE----LAELEEELAEAEERLEALEAELDALQERREALQR-LAEYSWDEIDVAS----AEREIAEL-------EAEL 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1272 NEL---SERVSKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQELLSEetrqklnLSGRLRQLEEDKGCLMEQL 1348
Cdd:COG4913 678 ERLdasSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE-------LQDRLEAAEDLARLELRAL 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1349 EEEMEAKQAVERQASSLSVQLSDLKKRL-EELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQEled 1427
Cdd:COG4913 751 LEERFAAALGDAVERELRENLEERIDALrARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEED--- 827
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1343958102 1428 vlmdldsqrqlvsNLEKKQKKFDQMLAE--ERAVS---AKSAEERDRAEAELRE 1476
Cdd:COG4913 828 -------------GLPEYEERFKELLNEnsIEFVAdllSKLRRAIREIKERIDP 868
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1243-1912 |
3.57e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 82.11 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1243 KQDVEQKKKKVEAQLNDLQlRFSESERQRNELSERVSKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQELLSE 1322
Cdd:PTZ00121 1052 IDGNHEGKAEAKAHVGQDE-GLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKA 1130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1323 ETRQKLNLSGRL---RQLEEDKgclmeqleEEMEAKQAVERQASSLSVQLSDLKK-----RLEELSAAVEL--------L 1386
Cdd:PTZ00121 1131 EEARKAEDARKAeeaRKAEDAK--------RVEIARKAEDARKAEEARKAEDAKKaeaarKAEEVRKAEELrkaedarkA 1202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1387 EEGKK--RLQRELEAASGDYEEKAAAYDKLEKSRGRLQQ--------------ELEDVLMDLDSQRQLVSNLEKKQKKFD 1450
Cdd:PTZ00121 1203 EAARKaeEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEakkaeeernneeirKFEEARMAHFARRQAAIKAEEARKADE 1282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1451 QMLAEE--RAVSAKSAEERDRAEAELREKETKvlalmKMLEDKQEALQEAERTVKALRVEMEDLiSSKDDVGKSvhDLER 1528
Cdd:PTZ00121 1283 LKKAEEkkKADEAKKAEEKKKADEAKKKAEEA-----KKADEAKKKAEEAKKKADAAKKKAEEA-KKAAEAAKA--EAEA 1354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1529 AKRGLEAFVEEMKTQMEELEDELQVAEDAKLRLEVNSQAlraqheRELQAREEQGEEKRRQLLKQVRELEAELEEERK-- 1606
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA------DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKae 1428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1607 QRTLASAARKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQGQLKELHRELEEGRAAhKEILASAREAERRCKNLE--AE 1684
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADEAKkaAE 1507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1685 ILQMQEMLAAAERARKQAETERDELSEEvaggssgrsllSDEKRRLEAKISQLEEELEEEQANVETLNERLRKSQQLVDQ 1764
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAKKAEEAKK-----------ADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK 1576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1765 LGAELTAERASSQNREGSRLQLEKQTRDLKAKLQDVESQARSKLKSSVAALEAKLREAEEQLEVESRERQASAKNLRQKE 1844
Cdd:PTZ00121 1577 NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1343958102 1845 KKLKDLTAQMEDERKQAQDYKDQMEKSSARMKQLKHQLEEAEEEAQRVAAARRKLQRELDEALEANDA 1912
Cdd:PTZ00121 1657 EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA 1724
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
857-1485 |
4.16e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 81.62 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 857 LKAVREAAAKAEADLKDI--------TQKHSQLVE-EQAMLEAKLQAEAELYAEAEDMRVRLEAKKQELEEVLHEMEARL 927
Cdd:PRK02224 164 LEEYRERASDARLGVERVlsdqrgslDQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 928 EEEEERsislQQEKKEMEQELQLMEAHIVQEEDARQKLqleKAAVEGRVKKLEEnlllsedqnnklqkerklLEERLADM 1007
Cdd:PRK02224 244 EEHEER----REELETLEAEIEDLRETIAETEREREEL---AEEVRDLRERLEE------------------LEEERDDL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1008 SSNLAEEEEKSKNLSKLKSKHESMISELEVRLkkeEKTRQDVEKAKRKVEAelvdLQEQQADLQAQLAELRAQLAAKEEE 1087
Cdd:PRK02224 299 LAEAGLDDADAEAVEARREELEDRDEELRDRL---EECRVAAQAHNEEAES----LREDADDLEERAEELREEAAELESE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1088 LQTTQACLDEESrqrgaalKRVRDLEALLAELQEDLEAEKVARGKAEAARRDLGEELNSLRSELEdslDTTAAQQELRVK 1167
Cdd:PRK02224 372 LEEAREAVEDRR-------EEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA---ELEATLRTARER 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1168 REQEMAMLKKA------MEDEGRSHETQIQELRQKhgqaVEELREHLEQAKKVRAALEKAKQALEkeaadlsaDLRALSS 1241
Cdd:PRK02224 442 VEEAEALLEAGkcpecgQPVEGSPHVETIEEDRER----VEELEAELEDLEEEVEEVEERLERAE--------DLVEAED 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1242 TKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAqells 1321
Cdd:PRK02224 510 RIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAEL----- 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1322 EETRQKLNLSGRLRQLEEDKGCLMEQLEEEMEAKQAVERQASSlsvQLSDLKKRLEELS-----AAVELLEEGKKRLQRE 1396
Cdd:PRK02224 585 KERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRE---RLAEKRERKRELEaefdeARIEEAREDKERAEEY 661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1397 LEAASGDYEEKAAAYDKLEKSRGRLQQELEdvlmDLDSQRQLVSNLEKKQKKFDQMLAEERAVSAKSAEERdraeAELRE 1476
Cdd:PRK02224 662 LEQVEEKLDELREERDDLQAEIGAVENELE----ELEELRERREALENRVEALEALYDEAEELESMYGDLR----AELRQ 733
|
....*....
gi 1343958102 1477 KETKVLALM 1485
Cdd:PRK02224 734 RNVETLERM 742
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
857-1540 |
5.25e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 81.73 E-value: 5.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 857 LKAVREAAAKAE------------ADLKDITQKHSQLVEEQAMLEAKLQAEAELYAEAEDMRVRLEAKKQelEEVLHEME 924
Cdd:PTZ00121 1229 VKKAEEAKKDAEeakkaeeernneEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKA--EEKKKADE 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 925 ARLEEEEERSIslQQEKKEMEQELQLMEAHIVQEEDARQKLQLEKAAVEGRVKKLEenlllSEDQNNKLQKERKLLEERL 1004
Cdd:PTZ00121 1307 AKKKAEEAKKA--DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAE-----AAEEKAEAAEKKKEEAKKK 1379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1005 ADMSSNLAEEEEKSKNLSKLKSKHESMISElevrLKKEEKTRQDVEKAKRKVEAElvdlqeqqadLQAQLAELRAQLAAK 1084
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEAKKKAEEDKKKADE----LKKAAAAKKKADEAKKKAEEK----------KKADEAKKKAEEAKK 1445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1085 EEEL--QTTQACLDEESRQRGAALKRVRDLEALLAELQEDLEAEKVA---RGKAEAARRdlGEELNSLRSELEDSLDTTA 1159
Cdd:PTZ00121 1446 ADEAkkKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAeeaKKKADEAKK--AAEAKKKADEAKKAEEAKK 1523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1160 AQQELRVKREQEMAMLKKAMEDEGRSHETQIQELRQ-KHGQAVEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRA 1238
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE 1603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1239 LSSTKqdVEQKKKKVEAQLNDLQLRFSESERQRNELSERvsKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQE 1318
Cdd:PTZ00121 1604 EKKMK--AEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK--KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1319 LLSEETRQKLNLSGRLRQLEEDKGCLMEQLEEEMEAKQAVErqasslsvqlsdLKKRLEELSAAVELLEEGKKRLQRELE 1398
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE------------LKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1399 AASGDYEEK---AAAYDKLEKSRGRLQQELEDVLmdldsQRQLVSNLEKKQKKFDQMLAEERAVSAKSAEERDRAEAELR 1475
Cdd:PTZ00121 1748 EAKKDEEEKkkiAHLKKEEEKKAEEIRKEKEAVI-----EEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVIN 1822
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1343958102 1476 E-KETKVLALMKMLEDKQEALQEAERTVKalRVEMEDLISSKDdvGKSVHDLERAKRGLEAFVEEM 1540
Cdd:PTZ00121 1823 DsKEMEDSAIKEVADSKNMQLEEADAFEK--HKFNKNNENGED--GNKEADFNKEKDLKEDDEEEI 1884
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1198-1863 |
5.62e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 81.11 E-value: 5.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1198 GQAVEELREHLEQAKKVRAALEKAKQALEkeaadLSADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSEseRQRNELSER 1277
Cdd:COG4913 224 FEAADALVEHFDDLERAHEALEDAREQIE-----LLEPIRELAERYAAARERLAELEYLRAALRLWFAQ--RRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1278 VSKMTVELDSVTGLLNEAEgrniklskeassisSQLQDAQELLSEETRQKLNLSG-RLRQLEEDKgclmeqlEEEMEAKQ 1356
Cdd:COG4913 297 LEELRAELARLEAELERLE--------------ARLDALREELDELEAQIRGNGGdRLEQLEREI-------ERLERELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1357 AVERQASSLSVQLSDLKkrlEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLDSQR 1436
Cdd:COG4913 356 ERERRRARLEALLAALG---LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1437 QLVSNLEKKQKKFDQMLAEERAVSA------------KSAEERDRAEAElreketKVL---ALMKMLEDK--QEALQEAE 1499
Cdd:COG4913 433 RRKSNIPARLLALRDALAEALGLDEaelpfvgelievRPEEERWRGAIE------RVLggfALTLLVPPEhyAAALRWVN 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1500 RTVKALRVEMEdlisskdDVGKSVHDLERAKRGLEAFVEEMKTQMEELEDELQ--VAEDAKLRLEVNSQALRaQHERELQ 1577
Cdd:COG4913 507 RLHLRGRLVYE-------RVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEaeLGRRFDYVCVDSPEELR-RHPRAIT 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1578 aREEQGEEKRRQLLKQVReleaelEEERKQRTLASAARKK---LEGEVKNTEEQLEAASRgRDEALKQLRKNQGQLKELH 1654
Cdd:COG4913 579 -RAGQVKGNGTRHEKDDR------RRIRSRYVLGFDNRAKlaaLEAELAELEEELAEAEE-RLEALEAELDALQERREAL 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1655 RELEEGRAAHKEILASAREAERrcknLEAEILQMQE---MLAAAERARKQAETERDELSEEVAGgssgrslLSDEKRRLE 1731
Cdd:COG4913 651 QRLAEYSWDEIDVASAEREIAE----LEAELERLDAssdDLAALEEQLEELEAELEELEEELDE-------LKGEIGRLE 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1732 AKISQLEEELEEEQANVETLNERlrkSQQLVDQLGAELTAERASSQNREGSRLQLEKQTRDLKAKLQDVESQARSKLKS- 1810
Cdd:COG4913 720 KELEQAEEELDELQDRLEAAEDL---ARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAf 796
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1343958102 1811 -------------SVAALE---AKLREAEEQLEVESRERQASAKNlRQKEKKLKDLTAQMEDERKQAQD 1863
Cdd:COG4913 797 nrewpaetadldaDLESLPeylALLDRLEEDGLPEYEERFKELLN-ENSIEFVADLLSKLRRAIREIKE 864
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
940-1562 |
5.93e-15 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 80.83 E-value: 5.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 940 EKKEMEQELQLMEAHIVQEEDARQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLLEERLADMSSNLAEEEEKSK 1019
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1020 NLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQACLDEES 1099
Cdd:TIGR04523 114 NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1100 RQRGAALKRVRDLEALLaELQEDLEAEKvargkaeaarrdlgEELNSLRSELEDSLdttaaqQELRVKREQEMAMLKKAm 1179
Cdd:TIGR04523 194 NKLLKLELLLSNLKKKI-QKNKSLESQI--------------SELKKQNNQLKDNI------EKKQQEINEKTTEISNT- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1180 edegrshETQIQELRQKHGQAVEELRE---HLEQAKKVRAALEKAKQALEKEAADLSADLRA--LSSTKQDVEQKKKKVE 1254
Cdd:TIGR04523 252 -------QTQLNQLKDEQNKIKKQLSEkqkELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwNKELKSELKNQEKKLE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1255 aqlnDLQLRFSESERQRNELSERVSKMTVELDSVTG----LLNEAEGRNIKLSKEASSISSQLQDAQELLSeetrQKLNL 1330
Cdd:TIGR04523 325 ----EIQNQISQNNKIISQLNEQISQLKKELTNSESenseKQRELEEKQNEIEKLKKENQSYKQEIKNLES----QINDL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1331 SGRLRQLEEDKGCLMEQLEEEMEAKQAVERQASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAA 1410
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRS 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1411 YDKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSAKSAEERDRAEAELREKETKVLALMKML-- 1488
Cdd:TIGR04523 477 INKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkk 556
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1343958102 1489 EDKQEALQEAERTVKALRVEMEDLISSKDDVGKSVHDLERAKRGLEAFVEEMKTQMEELEDELQVAEDAKLRLE 1562
Cdd:TIGR04523 557 ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
994-1718 |
7.46e-15 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 81.16 E-value: 7.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 994 QKERKLLEERLADMSSNLAEEEEKSKNL---SKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEA--ELVDL-QEQQ 1067
Cdd:PRK04863 299 RRQLAAEQYRLVEMARELAELNEAESDLeqdYQAASDHLNLVQTALRQQEKIERYQADLEELEERLEEqnEVVEEaDEQQ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1068 ADLQAQLA-------ELRAQLAAKEE--ELQTTQACldeESRQRGAALKRVR---DLEALLAELQEDLEAEKVARGKAea 1135
Cdd:PRK04863 379 EENEARAEaaeeevdELKSQLADYQQalDVQQTRAI---QYQQAVQALERAKqlcGLPDLTADNAEDWLEEFQAKEQE-- 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1136 arrdLGEELNSLRSELEDSLDT----TAAQQELR-----VKREQEMAMLKKAMED--EGRSHETQIQELRQKHGQAVEEL 1204
Cdd:PRK04863 454 ----ATEELLSLEQKLSVAQAAhsqfEQAYQLVRkiageVSRSEAWDVARELLRRlrEQRHLAEQLQQLRMRLSELEQRL 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1205 REH------LEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNE----- 1273
Cdd:PRK04863 530 RQQqraerlLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaaq 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1274 --------------------------LSERVSKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQE-----LLSE 1322
Cdd:PRK04863 610 dalarlreqsgeefedsqdvteymqqLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAErfggvLLSE 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1323 ------------------ETRQKL---NLSGRLRQLEEDKGCLM------EQLEEEMEAKQAVERQASSLSVQLSDLK-- 1373
Cdd:PRK04863 690 iyddvsledapyfsalygPARHAIvvpDLSDAAEQLAGLEDCPEdlylieGDPDSFDDSVFSVEELEKAVVVKIADRQwr 769
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1374 ----------------KRLEELSAAVELLEEG-------KKRLQRELEAASGDYEEKAA-AYD-----KLEKSRGRLQqE 1424
Cdd:PRK04863 770 ysrfpevplfgraareKRIEQLRAEREELAERyatlsfdVQKLQRLHQAFSRFIGSHLAvAFEadpeaELRQLNRRRV-E 848
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1425 LEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSAKSAEER--DRAEaELREKETKVLALMKMLEDKQEALQEAERTV 1502
Cdd:PRK04863 849 LERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETlaDRVE-EIREQLDEAEEAKRFVQQHGNALAQLEPIV 927
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1503 KALRVEMEDLISSKDDVGKSVHDLERAKRGLEAfveemktqmeeLEDELQVA-----EDAKLRLEVNSQ---ALRAQHER 1574
Cdd:PRK04863 928 SVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFA-----------LTEVVQRRahfsyEDAAEMLAKNSDlneKLRQRLEQ 996
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1575 ELQAREEQGEEKRRQL-----LKQVRELEAELEEeRKQRTLASAARKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQGQ 1649
Cdd:PRK04863 997 AEQERTRAREQLRQAQaqlaqYNQVLASLKSSYD-AKRQMLQELKQELQDLGVPADSGAEERARARRDELHARLSANRSR 1075
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1343958102 1650 LKELHRELEEGRAAHKEILASAREAERRCKNLEAEILQMQEMLAAAERARKQAETERDELSEEVAGGSS 1718
Cdd:PRK04863 1076 RNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVERRLHRRELAYLSA 1144
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
29-73 |
1.35e-14 |
|
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: 69.38 E-value: 1.35e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1343958102 29 AAKKMVWVPSEREGFEAASIREEKGEQVLVELSNGQKVTVSKDDI 73
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
867-1165 |
1.60e-14 |
|
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: 79.73 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 867 AEADLKDITQKHSQLVEEQAMLEAKLQAEAELYAEAEDMRVRLEAKKQELEEVLHEMEAR-----LEEEEERSISLQQEK 941
Cdd:TIGR02169 721 IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlndleARLSHSRIPEIQAEL 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 942 KEMEQELQLMEAHIVQEEDARQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLLEERLADMSSNLAEeeeksknl 1021
Cdd:TIGR02169 801 SKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE-------- 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1022 sklkskHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQACLDEESRQ 1101
Cdd:TIGR02169 873 ------LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI 946
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1343958102 1102 RGAALKrVRDLEALLAELQEDLEAEKVARGKA-------EAARRDLGEELNSLRSELEDSLDTTAAQQELR 1165
Cdd:TIGR02169 947 PEEELS-LEDVQAELQRVEEEIRALEPVNMLAiqeyeevLKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1106-1666 |
1.79e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 79.34 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1106 LKRVRDLEALLAELQEDLEAEKVARGKAEAARRDLGEELNSLRSELEDSLDTTAAQQELRVKreqemamlKKAMEDEGRS 1185
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKE--------LESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1186 HETQIQELRQKhgqaVEELREHLEQAKKVRAALEKAKQaLEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLQLRFS 1265
Cdd:PRK03918 257 LEEKIRELEER----IEELKKEIEELEEKVKELKELKE-KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1266 ESErqrnELSERVSKMTVELDSVTGLLNEAEGRnIKLSKEASSISSQLQDAQELLSEETRQKLNlsgrlRQLEEDKgclm 1345
Cdd:PRK03918 332 ELE----EKEERLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLTGLTPEKLE-----KELEELE---- 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1346 eqleeemEAKQAVERQASSLSVQLSDLKKRLEELSAAV---------------ELLEEGKKRLQRELEAASGDYEEKAAA 1410
Cdd:PRK03918 398 -------KAKEEIEEEISKITARIGELKKEIKELKKAIeelkkakgkcpvcgrELTEEHRKELLEEYTAELKRIEKELKE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1411 YDKLEKsrgRLQQELEDVLMDLDSQRQLVS---------NLEKKQKKFDQMLAEERAVSAKSAEER-DRAEAELR--EKE 1478
Cdd:PRK03918 471 IEEKER---KLRKELRELEKVLKKESELIKlkelaeqlkELEEKLKKYNLEELEKKAEEYEKLKEKlIKLKGEIKslKKE 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1479 TKVL-ALMKMLEDKQEALQEAERTVKALRVEMEDL-ISSKDDVGKSVHDLERAKR---GLEAFVEEMKTQMEELEDELQV 1553
Cdd:PRK03918 548 LEKLeELKKKLAELEKKLDELEEELAELLKELEELgFESVEELEERLKELEPFYNeylELKDAEKELEREEKELKKLEEE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1554 AEDAKLRLEVNSQALRAQHERELQAREEQGEEKRRQLLKQVRELEAELEEERKQRTLASAARKKLEGEVKNTEEQLEAAS 1633
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
570 580 590
....*....|....*....|....*....|...
gi 1343958102 1634 RGRDEaLKQLRKNQGQLKELHRELEEGRAAHKE 1666
Cdd:PRK03918 708 KAKKE-LEKLEKALERVEELREKVKKYKALLKE 739
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1240-1824 |
2.56e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.93 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1240 SSTKQDVEQKKKKVEAQLNDLQLRFSESERQrnELSERVSKMTVELDSVTGLLNEAEGRNIKlskeassISSQLQDAQEL 1319
Cdd:PRK02224 172 SDARLGVERVLSDQRGSLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQ-------ARETRDEADEV 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1320 LS--EETRQKLN-LSGRLRQLEEDKgclmeqleeemeakQAVERQASSLSVQLSDLKKRLEELSAAVELLEEgkkrlqrE 1396
Cdd:PRK02224 243 LEehEERREELEtLEAEIEDLRETI--------------AETEREREELAEEVRDLRERLEELEEERDDLLA-------E 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1397 LEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSAKSAEERDRAEAELRE 1476
Cdd:PRK02224 302 AGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVED 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1477 KETKVLALMKMLEDKQEALQEAERTVKALRVEMEDLISSKDDVGKSVHDLERAKRGLEAFVEEMKTQMEE---------L 1547
Cdd:PRK02224 382 RREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpV 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1548 EDELQV-----AEDAKLRLEVNSQALRAQHErELQAREEQGE-----EKRRQLLKQVRELEAELEEERkqRTLASAARKK 1617
Cdd:PRK02224 462 EGSPHVetieeDRERVEELEAELEDLEEEVE-EVEERLERAEdlveaEDRIERLEERREDLEELIAER--RETIEEKRER 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1618 LEGEVKNTEEqLEAASRGRDEALKQLRKNQGQLKELHRELEEGRAAhkeiLASAREAERRCKNLEAEILQMQEMLAAAER 1697
Cdd:PRK02224 539 AEELRERAAE-LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE----LKERIESLERIRTLLAAIADAEDEIERLRE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1698 ARKQAETERDELSEEVAGgssgrslLSDEKRRLEAKIsqleeeleeEQANVETLNERLRKSQQLVDQLG---AELTAERA 1774
Cdd:PRK02224 614 KREALAELNDERRERLAE-------KRERKRELEAEF---------DEARIEEAREDKERAEEYLEQVEeklDELREERD 677
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1775 SSQNREGSRLQLEKQTRDLKAKLQDVESQarsklkssVAALEAKLREAEE 1824
Cdd:PRK02224 678 DLQAEIGAVENELEELEELRERREALENR--------VEALEALYDEAEE 719
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
905-1253 |
2.90e-14 |
|
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: 78.96 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 905 MRVRLEAKKQELEEVLhemeARLEEEEERSISLQQEKKEMEQELQLMEAHIVQEEDARQKLQLEKAAVEGRVKKLEENLL 984
Cdd:TIGR02169 679 LRERLEGLKRELSSLQ----SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 985 LSEDQNNKL-----QKERKL--LEERLADMSSNLAEE--EEKSKNLSKLKSKH---ESMISELEVRLKKEEKTRQDVEKA 1052
Cdd:TIGR02169 755 NVKSELKELearieELEEDLhkLEEALNDLEARLSHSriPEIQAELSKLEEEVsriEARLREIEQKLNRLTLEKEYLEKE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1053 KRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQAcldeesrqrgaalkRVRDLEALLAELQEDLEAEKVARGK 1132
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA--------------ALRDLESRLGDLKKERDELEAQLRE 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1133 AEAARRDLGEELNSLRSELEDSLDTTAAQQElrvkREQEMAMLKKAMEDEGRSH--ETQIQELRQKHGQAVEELR----- 1205
Cdd:TIGR02169 901 LERKIEELEAQIEKKRKRLSELKAKLEALEE----ELSEIEDPKGEDEEIPEEElsLEDVQAELQRVEEEIRALEpvnml 976
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1206 --EHLEQAKKVRAALEKAKQALEKEAadlsadlRALSSTKQDVEQKKKKV 1253
Cdd:TIGR02169 977 aiQEYEEVLKRLDELKEKRAKLEEER-------KAILERIEEYEKKKREV 1019
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
975-1798 |
3.80e-14 |
|
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: 78.62 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 975 RVKKLEENLllseDQNNKLQKERKL-LEERLADMSSNLAEEEEKSKNLSKLKSKHEsmiselevrlKKEEKTRQDVEKAK 1053
Cdd:pfam15921 86 QVKDLQRRL----NESNELHEKQKFyLRQSVIDLQTKLQEMQMERDAMADIRRRES----------QSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1054 RKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQACLDEESRQRGaalKRVRDLEALLAELQEDLEAekvargKA 1133
Cdd:pfam15921 152 HELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASG---KKIYEHDSMSTMHFRSLGS------AI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1134 EAARRDLGEELNSLRSEL---EDSLDTtaaqqeLRVKREQEMAMLKKamedegrSHETQIQELRQKHGQAVEELREHLEQ 1210
Cdd:pfam15921 223 SKILRELDTEISYLKGRIfpvEDQLEA------LKSESQNKIELLLQ-------QHQDRIEQLISEHEVEITGLTEKASS 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1211 AKKVRAALEKAKQALEKEAADLSA-DLRALSSTKQDVEQkkkkveaqlndLQLRFSESERQRNELSERVSKMTVELDSVt 1289
Cdd:pfam15921 290 ARSQANSIQSQLEIIQEQARNQNSmYMRQLSDLESTVSQ-----------LRSELREAKRMYEDKIEELEKQLVLANSE- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1290 glLNEAEGRNIKLSKEASSISSQLqdaQELLSEETRQKLNLSgrlrqLEEDKGclmeqleeemeaKQAVERQASSlSVQL 1369
Cdd:pfam15921 358 --LTEARTERDQFSQESGNLDDQL---QKLLADLHKREKELS-----LEKEQN------------KRLWDRDTGN-SITI 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1370 SDLKKRLEELSAAVELLE--------EGKKRLQRELEAASGDYE--EKAAAYD-KLEKSRGRLQQELEDVL---MDLDSQ 1435
Cdd:pfam15921 415 DHLRRELDDRNMEVQRLEallkamksECQGQMERQMAAIQGKNEslEKVSSLTaQLESTKEMLRKVVEELTakkMTLESS 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1436 RQLVSNLEKKQKKfdqmlaEERAVSAKSAE---ERDRAEAELREketkvlalMKMLEDKQEALQEAERTVKALRVEMedl 1512
Cdd:pfam15921 495 ERTVSDLTASLQE------KERAIEATNAEitkLRSRVDLKLQE--------LQHLKNEGDHLRNVQTECEALKLQM--- 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1513 iSSKDDVgksvhdLERAKRGLEAFVeEMKTQMEELEDELQVaEDAKLRLEVNSQALRAQherELQAREEQGEEKRRQL-- 1590
Cdd:pfam15921 558 -AEKDKV------IEILRQQIENMT-QLVGQHGRTAGAMQV-EKAQLEKEINDRRLELQ---EFKILKDKKDAKIRELea 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1591 ------LKQVRELEAELEEERKQRTLASaARKKLEGEVKNTEEQLEAASRGRdEALKQLRKNQG------------QLKE 1652
Cdd:pfam15921 626 rvsdleLEKVKLVNAGSERLRAVKDIKQ-ERDQLLNEVKTSRNELNSLSEDY-EVLKRNFRNKSeemetttnklkmQLKS 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1653 LHRELEEGRAAHKEILASAREAERRCknleaeiLQMQEMLAAAERARKQAETERDELSEEVAGGSSGRSLLSDEKRRLEA 1732
Cdd:pfam15921 704 AQSELEQTRNTLKSMEGSDGHAMKVA-------MGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQ 776
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1343958102 1733 KISQLEEELEEEQANVETLNERLRKSQQLVDQLgaELTAERASSQNREGSRLQLEKQTRDLKAKLQ 1798
Cdd:pfam15921 777 ELSTVATEKNKMAGELEVLRSQERRLKEKVANM--EVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
832-1422 |
6.24e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.80 E-value: 6.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 832 RLFTKVKPLLQVTRQEEEMGQKEEELKAVREAAAKAEADLKDITQKHSQLVEEQAMLEAKLQAEAELYAEAEDMRVRLEA 911
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 912 KKQELEEVlhemearleeeEERSISLQQEKKEMEQELQLMEahivQEEDARQKLQLEKAAVEGRVKKLEENLLLSEDQNN 991
Cdd:PRK03918 274 EIEELEEK-----------VKELKELKEKAEEYIKLSEFYE----EYLDELREIEKRLSRLEEEINGIEERIKELEEKEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 992 KLQKERKLLEERLADmssnLAEEEEKSKNLSKLKSKHESMiSELEVRLK-----KEEKTRQDVEKAKRKVEAELVDLQEQ 1066
Cdd:PRK03918 339 RLEELKKKLKELEKR----LEELEERHELYEEAKAKKEEL-ERLKKRLTgltpeKLEKELEELEKAKEEIEEEISKITAR 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1067 QADLQAQLAELRAQLAAKEEELQTTQAC---LDEESRQRgaalkrvrdleaLLAELQEDLEAEKVARGKAEAARRDLGEE 1143
Cdd:PRK03918 414 IGELKKEIKELKKAIEELKKAKGKCPVCgreLTEEHRKE------------LLEEYTAELKRIEKELKEIEEKERKLRKE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1144 LNSLRSELEdsldttaaqQELRVKREQEMAMLKKAMEDEGRSHEtqIQELRQKHgqavEELREHLEQAKKVRAALEKAKQ 1223
Cdd:PRK03918 482 LRELEKVLK---------KESELIKLKELAEQLKELEEKLKKYN--LEELEKKA----EEYEKLKEKLIKLKGEIKSLKK 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1224 ALEKEaADLSADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVELDSVTGLLNEAEGRNIKLS 1303
Cdd:PRK03918 547 ELEKL-EELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLE 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1304 KEASSISSQLQDAQELLsEETRQKLNLSGRLRQLEEDKGclmeqleeemeakqaVERQASSLSVQLSDLKKRLEELSAAV 1383
Cdd:PRK03918 626 EELDKAFEELAETEKRL-EELRKELEELEKKYSEEEYEE---------------LREEYLELSRELAGLRAELEELEKRR 689
|
570 580 590
....*....|....*....|....*....|....*....
gi 1343958102 1384 ELLEEGKKRLQRELEAAsgdyEEKAAAYDKLEKSRGRLQ 1422
Cdd:PRK03918 690 EEIKKTLEKLKEELEER----EKAKKELEKLEKALERVE 724
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1394-1793 |
8.18e-14 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 77.69 E-value: 8.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1394 QRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDvlmdLDSQRQLVSNLEKKQKKFDQM----------LAEERAVSAKS 1463
Cdd:PRK04863 299 RRQLAAEQYRLVEMARELAELNEAESDLEQDYQA----ASDHLNLVQTALRQQEKIERYqadleeleerLEEQNEVVEEA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1464 AEERDRAEAELREKETKVLALMKMLEDKQEALQEAERtvKALRVEmedlisskddvgKSVHDLERAKR----------GL 1533
Cdd:PRK04863 375 DEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQT--RAIQYQ------------QAVQALERAKQlcglpdltadNA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1534 EAFVEEMKTQMEELEDELQVAEDaKLRLevnSQALRAQHERELQAREEQGEEKRRQLLKQVreleaeleeerkqrtlasa 1613
Cdd:PRK04863 441 EDWLEEFQAKEQEATEELLSLEQ-KLSV---AQAAHSQFEQAYQLVRKIAGEVSRSEAWDV------------------- 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1614 ARKKLEgevKNTEEQLEAASrgrdeaLKQLRknqGQLKELHRELEEgraahkeilasAREAERRCKNLEAEILQMQEMLA 1693
Cdd:PRK04863 498 ARELLR---RLREQRHLAEQ------LQQLR---MRLSELEQRLRQ-----------QQRAERLLAEFCKRLGKNLDDED 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1694 AAERARKQAETERDELSEEVAGGSSGRSLLSDEKRRLEAKISQLEEEL---EEEQANVETLNE----RLRKSQQLVDQLG 1766
Cdd:PRK04863 555 ELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARApawLAAQDALARLREqsgeEFEDSQDVTEYMQ 634
|
410 420 430
....*....|....*....|....*....|
gi 1343958102 1767 AELTAERASSQNREGS---RLQLEKQTRDL 1793
Cdd:PRK04863 635 QLLERERELTVERDELaarKQALDEEIERL 664
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1046-1775 |
1.33e-13 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 76.92 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1046 RQDVEKAKRKVEAE---LVDLQEQQADLQAQLAELRAQLAAKEEELQTTQACLdeesRQRGAALKRVRDLEALLAELQED 1122
Cdd:PRK04863 292 RRELYTSRRQLAAEqyrLVEMARELAELNEAESDLEQDYQAASDHLNLVQTAL----RQQEKIERYQADLEELEERLEEQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1123 LEAEKVARGKAEAARRDLG---EELNSLRSELEDSLDTTAAQQELRVKREQEMAMLKKAMEDEGRSH------ETQIQEL 1193
Cdd:PRK04863 368 NEVVEEADEQQEENEARAEaaeEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQLCGLPDltadnaEDWLEEF 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1194 RQKHGQAVEELReHLEQ----AKKVRAALEKAKQALEKEAADLSAD---------LRALSSTKQDVEQKKKkVEAQLNDL 1260
Cdd:PRK04863 448 QAKEQEATEELL-SLEQklsvAQAAHSQFEQAYQLVRKIAGEVSRSeawdvarelLRRLREQRHLAEQLQQ-LRMRLSEL 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1261 QLRFSE---SERQRNELSERVSKMTVELDSVTGLLNEAEGRNIKLSKEASSI---SSQLQDAQELLSEETRQK------- 1327
Cdd:PRK04863 526 EQRLRQqqrAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEArerRMALRQQLEQLQARIQRLaarapaw 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1328 LNLSGRLRQLEEdkgclmeqleeemeakQAVERQASSLSV--QLSDLKKRLEELSAAVELLEEGKKRLQRELEAASG--- 1402
Cdd:PRK04863 606 LAAQDALARLRE----------------QSGEEFEDSQDVteYMQQLLERERELTVERDELAARKQALDEEIERLSQpgg 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1403 ----------------------------DYEEKAAAY---------DKLEKSRGRLQQE---LEDVLM---DLDSQRQLV 1439
Cdd:PRK04863 670 sedprlnalaerfggvllseiyddvsleDAPYFSALYgparhaivvPDLSDAAEQLAGLedcPEDLYLiegDPDSFDDSV 749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1440 SNLEKKQKKFDQMLAE---------ERAVSAKSAEERdRAEAELREKETKVLALMKMLEDkqeaLQEAERTVKALR---- 1506
Cdd:PRK04863 750 FSVEELEKAVVVKIADrqwrysrfpEVPLFGRAAREK-RIEQLRAEREELAERYATLSFD----VQKLQRLHQAFSrfig 824
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1507 ------------VEMEDLISSKDDVGKSVHDLE-----------RAKRGLEA-----------FVEEMKTQMEELEDELQ 1552
Cdd:PRK04863 825 shlavafeadpeAELRQLNRRRVELERALADHEsqeqqqrsqleQAKEGLSAlnrllprlnllADETLADRVEEIREQLD 904
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1553 VAEDAKL----------RLEVNSQALRA---QHEReLQAREEQGEEKRRQLLKQVRELEAELEeeRKQRTLASAARKKLE 1619
Cdd:PRK04863 905 EAEEAKRfvqqhgnalaQLEPIVSVLQSdpeQFEQ-LKQDYQQAQQTQRDAKQQAFALTEVVQ--RRAHFSYEDAAEMLA 981
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1620 GEVKNTE---EQLEAASRGRDEALKQLRKNQGQLKElhreleegraaHKEILASAREAERRCKNLEAEILQ-MQEM-LAA 1694
Cdd:PRK04863 982 KNSDLNEklrQRLEQAEQERTRAREQLRQAQAQLAQ-----------YNQVLASLKSSYDAKRQMLQELKQeLQDLgVPA 1050
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1695 AERARKQAETERDELSEEVaggssgrsllsdekRRLEAKISQLEEELEEEQANVETLNERLRKSQQLVDQLGAELTAERA 1774
Cdd:PRK04863 1051 DSGAEERARARRDELHARL--------------SANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKA 1116
|
.
gi 1343958102 1775 S 1775
Cdd:PRK04863 1117 G 1117
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
940-1503 |
1.54e-13 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 76.30 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 940 EKKEMEQELQLMEAHIVQEEDARQKLQLE---KAAVEGRVKKLEENLLLSEDQNNKLQKERKLLEERlADMSSNLAEEEE 1016
Cdd:pfam05483 200 EELRVQAENARLEMHFKLKEDHEKIQHLEeeyKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEES-RDKANQLEEKTK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1017 -KSKNLSKLKSKHESMISELE---VRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQ 1092
Cdd:pfam05483 279 lQDENLKELIEKKDHLTKELEdikMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATT 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1093 ACLDEESRQRGAALKRVRD-LEALLAELQE---DLEAEKVARGKAEAARRDLGEELNSLRSELEDSLDTTAAQQELRVKr 1168
Cdd:pfam05483 359 CSLEELLRTEQQRLEKNEDqLKIITMELQKkssELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGK- 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1169 EQEMAMLKKAMEDEGRSHETQIQELR---QKHGQAVEELREHLEQAKKVRAALEK-------AKQALEKEAADLSADLRa 1238
Cdd:pfam05483 438 EQELIFLLQAREKEIHDLEIQLTAIKtseEHYLKEVEDLKTELEKEKLKNIELTAhcdklllENKELTQEASDMTLELK- 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1239 lsSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQE 1318
Cdd:pfam05483 517 --KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILEN 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1319 LLSEETRQKLNLSGRLRQLEEDKGCLMEQLEEEMEAKQAVERQASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELe 1398
Cdd:pfam05483 595 KCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKL- 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1399 aaSGDYEEKAAAYDKLEKsrgrLQQELedvlmDLDSQR---QLVSNLEKKQKKFDQMLAEE-------RAVSAKSAEERD 1468
Cdd:pfam05483 674 --LEEVEKAKAIADEAVK----LQKEI-----DKRCQHkiaEMVALMEKHKHQYDKIIEERdselglyKNKEQEQSSAKA 742
|
570 580 590
....*....|....*....|....*....|....*
gi 1343958102 1469 RAEAELREKETKVLALMKMLEDKQEALQEAERTVK 1503
Cdd:pfam05483 743 ALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1456-1926 |
1.70e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 76.23 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1456 ERAVSAKSAEER---------DRAEAELREKETKVL--------ALMKMLEDKQEALQEAERTVKALRVEMEDLISSKDD 1518
Cdd:PRK02224 169 ERASDARLGVERvlsdqrgslDQLKAQIEEKEEKDLherlngleSELAELDEEIERYEEQREQARETRDEADEVLEEHEE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1519 VGKSVHDLERAKRGLEAFVEEMKTQMEELEDELQVAEDAKLRLEVNSQALRAQHERE------LQAREEQGEEKRRQLLK 1592
Cdd:PRK02224 249 RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDdadaeaVEARREELEDRDEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1593 QVRELEAELEEERKQRTLASAARKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQGQLKELHRELEEGRAA--------- 1663
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdlg 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1664 ----HKEILASAREAER-RCKNLEAEILQMQEMLAAAER---ARKQAETERD-----------ELSEEVAGGSSGRSLLS 1724
Cdd:PRK02224 409 naedFLEELREERDELReREAELEATLRTARERVEEAEAlleAGKCPECGQPvegsphvetieEDRERVEELEAELEDLE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1725 DEKRRLEAKISQLEEELEEeQANVETLNERLRKSQQLVDQ--LGAELTAERASSQNREGSRLQLEKQTRDLKAklQDVES 1802
Cdd:PRK02224 489 EEVEEVEERLERAEDLVEA-EDRIERLEERREDLEELIAErrETIEEKRERAEELRERAAELEAEAEEKREAA--AEAEE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1803 QARSKLkSSVAALEAKLREAEEQLEV--ESRERQASAKNLRQK----EKKLKDLtAQMEDERKqaqdykDQMEKSSARMK 1876
Cdd:PRK02224 566 EAEEAR-EEVAELNSKLAELKERIESleRIRTLLAAIADAEDEierlREKREAL-AELNDERR------ERLAEKRERKR 637
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1343958102 1877 QLKHQ-----LEEAEEEAQRVAAARRKLQRELDEALEANDALSREVSSLRSKLRR 1926
Cdd:PRK02224 638 ELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
997-1645 |
1.73e-13 |
|
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: 76.42 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 997 RKLLEERLADMSSNLAEEEEKSKNLSKLKSKHESMISELEVR-----LKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQ 1071
Cdd:pfam12128 199 KSMIVAILEDDGVVPPKSRLNRQQVEHWIRDIQAIAGIMKIRpeftkLQQEFNTLESAELRLSHLHFGYKSDETLIASRQ 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1072 ----AQLAELRAQLAAKEEELQTTQACLDEE-SRQRGAALKRVRDLEAL----LAELQEDLEAEKVARGKAEAARRDLGE 1142
Cdd:pfam12128 279 eerqETSAELNQLLRTLDDQWKEKRDELNGElSAADAAVAKDRSELEALedqhGAFLDADIETAAADQEQLPSWQSELEN 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1143 ELNSLRSELEDSLDTTAAQQELRVKREQEMAM--------LKKAMEDEGRSH-------ETQIQELRQKHGQAVEELReh 1207
Cdd:pfam12128 359 LEERLKALTGKHQDVTAKYNRRRSKIKEQNNRdiagikdkLAKIREARDRQLavaeddlQALESELREQLEAGKLEFN-- 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1208 lEQAKKVRAALEKAK------QALEKEAADLSADLRALSSTKQDVEQKKKKVE-AQLNDLQLR--FSESERQRNELSERV 1278
Cdd:pfam12128 437 -EEEYRLKSRLGELKlrlnqaTATPELLLQLENFDERIERAREEQEAANAEVErLQSELRQARkrRDQASEALRQASRRL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1279 SKMTVELDSVTGLLNEAEGRNIK-LSKEAS----SISSQLQDAQ--------ELLSEETRQKLNLSG---RLRQLEEDKG 1342
Cdd:pfam12128 516 EERQSALDELELQLFPQAGTLLHfLRKEAPdweqSIGKVISPELlhrtdldpEVWDGSVGGELNLYGvklDLKRIDVPEW 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1343 CLMEQLEEEMEAK-----QAVERQASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGdyeEKAAAYDKLEKS 1417
Cdd:pfam12128 596 AASEEELRERLDKaeealQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFD---EKQSEKDKKNKA 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1418 RGRLQQELEDVLMDLDSQRQLvsnLEKKQKkfdQMLAEERAVSAKSAEERDRAEAELREKETKVLALMKMLEDKQEALQE 1497
Cdd:pfam12128 673 LAERKDSANERLNSLEAQLKQ---LDKKHQ---AWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAK 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1498 AErtVKALRVEMEDLISSKDDVGKSVHDLERAKRGLEAFVEE-------------------------MKTQMEELEDELQ 1552
Cdd:pfam12128 747 AE--LKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERiavrrqevlryfdwyqetwlqrrprLATQLSNIERAIS 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1553 VAEDAKLRLEVNSQALRAQHERELQAREEQgEEKRRQLLKQVRELEAELEEERKQRTLASAarkklEGEVKNTEEQLEAA 1632
Cdd:pfam12128 825 ELQQQLARLIADTKLRRAKLEMERKASEKQ-QVRLSENLRGLRCEMSKLATLKEDANSEQA-----QGSIGERLAQLEDL 898
|
730
....*....|...
gi 1343958102 1633 SRGRDEALKQLRK 1645
Cdd:pfam12128 899 KLKRDYLSESVKK 911
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
866-1689 |
1.80e-13 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 76.24 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 866 KAEADLKDITQKHSQLVEEQAMLEAKLQAEAELYAEAEDMRVRLEAKKQELEEVLHEMEARLEEEEERSISLQQEKK--- 942
Cdd:TIGR00606 186 KALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSkim 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 943 EMEQELQLMEAHIVQEEDARQKLQLEKAAV---------------EGRVKKLEENLLLSEDQNNKLQKERKLLEERLADM 1007
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKVfqgtdeqlndlyhnhQRTVREKERELVDCQRELEKLNKERRLLNQEKTEL 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1008 SSNLAEEEEKSKNLSKLKSKHESMISELEVRLKKE----------------EKTRQDVEKAKRKVEAELVDLQEQQADLQ 1071
Cdd:TIGR00606 346 LVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDgfergpfserqiknfhTLVIERQEDEAKTAAQLCADLQSKERLKQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1072 AQLAELRAQLAAKEEELQTTQACLDEESRQRGAALKRVRDLEA---LLAELQEDLEAEKVARGKAE--AARRDLGEELNS 1146
Cdd:TIGR00606 426 EQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGssdRILELDQELRKAERELSKAEknSLTETLKKEVKS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1147 LRSELEDSLDTTAAQQELRVKREQEMAMLKKaMEDEGRSHETQIQELRQKHGQAVEELREHL------EQAKKVRAALEK 1220
Cdd:TIGR00606 506 LQNEKADLDRKLRKLDQEMEQLNHHTTTRTQ-MEMLTKDKMDKDEQIRKIKSRHSDELTSLLgyfpnkKQLEDWLHSKSK 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1221 AKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQL-----------------NDLQLRFSESERQRNELSERVSKMTV 1283
Cdd:TIGR00606 585 EINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLssyedklfdvcgsqdeeSDLERLKEEIEKSSKQRAMLAGATAV 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1284 ELDSVTGLLNEAEG------RNIKLSKEASSISSQLQ-----------DAQELLSEETRQKLNLSGRLRQLEEDKGCLME 1346
Cdd:TIGR00606 665 YSQFITQLTDENQSccpvcqRVFQTEAELQEFISDLQsklrlapdklkSTESELKKKEKRRDEMLGLAPGRQSIIDLKEK 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1347 QLEEEMEAKQAVERQASSLSVQLSDLKKRLEELSAAVELLEEGK------KRLQRELEAASGDYEEKAA---------AY 1411
Cdd:TIGR00606 745 EIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLtdvtimERFQMELKDVERKIAQQAAklqgsdldrTV 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1412 DKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAE---ERAVSAKSAEERDRAEAELREKETKVLALMKML 1488
Cdd:TIGR00606 825 QQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNElksEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREI 904
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1489 EDKQEALQEAERTVKALRVEMEDLISSKDDVGKSVHD-LERAKRGLEAFVEEMKTQMEELEDElqvAEDAKLRLEVNSQA 1567
Cdd:TIGR00606 905 KDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDkVNDIKEKVKNIHGYMKDIENKIQDG---KDDYLKQKETELNT 981
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1568 LRAQHErELQAREEQGEEKRRQLLKQVRELEAELEEERKQRTlasaaRKKLEGEVKNTEEQLEaasrgrdEALKQLRKNQ 1647
Cdd:TIGR00606 982 VNAQLE-ECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLT-----LRKRENELKEVEEELK-------QHLKEMGQMQ 1048
|
890 900 910 920
....*....|....*....|....*....|....*....|....*..
gi 1343958102 1648 -GQLKELHRELEEG----RAAHKEILASAREAERRCKNLEAEILQMQ 1689
Cdd:TIGR00606 1049 vLQMKQEHQKLEENidliKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1007-1235 |
9.96e-13 |
|
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: 72.10 E-value: 9.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1007 MSSNLAEEEEKSKNLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEE 1086
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1087 ELQTTQACLDEESRQRGAALKRV-----RDLEALLAELQEDLEAEKVAR--GKAEAARRDLGEELNSLRSELEDSLDTTA 1159
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALyrlgrQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1343958102 1160 AQQELRVKREQEMAMLKKAMEDEGRSHETQIQELRQKHGQAVEELREHLEQAKKVRAALEKAKQALEKEAADLSAD 1235
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1107-1909 |
1.69e-12 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 73.07 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1107 KRVRDLEALLAELQEDLEAEKVARG---------------------KAEAARRDLGEELNSLRSELEDSLDTTAAQQELR 1165
Cdd:PRK04863 230 KAFQDMEAALRENRMTLEAIRVTQSdrdlfkhlitestnyvaadymRHANERRVHLEEALELRRELYTSRRQLAAEQYRL 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1166 VKREQEMAMLKkamedEGRSH-ETQIQELRQkHGQAVEELREHLEQAKKVRAALEKAKQALE------KEAADLSADLRA 1238
Cdd:PRK04863 310 VEMARELAELN-----EAESDlEQDYQAASD-HLNLVQTALRQQEKIERYQADLEELEERLEeqnevvEEADEQQEENEA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1239 -LSSTKQDVEQKKKkveaQLNDLQLRFSESE------RQRNELSERV----SKMTVELDSVTGLLNEAEGRNIKLSKEAS 1307
Cdd:PRK04863 384 rAEAAEEEVDELKS----QLADYQQALDVQQtraiqyQQAVQALERAkqlcGLPDLTADNAEDWLEEFQAKEQEATEELL 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1308 SISSQLQDAQELLSEETrQKLNLSGR-----------------LRQLEEDKgclmeqleeemeakqAVERQASSLSVQLS 1370
Cdd:PRK04863 460 SLEQKLSVAQAAHSQFE-QAYQLVRKiagevsrseawdvarelLRRLREQR---------------HLAEQLQQLRMRLS 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1371 DLKKRLEELSAAVELLEEGKKRLQRELEAAsgdyeekaaayDKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKKFD 1450
Cdd:PRK04863 524 ELEQRLRQQQRAERLLAEFCKRLGKNLDDE-----------DELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQ 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1451 QMLAEERAVS-----AKSAEERDRAE-AELREKETKVLALMKMLEDKQEALQEAERTVKALRVEMEDLISS--------- 1515
Cdd:PRK04863 593 ARIQRLAARApawlaAQDALARLREQsGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERlsqpggsed 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1516 ------KDDVGKS-----------------------------VHDLERAKRGLEAfVEEMKTQMEELEDELQVAEDAKLR 1560
Cdd:PRK04863 673 prlnalAERFGGVllseiyddvsledapyfsalygparhaivVPDLSDAAEQLAG-LEDCPEDLYLIEGDPDSFDDSVFS 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1561 LEVNSQALrAQHERELQAREEQ-------GEEKRRQLLKQVRELEAEleeerKQRTLASAARkklegEVKNTEEQLEAAS 1633
Cdd:PRK04863 752 VEELEKAV-VVKIADRQWRYSRfpevplfGRAAREKRIEQLRAEREE-----LAERYATLSF-----DVQKLQRLHQAFS 820
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1634 R-----------GRDEAlkQLRKNQGQLKELHRELEEGRAAHKEILASAREAERRCKNLEAeiLQMQEMLAAAERARKQA 1702
Cdd:PRK04863 821 RfigshlavafeADPEA--ELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNR--LLPRLNLLADETLADRV 896
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1703 ETERDELSE-EVAG---GSSGRSLLSDEKrrLEAKISQLEEELEEEQANVETLNERLRKSQQLVDQLgAELTAERA---- 1774
Cdd:PRK04863 897 EEIREQLDEaEEAKrfvQQHGNALAQLEP--IVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFAL-TEVVQRRAhfsy 973
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1775 -SSQNREGSRLQLEKQtrdLKAKLQDVEsQARSKLKSSVAALEAKLREAEEQLEVESRERQASAKNLRQKEKKLKDLTAQ 1853
Cdd:PRK04863 974 eDAAEMLAKNSDLNEK---LRQRLEQAE-QERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVP 1049
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1343958102 1854 M-EDERKQAQDYKDQMEK----SSARMKQLKHQLEEAEEEAQRVAAARRKLQRELDEALEA 1909
Cdd:PRK04863 1050 AdSGAEERARARRDELHArlsaNRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQ 1110
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
912-1296 |
1.76e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 73.18 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 912 KKQELEEVLHEMEARLEEEEERSiSLQQEKKEMEQELQLMEAHIVQEEDARQKLQLEKAAVEGRVKKLEENLLLSEDQNN 991
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELS-SLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 992 KLQKERKLLEERLADMSSNLAEEEEKsknlsklKSKHESMISELEVRLKKEEKtrQDVEKAKRKVEAELVDLQEQQADLQ 1071
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEED-------LHKLEEALNDLEARLSHSRI--PEIQAELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1072 AQLAELRAQLAAKEEELQTTQACLDEESRQRGAALKRVRDLEALLAELQEDLEaekvargKAEAARRDLGEELNSLRSEL 1151
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE-------ELEAALRDLESRLGDLKKER 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1152 EDsldttaaqqelrvkreqemamlkkaMEDEGRSHETQIQELRQKhgqaVEELREHLEQAKKVRAALEKAKQALEKEAAD 1231
Cdd:TIGR02169 892 DE-------------------------LEAQLRELERKIEELEAQ----IEKKRKRLSELKAKLEALEEELSEIEDPKGE 942
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1343958102 1232 LSADLRALSSTkQDVEQKKKKVEAQLNDLQ-------LRFSESERQRNELSERVSKMTVELDSVTGLLNEAE 1296
Cdd:TIGR02169 943 DEEIPEEELSL-EDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1481-1926 |
2.06e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 72.64 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1481 VLALMKMLEDKQEALQEAERTVKALRvEMEDLISSKDDVGKSVHDLERAKRGLEAF-----VEEMKTQMEELEDELQVAE 1555
Cdd:COG4913 230 LVEHFDDLERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWfaqrrLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1556 DAKLRLEVNSQALRAQHERELQAREEQGEEKRRQLLKQVRELEAELEEERKQRTLASAARKKLEGEVKNTEEQLEAASRG 1635
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1636 RDEALKQLRKNQGQLK----ELHRELEEGRAAHKEILASAREAERRCKNLEAEILQMQEMLAAAERARK----------- 1700
Cdd:COG4913 389 AAALLEALEEELEALEealaEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEaelpfvgelie 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1701 -QAETERDELSEEVAGGSSGRSLLSDEKRRLEA----------------KISQLEEELEEEQANVETL------------ 1751
Cdd:COG4913 469 vRPEEERWRGAIERVLGGFALTLLVPPEHYAAAlrwvnrlhlrgrlvyeRVRTGLPDPERPRLDPDSLagkldfkphpfr 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1752 ---NERLRKSQQLV-----DQLGAE---LTAERASSQNREGSRLQLEKQTR-------DLKAKLQDVESQARsKLKSSVA 1813
Cdd:COG4913 549 awlEAELGRRFDYVcvdspEELRRHpraITRAGQVKGNGTRHEKDDRRRIRsryvlgfDNRAKLAALEAELA-ELEEELA 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1814 ALEAKLREAEEQLEvESRERQASAKNLRQKEKKLKDLtAQMEDERKQAQDYKDQMEKSSARMKQLKHQLeeaeeeaqrva 1893
Cdd:COG4913 628 EAEERLEALEAELD-ALQERREALQRLAEYSWDEIDV-ASAEREIAELEAELERLDASSDDLAALEEQL----------- 694
|
490 500 510
....*....|....*....|....*....|...
gi 1343958102 1894 aarRKLQRELDEALEANDALSREVSSLRSKLRR 1926
Cdd:COG4913 695 ---EELEAELEELEEELDELKGEIGRLEKELEQ 724
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1064-1285 |
2.48e-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: 70.95 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1064 QEQQADLQAQLAELRAQLAAKEEELQTTQACLDEESRQRGAALKRVRDLEALLAELQEDLEAEKVARGKAEAARRDLGEE 1143
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1144 LNSLRSELEDSLdttAAQQELRVKREQEMAMLKKAMEDEGRShETQIQELRQKHGQAVEELREHLEQAKKVRAALEKAKQ 1223
Cdd:COG4942 99 LEAQKEELAELL---RALYRLGRQPPLALLLSPEDFLDAVRR-LQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1343958102 1224 ALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVEL 1285
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
995-1766 |
2.83e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 72.31 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 995 KERKLLEERLADMSSNLAEEEEKSKNLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQL 1074
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1075 AELRAQLAAKEEELQTTQACldeesRQRGAALKRVRDLEALLAELQEDLE-AEKVARGKAEAARRdlgEELNSLRSELED 1153
Cdd:TIGR00618 243 AYLTQKREAQEEQLKKQQLL-----KQLRARIEELRAQEAVLEETQERINrARKAAPLAAHIKAV---TQIEQQAQRIHT 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1154 SLdttaaqQELRVKREQEMAMLKKAMEDegRSHETQIQELRQKHGQAVEELREHLEQAKKVRAALEKAK---QALEKEAA 1230
Cdd:TIGR00618 315 EL------QSKMRSRAKLLMKRAAHVKQ--QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHtltQHIHTLQQ 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1231 DLSADLRALSSTKQDVEQKKKKVEAQLNDLQlrfseseRQRNELSERVSKMTVEldsvtgllnEAEGRNIKLSKEASSIS 1310
Cdd:TIGR00618 387 QKTTLTQKLQSLCKELDILQREQATIDTRTS-------AFRDLQGQLAHAKKQQ---------ELQQRYAELCAAAITCT 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1311 SQLQDAQELLSEETRQklnlsgRLRQLEEDKGCLMEQLEEEMEAKQAVERQASSLSVQLSDLKKRLEELSAAVELLEEgK 1390
Cdd:TIGR00618 451 AQCEKLEKIHLQESAQ------SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDN-P 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1391 KRLQRELEAasgdyeekaaaydkLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLaeeravsAKSAEERDRA 1470
Cdd:TIGR00618 524 GPLTRRMQR--------------GEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSF-------SILTQCDNRS 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1471 EAELrekeTKVLALMKMLEDKQEALQEAERTVK-ALRVEMEDLISSKDDVGKSVHD------LERAKRGLEAFVEEMkTQ 1543
Cdd:TIGR00618 583 KEDI----PNLQNITVRLQDLTEKLSEAEDMLAcEQHALLRKLQPEQDLQDVRLHLqqcsqeLALKLTALHALQLTL-TQ 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1544 MEELEDELQVAEDAKLRLEVNSQALR-AQHERELQAREEQGEEKRRQLLKQVRELEAELEEERKQRTLASAARK-KLEGE 1621
Cdd:TIGR00618 658 ERVREHALSIRVLPKELLASRQLALQkMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGsDLAAR 737
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1622 VKNTEEQLEAASRGRDEALK-----QLRKNQGQLKELHRELEEGRAahkeilasAREAERRCKNLEAEILQMQEMLAAAE 1696
Cdd:TIGR00618 738 EDALNQSLKELMHQARTVLKarteaHFNNNEEVTAALQTGAELSHL--------AAEIQFFNRLREEDTHLLKTLEAEIG 809
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1697 RARKQAETERDELSEEVAGGSSGRSLLSDEKRRLEAKISQLEEELEEEQANVETLNERLRKSQQLVDQLG 1766
Cdd:TIGR00618 810 QEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1038-1270 |
1.12e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.02 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1038 RLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQAcldeesrQRGAALKRVRDLEALLA 1117
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ-------ELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1118 ELQEDLEAEKvargkAEAARRDLGEELNSLRSELEDSLDTTAAQQELR-VKREQEMAMLKKAMEDEGRSHETQIQELRQK 1196
Cdd:COG4942 94 ELRAELEAQK-----EELAELLRALYRLGRQPPLALLLSPEDFLDAVRrLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1343958102 1197 HGQAVEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQ 1270
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
878-1593 |
1.38e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 70.00 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 878 HSQLVEEQAMLEAKLQAEAELYAEAEDMRVRLEAKKQELEEVlhemearleeeeersisLQQEKKEMEQELQLMEAhivq 957
Cdd:TIGR00618 193 HGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREA-----------------LQQTQQSHAYLTQKREA---- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 958 eEDARQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLleERLAdmssnlaeeeEKSKNLSKLKSKHESMISELEV 1037
Cdd:TIGR00618 252 -QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKA--APLA----------AHIKAVTQIEQQAQRIHTELQS 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1038 RLKKEEKTRQDvekaKRKVEAELVDLQEQQADLQA-QLAELRAQLAAKEEELQTTQACLDEESRQRGAALKRVR----DL 1112
Cdd:TIGR00618 319 KMRSRAKLLMK----RAAHVKQQSSIEEQRRLLQTlHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKttltQK 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1113 EALLAELQEDLEAEKVARGKAEAARRDLGEELNSLRSELEDSLDTTAAQQELRVKREQEMAMLKKAMEDEGRSHETQIQE 1192
Cdd:TIGR00618 395 LQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1193 LRQKhgqavEELREHLEQAKKVRAALEKAKQALEKE----------AADLSADLRALSSTKQDVEQKKKKVEAQLNDLQL 1262
Cdd:TIGR00618 475 LQTK-----EQIHLQETRKKAVVLARLLELQEEPCPlcgscihpnpARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYH 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1263 RFSESERQRNELSERVSKMTVELDSVTGLLNEaegrnikLSKEASSISSQLQDAQELLSEETRQKLNLSGRLRQLEEDKG 1342
Cdd:TIGR00618 550 QLTSERKQRASLKEQMQEIQQSFSILTQCDNR-------SKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQ 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1343 CLMEQLEEEMEAKQAVERQASSLS----VQLSDLKKRLEELSAAVELLEEGK-KRLQRELEAASGDYEEKAAAYDKLEKS 1417
Cdd:TIGR00618 623 PEQDLQDVRLHLQQCSQELALKLTalhaLQLTLTQERVREHALSIRVLPKELlASRQLALQKMQSEKEQLTYWKEMLAQC 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1418 RGRLqQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSAKSAEERDRAEAELREKETKVLAL-MKMLEDKQEALQ 1496
Cdd:TIGR00618 703 QTLL-RELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEeVTAALQTGAELS 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1497 EAERTVKALRVEMEDLISSKDDVgKSVHDLERAKRGLEAFVEEMKTQMEELEDELQVAEDAKLRLEVNSQALRAQHEREL 1576
Cdd:TIGR00618 782 HLAAEIQFFNRLREEDTHLLKTL-EAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQ 860
|
730
....*....|....*..
gi 1343958102 1577 QAREEQGEEKRRQLLKQ 1593
Cdd:TIGR00618 861 LAQLTQEQAKIIQLSDK 877
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
861-1695 |
2.57e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 69.21 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 861 REAAAKAEADLkdiTQKHSQLVEEQAMLEAKLQAEAELYAEAEDMRVRLEAKKQELEEVLHEMEarleeeeersislQQE 940
Cdd:COG3096 284 SERALELRREL---FGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALR-------------QQE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 941 KKEMEQE------LQLMEAHIVQEE--DARQKLQLEKAAVEGRVKKLEENLL-----LSEDQN---------NKLQKERK 998
Cdd:COG3096 348 KIERYQEdleeltERLEEQEEVVEEaaEQLAEAEARLEAAEEEVDSLKSQLAdyqqaLDVQQTraiqyqqavQALEKARA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 999 LLEerLADMS-SNLAEEEEKSKnlSKLKSKHESMIsELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQ--LA 1075
Cdd:COG3096 428 LCG--LPDLTpENAEDYLAAFR--AKEQQATEEVL-ELEQKLSVADAARRQFEKAYELVCKIAGEVERSQAWQTARelLR 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1076 ELRAQ--LAAKEEELQTTQAcldeESRQRgaaLKRVRDLEALLAELQedleaekVARGKAEAARRDLGEELNSLRSELED 1153
Cdd:COG3096 503 RYRSQqaLAQRLQQLRAQLA----ELEQR---LRQQQNAERLLEEFC-------QRIGQQLDAAEELEELLAELEAQLEE 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1154 SLDTTAAQQELRVKREQEMAMLKkamedegrsheTQIQELRQKH------GQAVEELREHLEQAKKVRAALEKAKQ-ALE 1226
Cdd:COG3096 569 LEEQAAEAVEQRSELRQQLEQLR-----------ARIKELAARApawlaaQDALERLREQSGEALADSQEVTAAMQqLLE 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1227 KEaadlsadlRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVEL--DSVTglLNEA--------E 1296
Cdd:COG3096 638 RE--------REATVERDELAARKQALESQIERLSQPGGAEDPRLLALAERLGGVLLSEiyDDVT--LEDApyfsalygP 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1297 GRNIKLSKEASSISSQLQDAQELLS-----EETRQKLNLSGRLRQLEEDKGCLMEQLEEEMEAK---------QAVERQA 1362
Cdd:COG3096 708 ARHAIVVPDLSAVKEQLAGLEDCPEdlyliEGDPDSFDDSVFDAEELEDAVVVKLSDRQWRYSRfpevplfgrAAREKRL 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1363 SSLSVQLSDLKKRLEELSAAVELLEegkkRLQRELEAASGDY------EEKAAAYDKLEKSRGRLQQELEDVLMDLDSQR 1436
Cdd:COG3096 788 EELRAERDELAEQYAKASFDVQKLQ----RLHQAFSQFVGGHlavafaPDPEAELAALRQRRSELERELAQHRAQEQQLR 863
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1437 QLVSNLEKKQKKFDQMLAEERAVSAKSAEERDRaeaELREKETKVLALMKMLEDKQEALQEAERTVKALRVEMEDLISSK 1516
Cdd:COG3096 864 QQLDQLKEQLQLLNKLLPQANLLADETLADRLE---ELREELDAAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQ 940
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1517 DDVGKSVHDLERAKRGLEA--FVEEMKTQMEELEDELQVAEDAKLrlevnSQALRAQHERELQAREEQGeEKRRQLLKQV 1594
Cdd:COG3096 941 ADYLQAKEQQRRLKQQIFAlsEVVQRRPHFSYEDAVGLLGENSDL-----NEKLRARLEQAEEARREAR-EQLRQAQAQY 1014
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1595 RELEAELEEER-----KQRTLASAARKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQGQLKELHRELEEGRAAhkeila 1669
Cdd:COG3096 1015 SQYNQVLASLKssrdaKQQTLQELEQELEELGVQADAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAE------ 1088
|
890 900
....*....|....*....|....*.
gi 1343958102 1670 sAREAERRCKNLEAEILQMQEMLAAA 1695
Cdd:COG3096 1089 -MDSLQKRLRKAERDYKQEREQVVQA 1113
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1373-1926 |
3.35e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.55 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1373 KKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDvlmdLDSQRQLVSNLEKKQKKFDQM 1452
Cdd:PRK03918 178 IERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE----LEELKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1453 LAEERAVSAKSAEERDRAEAELREKETKVLALmkmledkqEALQEAERTVKALRVEMEDLISSKDDVGKSVHDLERAKRG 1532
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKEL--------KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1533 LEAFV---EEMKTQMEELEDELQVAEDAKLRLEVNSQALraQHERELQAREEQGEEKRRQLLKQvreleaeleEERKQRT 1609
Cdd:PRK03918 326 IEERIkelEEKEERLEELKKKLKELEKRLEELEERHELY--EEAKAKKEELERLKKRLTGLTPE---------KLEKELE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1610 LASAARKKLEGEVKNTEE---QLEAASRGRDEALKQLRKNQGQLKELHRELEEgraAHKEILASAREAErrCKNLEAEIL 1686
Cdd:PRK03918 395 ELEKAKEEIEEEISKITArigELKKEIKELKKAIEELKKAKGKCPVCGRELTE---EHRKELLEEYTAE--LKRIEKELK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1687 QMQEMLAAAERARKQAETERDELSEEVAGGSsgrslLSDEKRRLEAKISQLEEELEEEQAN-VETLNERLRKSQQLVDQL 1765
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESELIKLKE-----LAEQLKELEEKLKKYNLEELEKKAEeYEKLKEKLIKLKGEIKSL 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1766 GAELTAERAssqnREGSRLQLEKQTRDLKAKLQDVESQARSKLKSSVAALEAKLREAEEQLEvESRERQASAKNLRQKEK 1845
Cdd:PRK03918 545 KKELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYN-EYLELKDAEKELEREEK 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1846 KLKDLTAQMEDERKQAQDYKDQMEKSSARMKQLKHQLEEAEEEAQRVAAAR------------RKLQRELDEALEANDAL 1913
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLElsrelaglraelEELEKRREEIKKTLEKL 699
|
570
....*....|...
gi 1343958102 1914 SREVSSLRSKLRR 1926
Cdd:PRK03918 700 KEELEEREKAKKE 712
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
846-1592 |
4.67e-11 |
|
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: 68.46 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 846 QEEEMGQKEEELKAVREAAAKAEADLKDITQKHSQLVEEQAMLEAKLQAEAELYAEAEDMRVRLEAKKQELEEvlhemea 925
Cdd:pfam02463 284 QEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEE------- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 926 rleeeEERSISLQQEKKEmeqelqlmeahiVQEEDARQKLQLEKAAVEGRVKKLEENLllsEDQNNKLQKERKLLEERLA 1005
Cdd:pfam02463 357 -----EEEELEKLQEKLE------------QLEEELLAKKKLESERLSSAAKLKEEEL---ELKSEEEKEAQLLLELARQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1006 DMSSNLAEEEEKSKNLSKLKSKHEsmISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKE 1085
Cdd:pfam02463 417 LEDLLKEEKKEELEILEEEEESIE--LKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQK 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1086 EELQTTQACLDEE------SRQRGAALKRVRDLEALLAELQEDLEAEKVARGKA-----EAARRDLGEELNSLRSELEDS 1154
Cdd:pfam02463 495 LEERSQKESKARSglkvllALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAvivevSATADEVEERQKLVRALTELP 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1155 LDTTAAQQELRVKREQEMAMLKKAMEDEGRSHETQIQELRQKHGQAVEELREHLEQAKKVRAALEKAKQALEKEAADLSA 1234
Cdd:pfam02463 575 LGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSL 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1235 DLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVELDSVTGLLN----EAEGRNIKLSKEASSIS 1310
Cdd:pfam02463 655 EEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKklklEAEELLADRVQEAQDKI 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1311 SQLQDAQELLSEETRQKLNLSgRLRQLEEDKGCLMEQLEEEMEAKQAVERQASSLSVQLSDLKKRLE----ELSAAVELL 1386
Cdd:pfam02463 735 NEELKLLKQKIDEEEEEEEKS-RLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEeelrALEEELKEE 813
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1387 EEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQEL-EDVLMDLDSQRQLVSNLEKKQKKfdqMLAEERAVSAKSAE 1465
Cdd:pfam02463 814 AELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAeEELERLEEEITKEELLQELLLKE---EELEEQKLKDELES 890
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1466 ERDRAEAELREKETKVLALMKMLEDKQEALQEAERTVKALRVEMEDLISSKDDVGKSVHDLE--------RAKRGLEAFV 1537
Cdd:pfam02463 891 KEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEEnnkeeeeeRNKRLLLAKE 970
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1343958102 1538 EEMKTQMEELEDELQVAEDAKLRLEVNsQALRAQHERELQAREEQGEEKRRQLLK 1592
Cdd:pfam02463 971 ELGKVNLMAIEEFEEKEERYNKDELEK-ERLEEEKKKLIRAIIEETCQRLKEFLE 1024
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1076-1869 |
5.04e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 68.44 E-value: 5.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1076 ELRAQLAAKEEELQTTQACLDEESRQRGAALKRVRDLEALLAELQEDLEAEKVARGKAEAARRdLGEELNSLRSELEDSL 1155
Cdd:COG3096 282 ELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALR-QQEKIERYQEDLEELT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1156 DTTAAQQELRVKREQEMAML---KKAMEDEGRSHETQIQELRQkhgqAVEELREHLEQAKKVRAALEKAKQALEkeAADL 1232
Cdd:COG3096 361 ERLEEQEEVVEEAAEQLAEAearLEAAEEEVDSLKSQLADYQQ----ALDVQQTRAIQYQQAVQALEKARALCG--LPDL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1233 SADlrALSSTKQDVEQKKKKVEAQLNDLQLRFSESE---RQRNELSERVSKMTVELDSvtgllneaegrniklskeassi 1309
Cdd:COG3096 435 TPE--NAEDYLAAFRAKEQQATEEVLELEQKLSVADaarRQFEKAYELVCKIAGEVER---------------------- 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1310 SSQLQDAQELLSEETRQklnlsgrlrqleedkgclmeqleeemeakQAVERQASSLSVQLSDLKKRLEELSAAVELLEEG 1389
Cdd:COG3096 491 SQAWQTARELLRRYRSQ-----------------------------QALAQRLQQLRAQLAELEQRLRQQQNAERLLEEF 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1390 KKRLQRELEAAsgdyEEKAAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKKFDQM-------------LAEE 1456
Cdd:COG3096 542 CQRIGQQLDAA----EELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlaaqdalerLREQ 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1457 RAVSAKSAEERDRAEAELREKETKVLALMKMLEDKQEAL-QEAERTVKALRVEMEDLISSK------------DDV---- 1519
Cdd:COG3096 618 SGEALADSQEVTAAMQQLLEREREATVERDELAARKQALeSQIERLSQPGGAEDPRLLALAerlggvllseiyDDVtled 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1520 --------GKSVH-----DLERAKRGLEA---------FVE-------EMKTQMEELEDELQVaedaklrlEVNSQALRA 1570
Cdd:COG3096 698 apyfsalyGPARHaivvpDLSAVKEQLAGledcpedlyLIEgdpdsfdDSVFDAEELEDAVVV--------KLSDRQWRY 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1571 QHEREL-----QAREEQGEEKRRQLLKQVRELEAELEEERKQRTLASAARKKLEGEVK-----NTEEQLEAASRGRDEA- 1639
Cdd:COG3096 770 SRFPEVplfgrAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAvafapDPEAELAALRQRRSELe 849
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1640 --LKQLRKNQGQLKELHRELEEGRAAHKEILASA-----REAERRCKNLEAEILQMQEmlAAAERARKQAETErdELSEE 1712
Cdd:COG3096 850 reLAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAnlladETLADRLEELREELDAAQE--AQAFIQQHGKALA--QLEPL 925
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1713 VAggssgrSLLSD--EKRRLEAKISQLEEELEEEQANVETLNE---------------RLRKSQQLVDQLGAELT-AERA 1774
Cdd:COG3096 926 VA------VLQSDpeQFEQLQADYLQAKEQQRRLKQQIFALSEvvqrrphfsyedavgLLGENSDLNEKLRARLEqAEEA 999
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1775 SSQNREGSRlQLEKQTRDLKAKLQDVESQARSK------LKSSVAALEAKL-REAEEQLEVESRERQASAKNLRQK---- 1843
Cdd:COG3096 1000 RREAREQLR-QAQAQYSQYNQVLASLKSSRDAKqqtlqeLEQELEELGVQAdAEAEERARIRRDELHEELSQNRSRrsql 1078
|
890 900 910
....*....|....*....|....*....|
gi 1343958102 1844 EKKLKDLTAQMEDE----RKQAQDYKDQME 1869
Cdd:COG3096 1079 EKQLTRCEAEMDSLqkrlRKAERDYKQERE 1108
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1369-1922 |
5.96e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.76 E-value: 5.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1369 LSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKA--AAYDKLEKSRGRLQQELEDvlmdLDSQRQlvsNLEKKQ 1446
Cdd:PRK02224 164 LEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDlhERLNGLESELAELDEEIER----YEEQRE---QARETR 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1447 KKFDQMLAEERavsaKSAEERDRAEAELREKETKVLALMKMLEDKQEALQEAERTVKALRVEMEDLIsskDDVGKSVHDL 1526
Cdd:PRK02224 237 DEADEVLEEHE----ERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLL---AEAGLDDADA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1527 ERakrgLEAFVEEMKTQMEELEDELQVAEDAKLRLEVNSQALRAQhERELQAREEQGEEKRRQLLKQVRELEAELEEERK 1606
Cdd:PRK02224 310 EA----VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRED-ADDLEERAEELREEAAELESELEEAREAVEDRRE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1607 QRTLASAARKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQGQLKELHRELEEGRAAHKEilASAREAERRCKNLEAE-- 1684
Cdd:PRK02224 385 EIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEE--AEALLEAGKCPECGQPve 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1685 -------ILQMQEMLAAAERARKQAETERDELSEEVAGGSSGRSLlSDEKRRLEAKISQLEEELEEEQANVETLNERLRK 1757
Cdd:PRK02224 463 gsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLEELIAERRETIEEKRERAEE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1758 SQQLVDQLGAELTAERASSQNREGSRLQLEKQTRDLKAKLQDVES--QARSKLKSSVAALEAK------LREAEEQL--- 1826
Cdd:PRK02224 542 LRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKEriESLERIRTLLAAIADAedeierLREKREALael 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1827 EVESRERqasaknLRQKEKKLKDLTAQMEDER-KQAQDYKDQMEKSSARMKQLKHQLEEAEEEAQRVAAARRKLQRELDE 1905
Cdd:PRK02224 622 NDERRER------LAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE 695
|
570
....*....|....*..
gi 1343958102 1906 ALEANDALSREVSSLRS 1922
Cdd:PRK02224 696 LRERREALENRVEALEA 712
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1357-1924 |
6.37e-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: 67.79 E-value: 6.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1357 AVERQASSLSVQLSDLKKRLEELSAAVELLEEGKKrLQRELEAAsgDYEEKAAAYDKLEKSRGRLQQELEDVLMDLDSQR 1436
Cdd:TIGR02169 181 EVEENIERLDLIIDEKRQQLERLRREREKAERYQA-LLKEKREY--EGYELLKEKEALERQKEAIERQLASLEEELEKLT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1437 QLVSNLEKKQKKFDQMLAE-ERAVSAKSAEERDRAEAELREKETKVLALMKMLEDKQEALQEAERTVKALRVEMEDLISS 1515
Cdd:TIGR02169 258 EEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1516 KDDVGKSVHDLERAKRGLEAFVEEMKTQMEELEDELQvaedaklRLEVNSQALRAQHeRELQAREEQGEEKRRQLLKQVR 1595
Cdd:TIGR02169 338 IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE-------EVDKEFAETRDEL-KDYREKLEKLKREINELKRELD 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1596 ELEAELEEERKQRTLASAARKKLEGEVKNTEEQLEaasrgrdEALKQLRKNQGQLKELHRELEEgraahkeilasareAE 1675
Cdd:TIGR02169 410 RLQEELQRLSEELADLNAAIAGIEAKINELEEEKE-------DKALEIKKQEWKLEQLAADLSK--------------YE 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1676 RRCKNLEAEILQMQEMLAAAERARKQAETERDELSEEVAGGSSGRSLLSDEKRRLEAKISQLEEELEEEQANVET-LNER 1754
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVaAGNR 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1755 LRKSQQLVDQLGAE----LTAERAS-----------SQNREGSRLQLE-------------------------------- 1787
Cdd:TIGR02169 549 LNNVVVEDDAVAKEaielLKRRKAGratflplnkmrDERRDLSILSEDgvigfavdlvefdpkyepafkyvfgdtlvved 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1788 -KQTRDLKAKLQDVE---------------SQARSKLKSSVAALEAKLREAEEQLEVESRERQASAKNLRQKEKKLKDLT 1851
Cdd:TIGR02169 629 iEAARRLMGKYRMVTlegelfeksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELS 708
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1343958102 1852 AQMEDERKQAQDYKDQMEKSSARMKQLKHQLEEAEEEAQRVAAARRKLQRELDEALEANDALSREVSSLRSKL 1924
Cdd:TIGR02169 709 QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL 781
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1631-1861 |
8.80e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.94 E-value: 8.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1631 AASRGRDEALKQLRKNQGQLKELHRELEEGRAAHKEILASAREAERRCKNLEAEILQMQEMLAAAERARKQAETERDELS 1710
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1711 EEVAggsSGRSLLSDEKRRLEAKISQLEEELEEEQANVETLNERLRKSQQLVDQLGAELTAERASSQNREGSRLQLEKQT 1790
Cdd:COG4942 97 AELE---AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1343958102 1791 RDLKAKLQDVESQarsklKSSVAALEAKLREAEEQLEVESRERQASAKNLRQKEKKLKDLTAQMEDERKQA 1861
Cdd:COG4942 174 AELEALLAELEEE-----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
911-1132 |
9.96e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.94 E-value: 9.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 911 AKKQELEEVLHEMEARLEEEEERSISLQQEKKEMEQELQLMEAHIVQEEDARQKLQLEKAAVEGRVKKLEENLllsEDQN 990
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI---AELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 991 NKLQKERKLLEERLADM--------------SSNLAEEEEKSKNLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKV 1056
Cdd:COG4942 97 AELEAQKEELAELLRALyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1343958102 1057 EAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQACLDEESRQRGAALKRVRDLEALLAELQEDLEAEKVARGK 1132
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
936-1136 |
1.17e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 65.62 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 936 SLQQEKKEMEQELQLMEAHIVQEEDARQKLQLEKAAVEGRVKKLEENLllsEDQNNKLQKERKLLEERLADM-------- 1007
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI---AEAEAEIEERREELGERARALyrsggsvs 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1008 -------SSNLAEEEEKSKNLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQ 1080
Cdd:COG3883 104 yldvllgSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1343958102 1081 LAAKEEELQTTQACLDEESRQRGAALKRVRDLEALLAELQEDLEAEKVARGKAEAA 1136
Cdd:COG3883 184 LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1272-1901 |
1.49e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1272 NELSERVSKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQELLSeetrqklNLSGRLRQLEEDKGclmeQLEEE 1351
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE-------KLEKEVKELEELKE----EIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1352 MEAKQAVERQASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQreleaasgDYEEKAAAYDKLEKSRGRLQQELEDVLMD 1431
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK--------ELKEKAEEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1432 LDSQRQLVSNLEKKQKKfdqmlaeeravsaksAEERDRAEAELREKETKVLALMKMLEDKQEALQEAertvKALRVEMED 1511
Cdd:PRK03918 316 LSRLEEEINGIEERIKE---------------LEEKEERLEELKKKLKELEKRLEELEERHELYEEA----KAKKEELER 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1512 LisSKDDVGKSVHDLERAKRGLEAFVEEMKTQMEELEDELQVAEDAKLRLEVNSQALRAQHERELQAREEQGEEKRRQLL 1591
Cdd:PRK03918 377 L--KKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELL 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1592 KQVREleaeleeerkqrtlasaarkklegEVKNTEEQLEAAsrgrDEALKQLRKNqgqLKELHRELEEGR--AAHKEILA 1669
Cdd:PRK03918 455 EEYTA------------------------ELKRIEKELKEI----EEKERKLRKE---LRELEKVLKKESelIKLKELAE 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1670 SAREAERRCKNLEAEILqmqemlaaaerarKQAETERDELSEEVAGGSSGRSLLSDEKRRLEAKISQLEEELEEEQANVE 1749
Cdd:PRK03918 504 QLKELEEKLKKYNLEEL-------------EKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEE 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1750 TLNERLRKSQQL----VDQLGAELtAERASSQNREGSRLQLEKQTRDLKAKLQDVESQARSKLKSsVAALEAKLREAEEQ 1825
Cdd:PRK03918 571 ELAELLKELEELgfesVEELEERL-KELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEE-LAETEKRLEELRKE 648
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1343958102 1826 L-EVESRERQASAKNLRQKEKKLKDLTAQMEDERKQAQDYKDQMEKSSARMKQLKHQLEEAEEEAQRVAAARRKLQR 1901
Cdd:PRK03918 649 LeELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEE 725
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1354-1880 |
1.57e-10 |
|
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: 66.68 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1354 AKQAVERQASSLSVQLSDLKKRLEElsaAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLd 1433
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNE---SNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQL- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1434 sqRQLVSNLEkkqkkfdqmlaeeravSAKSAEERdraeaELREKETKVLALMKMLEDKQEALQEaertVKALRVEMEDLi 1513
Cdd:pfam15921 148 --QNTVHELE----------------AAKCLKED-----MLEDSNTQIEQLRKMMLSHEGVLQE----IRSILVDFEEA- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1514 sskddVGKSVHDLERAK----RGLEAFVEEMktqMEELEDELQVAEDAKLRLEVNSQALRAQHERELQAREEQGEEKRRQ 1589
Cdd:pfam15921 200 -----SGKKIYEHDSMStmhfRSLGSAISKI---LRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQ 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1590 LLKQVRELEAELEEErkqrtlASAARKklegEVKNTEEQLeaasrgrdEALKQLRKNQGQLkeLHRELEEGRAAHKEILA 1669
Cdd:pfam15921 272 LISEHEVEITGLTEK------ASSARS----QANSIQSQL--------EIIQEQARNQNSM--YMRQLSDLESTVSQLRS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1670 SAREAERrckNLEAEILQMQEMLAAAERARKQAETERDELSEEvaggsSGRslLSDEKRRLEAKISQLEEELEEEQANVE 1749
Cdd:pfam15921 332 ELREAKR---MYEDKIEELEKQLVLANSELTEARTERDQFSQE-----SGN--LDDQLQKLLADLHKREKELSLEKEQNK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1750 TLNERLRKSQQLVDQLGAELTAERASSQNREgSRLQLEKQTRDLKAKLQDVESQARSKLKSSVAALEAKLREAEEQLEVE 1829
Cdd:pfam15921 402 RLWDRDTGNSITIDHLRRELDDRNMEVQRLE-ALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKV 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1343958102 1830 SRERQASAKNLRQKEKKLKDLTAQMEDERKQAQDYKDQMEKSSAR----MKQLKH 1880
Cdd:pfam15921 481 VEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRvdlkLQELQH 535
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1206-1849 |
1.57e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 66.28 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1206 EHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQdveQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVEL 1285
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQ---ENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1286 DSvtgllNEAEGRNIKLSKEASSISSQLQDAQELLSEETRQ-KLNLSGRLRQ----------------------LEEDKG 1342
Cdd:pfam05483 148 KE-----NNATRHLCNLLKETCARSAEKTKKYEYEREETRQvYMDLNNNIEKmilafeelrvqaenarlemhfkLKEDHE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1343 CLMEQLEEEMEAKQAVERQASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEkaaaydkLEKSRGRLQ 1422
Cdd:pfam05483 223 KIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKE-------LIEKKDHLT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1423 QELEDVLMDL----DSQRQLVSNLEKKQKKFDQMLAEERAVSAKSAEERDRAEAELREKETKVLALMKMLEDKQEALQEA 1498
Cdd:pfam05483 296 KELEDIKMSLqrsmSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKN 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1499 ERTVKALRVEMEDLISSKDDVGKSVHDLE-----------------RAKRGLEAFVEEMKTQMEELEDELQVAEDAKLRL 1561
Cdd:pfam05483 376 EDQLKIITMELQKKSSELEEMTKFKNNKEveleelkkilaedekllDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDL 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1562 EVNSQALRAQHERELQAREEQGEEKRRQLLKQVRELEAELEEERKQRTLASAArKKLEGEVKNTEEQLEAASRGRDEALK 1641
Cdd:pfam05483 456 EIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEA-SDMTLELKKHQEDIINCKKQEERMLK 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1642 QLRKNQGQLKELHRELEEGRaahKEILASAREAERRCKNLEAEILQMQEMLAAAERARKQAETERDELSEEVAGGSSGRS 1721
Cdd:pfam05483 535 QIENLEEKEMNLRDELESVR---EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIE 611
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1722 LLSDEKRRLEAKISQLEEELEEEQANVETLNERLRKSQQ----LVDQLGAELTAERASSQN------------REGSRLQ 1785
Cdd:pfam05483 612 ELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQkfeeIIDNYQKEIEDKKISEEKlleevekakaiaDEAVKLQ 691
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1786 LEKQTR------------------------------DLKAKLQDVESQARSKLKSSVAALEAKLREAEEQLEVESRERQA 1835
Cdd:pfam05483 692 KEIDKRcqhkiaemvalmekhkhqydkiieerdselGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEK 771
|
730
....*....|....
gi 1343958102 1836 SAKNLRQKEKKLKD 1849
Cdd:pfam05483 772 LKMEAKENTAILKD 785
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
862-1656 |
1.97e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.52 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 862 EAAAKAEADLKDITQKhsqlVEEQAMLEAKLQAEAELYaeaedmRVRLEAKKQELEEV---LHEMEARLEEEEERSISLQ 938
Cdd:PRK04863 348 EKIERYQADLEELEER----LEEQNEVVEEADEQQEEN------EARAEAAEEEVDELksqLADYQQALDVQQTRAIQYQ 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 939 QEKK---EMEQELQLMEAHIVQEEDARQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLLEERLADMSSNLAEEE 1015
Cdd:PRK04863 418 QAVQaleRAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDV 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1016 EKSK------------NLSKLKSKH-------------ESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADL 1070
Cdd:PRK04863 498 ARELlrrlreqrhlaeQLQQLRMRLseleqrlrqqqraERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEA 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1071 QA----------QLAELRAQLAAKEEELQTTQACLDEESRQRGAALKRVRDLEALLAELQEDLEAEKVARGKAEAARRDL 1140
Cdd:PRK04863 578 RErrmalrqqleQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQAL 657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1141 GEELNSLrSELEDSLDTTaaqqelrvkreqemamLKKAMEDEGrshetqiqelrqkhGQAVEELREH--LEQAKKVRAAL 1218
Cdd:PRK04863 658 DEEIERL-SQPGGSEDPR----------------LNALAERFG--------------GVLLSEIYDDvsLEDAPYFSALY 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1219 EKAKQA-----LEKEAADLSA-------------DLRALSSTKQDVEQKKKKVEAQLNDLQLRFS--------------- 1265
Cdd:PRK04863 707 GPARHAivvpdLSDAAEQLAGledcpedlyliegDPDSFDDSVFSVEELEKAVVVKIADRQWRYSrfpevplfgraarek 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1266 ---ESERQRNELSERVSKMTVELdSVTGLLNEAEGRNIklskeASSISSQLQDAQELLSEETRQKLNLSGR-LRQLEEDK 1341
Cdd:PRK04863 787 rieQLRAEREELAERYATLSFDV-QKLQRLHQAFSRFI-----GSHLAVAFEADPEAELRQLNRRRVELERaLADHESQE 860
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1342 GCLMEQLEEEMEAKQAVERQASSLSVQLSD-LKKRLEELSAAVELLEEGKKRLQR------ELEAASGDYEEKAAAYDKL 1414
Cdd:PRK04863 861 QQQRSQLEQAKEGLSALNRLLPRLNLLADEtLADRVEEIREQLDEAEEAKRFVQQhgnalaQLEPIVSVLQSDPEQFEQL 940
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1415 EKSRGRLQQELEDVLMDLDSQRQLVSNLEK-KQKKFDQMLAEERAVSAKSAEERDRAEAELREKetkvlalmkmledKQE 1493
Cdd:PRK04863 941 KQDYQQAQQTQRDAKQQAFALTEVVQRRAHfSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRA-------------REQ 1007
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1494 ALQEAERTVKALRVeMEDLISSKDdvgksvhdlerAKRgleafvEEMKTQMEELED-ELQVAEDAKLRLevnsqalrAQH 1572
Cdd:PRK04863 1008 LRQAQAQLAQYNQV-LASLKSSYD-----------AKR------QMLQELKQELQDlGVPADSGAEERA--------RAR 1061
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1573 ERELQAREEQGEEKRRQLLKQVRELEAELEEERKQrtlasaaRKKLEGEVKNTEEQLEAASRGRDEALKQLRKNqGQLKE 1652
Cdd:PRK04863 1062 RDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKK-------LRKLERDYHEMREQVVNAKAGWCAVLRLVKDN-GVERR 1133
|
....
gi 1343958102 1653 LHRE 1656
Cdd:PRK04863 1134 LHRR 1137
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
829-1427 |
2.04e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 66.15 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 829 QWWRLFTKVKPLLQVTRQEEEMGQKEEELKAVReaaAKAEADLKDITQKHSQLVEEQAMLEAKLQAEAELYAEAEDMRVR 908
Cdd:TIGR00618 291 KAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSR---AKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSI 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 909 LEAKKQELEEVLHEMearleeeeersiSLQQEKKEMEQELQLM---------EAHIVQEEDARQK-LQLEKAAVEGRVKK 978
Cdd:TIGR00618 368 REISCQQHTLTQHIH------------TLQQQKTTLTQKLQSLckeldilqrEQATIDTRTSAFRdLQGQLAHAKKQQEL 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 979 LEENLLLSEDQNNKLQKERKLLEERLADMSSNLAEEEEKSKNLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEA 1058
Cdd:TIGR00618 436 QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNP 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1059 ELVD--------------------LQEQQADLQAQLAELRAQLAAKEEELQTTQACLDEESRQRGAALKRVRDLEALLAE 1118
Cdd:TIGR00618 516 ARQDidnpgpltrrmqrgeqtyaqLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVR 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1119 LQEDLEAEkvargkaeaarrdlgeelnslrSELEDSLdtTAAQQELRVKREQEMAMLKKAMEDEGRSHETQiQELRQKHG 1198
Cdd:TIGR00618 596 LQDLTEKL----------------------SEAEDML--ACEQHALLRKLQPEQDLQDVRLHLQQCSQELA-LKLTALHA 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1199 QAV----EELREHLEQAKKVRAALEKAKQALEKEAADLsadLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNEL 1274
Cdd:TIGR00618 651 LQLtltqERVREHALSIRVLPKELLASRQLALQKMQSE---KEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENAS 727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1275 SERVSKMTVELDSVTGLLNEAEgRNIKLSKEASSISSQLQDAQELLSEETRQKL-----NLSGRLRQLEEDKGclmEQLE 1349
Cdd:TIGR00618 728 SSLGSDLAAREDALNQSLKELM-HQARTVLKARTEAHFNNNEEVTAALQTGAELshlaaEIQFFNRLREEDTH---LLKT 803
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1343958102 1350 EEMEAKQAVERQASSLSVQLSDLKKRLEELSaavELLEEgKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELED 1427
Cdd:TIGR00618 804 LEAEIGQEIPSDEDILNLQCETLVQEEEQFL---SRLEE-KSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1212-1908 |
4.09e-10 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 65.38 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1212 KKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQlndlqlrfsesERQRNELSERVSKMTVELDSVTGL 1291
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYY-----------QLKEKLELEEEYLLYLDYLKLNEE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1292 LNEAEGRNIKLSKEASSISSQLQDAQELLSEETRQKLNLSGRLRQL-EEDKGCLMEQLEEEMEAKQAVERQASSLSVQLS 1370
Cdd:pfam02463 238 RIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLqEEELKLLAKEEEELKSELLKLERRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1371 DLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKKFD 1450
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEEL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1451 QMLAEERAVSAKSAEERDRAEAELREKETKVLALMKMLEDKQEALQEAERTVKALRVEMEDLISSKDDVGKSVHDLERAK 1530
Cdd:pfam02463 398 ELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKET 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1531 R----------GLEAFVEEMKTQMEELEDELQVAEDAKLRLEVNSQALRAQHERELQAREEQGEEKRR---QLLKQVREL 1597
Cdd:pfam02463 478 QlvklqeqlelLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIstaVIVEVSATA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1598 EAELEEERKQRTLASAARKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQGQLKELHRELEEGRAAHKEILASAREaerR 1677
Cdd:pfam02463 558 DEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTE---L 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1678 CKNLEAEILQMQEMLAAAERARKQAETERDELSEEVAGGSSGRSLLSDEKRRLEAKISQLEEELEEEQANVETLNERLRK 1757
Cdd:pfam02463 635 TKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKK 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1758 SQQLVDQLGAELTAERASSQNREGSRLQLEKQTRDLKAKLQDVESQARSKLKSSVAALEAKLREAEEQLEVESRERQASA 1837
Cdd:pfam02463 715 LKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEE 794
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1343958102 1838 KNLRQKEKKLKDLTAQMEDERKQAQDYKDQMEKSSARMKQLKHQLEEAEEEAQRVAAARRKLQRELDEALE 1908
Cdd:pfam02463 795 KLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITK 865
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
935-1455 |
4.49e-10 |
|
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: 64.76 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 935 ISLQQEKKEMEQELQlmeahivqeedaRQKLQLEKAAvegrvKKLEENLLLSEDQNNKLQKERKLLEERLADMSSNLAEE 1014
Cdd:pfam05557 12 SQLQNEKKQMELEHK------------RARIELEKKA-----SALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1015 EEksknlsklkskhesmiselEVRLKKeeKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQAC 1094
Cdd:pfam05557 75 AE-------------------LNRLKK--KYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1095 LDEESRQRGAALKRVRDLEALLAELQ-------------EDLE---------AEKVARGKAEAAR--------RDLGEEL 1144
Cdd:pfam05557 134 LEELQERLDLLKAKASEAEQLRQNLEkqqsslaeaeqriKELEfeiqsqeqdSEIVKNSKSELARipelekelERLREHN 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1145 NSLRSELEDSLDTTAAQQELRVKREQEMAMLKKA--MEDEGRSHETQIQE---LRQKHGQAV---EELREHLEQakkvra 1216
Cdd:pfam05557 214 KHLNENIENKLLLKEEVEDLKRKLEREEKYREEAatLELEKEKLEQELQSwvkLAQDTGLNLrspEDLSRRIEQ------ 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1217 aLEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVELDSVTGLLnEAE 1296
Cdd:pfam05557 288 -LQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAIL-ESY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1297 GRNIKLSKEASSISSQLQDAQELLSEETRQKLNLSGRLRQLEEDKGCLMEQLEEEMEAKQAVERQA-----SSLSVQLSD 1371
Cdd:pfam05557 366 DKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQEsladpSYSKEEVDS 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1372 LKKRLEELSAAVELLEEGKKRLQRELE---------------------AASGDYEEKAAAYDKLEKSRGRLQQELEDVLM 1430
Cdd:pfam05557 446 LRRKLETLELERQRLREQKNELEMELErrclqgdydpkktkvlhlsmnPAAEAYQQRKNQLEKLQAEIERLKRLLKKLED 525
|
570 580
....*....|....*....|....*.
gi 1343958102 1431 DLDSQRQL-VSNLEKKQKKFDQMLAE 1455
Cdd:pfam05557 526 DLEQVLRLpETTSTMNFKEVLDLRKE 551
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1054-1501 |
5.81e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.40 E-value: 5.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1054 RKVEAELVDLQEQQADLQaQLAELRAQLAAKEEELQTTQACLDEESRQRGAALKRVRDLEALLAELQEDLEAEKvargkA 1133
Cdd:COG4717 64 RKPELNLKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA-----L 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1134 EAARRDLGEELNSLRSELEDSLDTTAAQQELRVKREQEMAMLKKAMEDEGRSHETQIQELRQKHgqavEELREHLEQAKK 1213
Cdd:COG4717 138 EAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL----EELQQRLAELEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1214 VRAALEKAKQALEKEAADLSADLRALSSTKQdveQKKKKVEAQLNDLQLRFSESERQRNELSERV--------------- 1278
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAALEER---LKEARLLLLIAAALLALLGLGGSLLSLILTIagvlflvlgllallf 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1279 ---SKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQELLSEETRQKLNLSGRLRQLEEDKGCLMEQLEEEMEAK 1355
Cdd:COG4717 291 lllAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1356 QAVERQASSLSVQLSDLKKRLEELSAAVELLEEgKKRLQRELEAASGDYEEKAAAYDKLEksrgrLQQELEDVLMDLDSQ 1435
Cdd:COG4717 371 EIAALLAEAGVEDEEELRAALEQAEEYQELKEE-LEELEEQLEELLGELEELLEALDEEE-----LEEELEELEEELEEL 444
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1343958102 1436 RQLVSNLEKKQKKFDQML--AEERAVSAKSAEERDRAEAELREKETKVLALMKMLEDKQEALQEAERT 1501
Cdd:COG4717 445 EEELEELREELAELEAELeqLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
857-1465 |
1.01e-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: 63.83 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 857 LKAVREAAAKAEADLKDITQKHSQLVEEQAM------LEAKLQAEAELYAEAEDMRVRLEAKKQELEEVLHEMEARLEEE 930
Cdd:TIGR00618 228 LKHLREALQQTQQSHAYLTQKREAQEEQLKKqqllkqLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQ 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 931 EERSI--SLQQEKKEMEQELQLMEAHIVQEEDARQKLQLEKAAVEgrvkklEENLLLSEDQNNKLQKE----RKLLEERL 1004
Cdd:TIGR00618 308 QAQRIhtELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHS------QEIHIRDAHEVATSIREiscqQHTLTQHI 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1005 ADMSSNLAEEEEKSKNLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQ----------L 1074
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTaqceklekihL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1075 AELRAQLAAKEEELQTTQACLDEESRQ---RGAALKRVRDLEALLAELQEDLEAEKVARGKAEAARRDLGEELNSLRsEL 1151
Cdd:TIGR00618 462 QESAQSLKEREQQLQTKEQIHLQETRKkavVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYA-QL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1152 EDSLDTTAAQQELRVKREQEMAMLKKAMEDEGRSHETQIQELRQ---KHGQAVEELREHLEQAKKVRAALEKAKQALEKE 1228
Cdd:TIGR00618 541 ETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEdipNLQNITVRLQDLTEKLSEAEDMLACEQHALLRK 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1229 AADLSADLRaLSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERV-------------SKMTVELDSVTGLLNEA 1295
Cdd:TIGR00618 621 LQPEQDLQD-VRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVlpkellasrqlalQKMQSEKEQLTYWKEML 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1296 EGRNIKLSKEASSISSQLQDAQELLSEETRQKLNLSGRLRQLEEDKGCLMEQLEEEMEAKQAVERQASSLSVQLSDLKKR 1375
Cdd:TIGR00618 700 AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAE 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1376 LEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAY-DKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLA 1454
Cdd:TIGR00618 780 LSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDeDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSK 859
|
650
....*....|.
gi 1343958102 1455 EERAVSAKSAE 1465
Cdd:TIGR00618 860 QLAQLTQEQAK 870
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1487-1726 |
1.03e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.78 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1487 MLEDKqEALQEAERTVKalrvEMEDLISSKDDVgksvhdlERAKRGLEAF--VEEMKTQMEELEDELQVAEDAKLRLEVn 1564
Cdd:COG4913 217 MLEEP-DTFEAADALVE----HFDDLERAHEAL-------EDAREQIELLepIRELAERYAAARERLAELEYLRAALRL- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1565 sqaLRAQHEREL-QAREEQGEEKRRQLLKQVRELEAELEEERKQRTLASAARKKLEGEVKNT-EEQLEAASRGRDEALKQ 1642
Cdd:COG4913 284 ---WFAQRRLELlEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERR 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1643 LRKNQGQLKELHRELEEGRAAHKEILASAREAERRCKNLEAEIlqmQEMLAAAERARKQAETERDELSEEVAGGSSGRSL 1722
Cdd:COG4913 361 RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEAL---EEALAEAEAALRDLRRELRELEAEIASLERRKSN 437
|
....
gi 1343958102 1723 LSDE 1726
Cdd:COG4913 438 IPAR 441
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1298-1731 |
1.08e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1298 RNIKLSKEASSISSQLQDAQELLSEETRQKLNLSGRLRQLEEDKGCLMEQLEEEMEAKQAVE--RQASSLSVQLSDLKKR 1375
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1376 LEELSAAVELLEEgkkrLQRELEAASGDYEE-KAAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLA 1454
Cdd:COG4717 148 LEELEERLEELRE----LEEELEELEAELAElQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1455 EERAVSAKSAEERDRAEAELREKETKVL-----ALMKMLEDKQEALQEAERTVKALRVEMEDLISSKDDVGKSVHDLERA 1529
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLKEARLLlliaaALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1530 KRGLEAFVEEMKTQMEELEDELQV-----------AEDAKLRLEVNSQALRAQHERELQAREEQGEEKRRQLLKQVRELE 1598
Cdd:COG4717 304 AEELQALPALEELEEEELEELLAAlglppdlspeeLLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1599 AELEEERKQRtlaSAARKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQ--GQLKELHRELEEGRAAHKEILASAREAER 1676
Cdd:COG4717 384 EEELRAALEQ---AEEYQELKEELEELEEQLEELLGELEELLEALDEEEleEELEELEEELEELEEELEELREELAELEA 460
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1343958102 1677 RCKNLEAEilqmqEMLAAAERARKQAETERDELSEEVAGGSSGRSLLSDEKRRLE 1731
Cdd:COG4717 461 ELEQLEED-----GELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
937-1340 |
1.21e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 937 LQQEKKEMEQELQLMEAHIVQEEDARQKLQLEKAAVE--GRVKKLEENLLLSEDQNNKLQKERKLLEERLADMSSNLAEE 1014
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1015 EEKSKnlsKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQAc 1094
Cdd:COG4717 173 AELQE---ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1095 ldeesRQRGAALKRVRDLEALLAELQEDLEAEKVARGKAEAARRDLGEELNSLRSELEDSLDTTAAQQELRVKREQEMAM 1174
Cdd:COG4717 249 -----RLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1175 LKKAMEDEGRSHETQIQELRQKHGQAVEELRE--HLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKK 1252
Cdd:COG4717 324 LLAALGLPPDLSPEELLELLDRIEELQELLREaeELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEE 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1253 VEAQLNDLQLRFSESERQRNELSErvSKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDA--QELLSEETRQKLNL 1330
Cdd:COG4717 404 LEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEELEEELEELREELAELEAELEQLeeDGELAELLQELEEL 481
|
410
....*....|
gi 1343958102 1331 SGRLRQLEED 1340
Cdd:COG4717 482 KAELRELAEE 491
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1039-1870 |
1.31e-09 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 63.53 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1039 LKKEEKTRQDVEKAKRKVEAELVDLQEQQADlQAQLAELRAQLAAKEEELQTTQacldeesrqrgaalKRVRDLEALLAE 1118
Cdd:TIGR00606 185 IKALETLRQVRQTQGQKVQEHQMELKYLKQY-KEKACEIRDQITSKEAQLESSR--------------EIVKSYENELDP 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1119 LQEDLEaekvargkaeaarrdlgeELNSLRSELEDSLDTTAAQQELRVKREQEMAMLKKAMEDEGRSHETQIQELRQKHG 1198
Cdd:TIGR00606 250 LKNRLK------------------EIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQ 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1199 QAVEELREHLEQAKKVRAALEKAKQALEKEAADLsadlralsstkqDVEQKKKKVEAQLNDLQLRFSESERQRNELSERV 1278
Cdd:TIGR00606 312 RTVREKERELVDCQRELEKLNKERRLLNQEKTEL------------LVEQGRLQLQADRHQEHIRARDSLIQSLATRLEL 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1279 SKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQELLSEETRQKLNLSGRLRQLEEDKGCLMEQLEEEMEAKQAV 1358
Cdd:TIGR00606 380 DGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFV 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1359 ERQASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAydKLEKSRGRLQQELEDVLMDLDSQRQL 1438
Cdd:TIGR00606 460 IKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKA--DLDRKLRKLDQEMEQLNHHTTTRTQM 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1439 VSNLEKKQKKFDQML------AEERAVSAKSAEERDRAEAELREKETKVLALMKMLEDKQEALQEAERTVKALRVEMEDL 1512
Cdd:TIGR00606 538 EMLTKDKMDKDEQIRkiksrhSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESK 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1513 ISSKDDVGK------SVHDLERAKRGLEAFVEEMKTQMEELEDELQVAEDAKLRLEVNSQALRAQHERELQAREEQgEEK 1586
Cdd:TIGR00606 618 EEQLSSYEDklfdvcGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAEL-QEF 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1587 RRQLLKQVRELEAELEEERKQRTLASAARKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQGQLKELHRELEEGRAAHKE 1666
Cdd:TIGR00606 697 ISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGT 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1667 ILASAREAErRCKNLEAEILQMQEMLAAAERARKQAETERDelseevagGSSGRSLLSDEKRRLEAKISQLEEELEEEQA 1746
Cdd:TIGR00606 777 IMPEEESAK-VCLTDVTIMERFQMELKDVERKIAQQAAKLQ--------GSDLDRTVQQVNQEKQEKQHELDTVVSKIEL 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1747 NVETLNERLRKSQQLVDQLGaELTAERASSQNREGSRLQLEKQTRDLKAKLQDVE---SQARSKLKSSVAALEAKLREAE 1823
Cdd:TIGR00606 848 NRKLIQDQQEQIQHLKSKTN-ELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIreiKDAKEQDSPLETFLEKDQQEKE 926
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 1343958102 1824 EQLEVESRERQASAKNLRQKEKKLKDLTAQMEDERKQAQDYKDQMEK 1870
Cdd:TIGR00606 927 ELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLK 973
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
945-1285 |
1.36e-09 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has 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: 62.39 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 945 EQELQLMEAHIVQEEDARQKLQLEKAAVEgrvkKLEENLLLSEDQNNKLQKERKLLEERLADMSSNLAEEEEKSKNLSKL 1024
Cdd:pfam19220 37 EAILRELPQAKSRLLELEALLAQERAAYG----KLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1025 KSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQACLDEESRQRGA 1104
Cdd:pfam19220 113 LRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1105 ALKRVRDLEALLA-------ELQEDLEAEKVARGKAEAARRD----LGEELNSLRSELEDSLDTTAAQQELRVKREQEMA 1173
Cdd:pfam19220 193 LTRRLAELETQLDatrarlrALEGQLAAEQAERERAEAQLEEaveaHRAERASLRMKLEALTARAAATEQLLAEARNQLR 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1174 MLKKAMEDEGRSHETQIQELRQKHgQAVEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKV 1253
Cdd:pfam19220 273 DRDEAIRAAERRLKEASIERDTLE-RRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASL 351
|
330 340 350
....*....|....*....|....*....|..
gi 1343958102 1254 EAQLNDLQLRFsesERQRNELSERVSKMTVEL 1285
Cdd:pfam19220 352 SDRIAELTKRF---EVERAALEQANRRLKEEL 380
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1211-1462 |
1.49e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1211 AKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVELDSVTG 1290
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1291 LLNEAEGRNIKLSKEASSISSQLQDAQELLSEETRQKLNLSGRLRQLeedkgclmeqleeemeaKQAVERQASSLSVQLS 1370
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL-----------------APARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1371 DLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKKFD 1450
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
250
....*....|..
gi 1343958102 1451 QMLAEERAVSAK 1462
Cdd:COG4942 241 ERTPAAGFAALK 252
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
936-1674 |
2.11e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 63.05 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 936 SLQQEKKEMEQELQLMEAHIVQEEDARQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKER-KLLEERLADMSSNLAEE 1014
Cdd:COG3096 452 QATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERSQAWQTARELLRRYRSQQALAQRlQQLRAQLAELEQRLRQQ 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1015 EEKsknlsklkskhESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQ----------LAAK 1084
Cdd:COG3096 532 QNA-----------ERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQleqlrarikeLAAR 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1085 EEELQTTQACLDEESRQRGAALKRVRDLEALLAELQEDLEAEKVARGKAEAARRDLGEELNSLrseledSLDTTAAQQEL 1164
Cdd:COG3096 601 APAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERL------SQPGGAEDPRL 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1165 RVKREQEMAMLKKAMEDEGRSHETQIQELR---QKHGQAVEELrehleqaKKVRAALekakQALEKEAADL---SADLRA 1238
Cdd:COG3096 675 LALAERLGGVLLSEIYDDVTLEDAPYFSALygpARHAIVVPDL-------SAVKEQL----AGLEDCPEDLyliEGDPDS 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1239 LSSTKQDVEQKKKKVEAQLNDLQLRFSESERQ----RNELSERVSKMTVELDSVTGLLNEAEGRNIKLSKEASS----IS 1310
Cdd:COG3096 744 FDDSVFDAEELEDAVVVKLSDRQWRYSRFPEVplfgRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAfsqfVG 823
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1311 SQLQDAQELLSEETRQKLNlsGRLRQLEedkgclmEQLEEEMEAKQAVERQASSLSVQLSDLKKRLEELSA-AVELLEEG 1389
Cdd:COG3096 824 GHLAVAFAPDPEAELAALR--QRRSELE-------RELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLlADETLADR 894
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1390 KKRLQRELEAAsgdyeEKAAAYdklEKSRGRLQQELEDVLMDLDSQRQlvsnlekkqkKFDQMlaeeravsaksAEERDR 1469
Cdd:COG3096 895 LEELREELDAA-----QEAQAF---IQQHGKALAQLEPLVAVLQSDPE----------QFEQL-----------QADYLQ 945
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1470 AEAELREKETKVLALMKMLEDKQE-ALQEAERTvkalrvemedLISSKDDVGKSVHDLERAKRGLEAFVEEMKTQMEELE 1548
Cdd:COG3096 946 AKEQQRRLKQQIFALSEVVQRRPHfSYEDAVGL----------LGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYS 1015
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1549 DELQVAEDAKLRLEVNSQALRAqHERELQA--------REEQGEEKRRQLLKQVRELEAELEEERKQRTLASAARKKLEG 1620
Cdd:COG3096 1016 QYNQVLASLKSSRDAKQQTLQE-LEQELEElgvqadaeAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQK 1094
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1343958102 1621 EVKNTE-------EQLEAASRGRDeALKQLRKNQGQLKELHR------ELEEGRAAHKEILASAREA 1674
Cdd:COG3096 1095 RLRKAErdykqerEQVVQAKAGWC-AVLRLARDNDVERRLHRrelaylSADELRSMSDKALGALRLA 1160
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1368-1925 |
2.55e-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: 62.55 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1368 QLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDK-LEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQ 1446
Cdd:pfam12128 252 TLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDqWKEKRDELNGELSAADAAVAKDRSELEALEDQH 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1447 KKFDQMLAEERAVSAkSAEERDRAEAELREKEtkvlalMKMLEDKQEALQEAERTVKALRVEmedlisskddvgKSVHDL 1526
Cdd:pfam12128 332 GAFLDADIETAAADQ-EQLPSWQSELENLEER------LKALTGKHQDVTAKYNRRRSKIKE------------QNNRDI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1527 ERAKRGLEAFVEEMKTQMEELEDELQVAEDAkLRLEVNSQALRAQhERELQAREEQGEEKRRqlLKQVRELEAELEEERK 1606
Cdd:pfam12128 393 AGIKDKLAKIREARDRQLAVAEDDLQALESE-LREQLEAGKLEFN-EEEYRLKSRLGELKLR--LNQATATPELLLQLEN 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1607 QRTLASAARKKLEGEVKNTEE---QLEAASRGRDEALKQLRKNQGQLKELHRELEE------------------------ 1659
Cdd:pfam12128 469 FDERIERAREEQEAANAEVERlqsELRQARKRRDQASEALRQASRRLEERQSALDElelqlfpqagtllhflrkeapdwe 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1660 ---GRAAHKEIL------------ASAREAERRCKNLEAEILQMQEMLAAAErarkQAETERDELSEEVAGGSSGRSLLS 1724
Cdd:pfam12128 549 qsiGKVISPELLhrtdldpevwdgSVGGELNLYGVKLDLKRIDVPEWAASEE----ELRERLDKAEEALQSAREKQAAAE 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1725 DEKRRLEAKISQLEEELEEEQANVETLNERLRK----SQQLVDQLGAELTAERASSQNR----EGSRLQLEKQTRDLKAK 1796
Cdd:pfam12128 625 EQLVQANGELEKASREETFARTALKNARLDLRRlfdeKQSEKDKKNKALAERKDSANERlnslEAQLKQLDKKHQAWLEE 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1797 LQDVESQARSKLKSSVAALEAKLREAEEQLEVESRERQASAK----------------------NLRQKEKKLKDLTAQM 1854
Cdd:pfam12128 705 QKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKaelkaletwykrdlaslgvdpdVIAKLKREIRTLERKI 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1855 EDERKQAQD---YKD-QMEKSSARMKQLKHQLEEAEEEAQRVAAARRKLQRE-------LDEALEANDALSREVSSLRSK 1923
Cdd:pfam12128 785 ERIAVRRQEvlrYFDwYQETWLQRRPRLATQLSNIERAISELQQQLARLIADtklrrakLEMERKASEKQQVRLSENLRG 864
|
..
gi 1343958102 1924 LR 1925
Cdd:pfam12128 865 LR 866
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1070-1595 |
2.68e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1070 LQAQLAELRAQLAAKEEELQTTQAcldeesRQRGAALKRVRDLEALLAELQEDLEAEKVARGKAEAARRDLgEELNSLRS 1149
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQG------RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEEL-EELEAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1150 ELEDSLDTTAAQQELR--VKREQEMAMLKKAMEDEGRSHETQIQELRQKHGQAVEELREHLEQAKKVRAALEKAKQALEK 1227
Cdd:COG4717 113 ELREELEKLEKLLQLLplYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1228 EAADLSADLRALSSTKQDVEQKKKKVEAQLNDL--QLRFSESERQRNELSERVSKMTVELDSVTGLLnEAEGRNIKLSKE 1305
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELeeELEQLENELEAAALEERLKEARLLLLIAAALL-ALLGLGGSLLSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1306 ASSISSQLQDAQELL----SEETRQKLNLSGRLRQLEEdkgclmeQLEEEMEAKQAVERQASSLSVQLSDLKKRLEELSA 1381
Cdd:COG4717 272 ILTIAGVLFLVLGLLallfLLLAREKASLGKEAEELQA-------LPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1382 AVELLeegkKRLQRELEAAsgdyeEKAAAYDKLEKSRGRLQQELedvlmDLDSQRQLVSNLEKKQKKFDQmlaeeravsa 1461
Cdd:COG4717 345 RIEEL----QELLREAEEL-----EEELQLEELEQEIAALLAEA-----GVEDEEELRAALEQAEEYQEL---------- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1462 ksAEERDRAEAELREKETKVLALMKMLEDKQ--EALQEAERTVKALRVEMEDLISSKDDVGKSVHDLERAKRgleafVEE 1539
Cdd:COG4717 401 --KEELEELEEQLEELLGELEELLEALDEEEleEELEELEEELEELEEELEELREELAELEAELEQLEEDGE-----LAE 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1343958102 1540 MKTQMEELEDELQVAEDAKLRLEVNSQALRaqherelQAREEQGEEKRRQLLKQVR 1595
Cdd:COG4717 474 LLQELEELKAELRELAEEWAALKLALELLE-------EAREEYREERLPPVLERAS 522
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1481-1717 |
3.10e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.32 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1481 VLALMKMLEDKQEALQEAERTVKALRVEMEDLISSKDDVGKSVHDLERAKRGLEAFVEEMKTQMEELEDELQVAEDAKLR 1560
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1561 LEVNSQALRAQHERELQAREEQGEEKRRQLLKQVRELEAELEEERKQRTLASAARKKLEgEVKNTEEQLEAASRGRDEAL 1640
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAE-ELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1641 KQLRKNQGQLKELHRELEEGRAAHKEILASAR----EAERRCKNLEAEILQMQEMLAAAERARKQAETERDELSEEVAGG 1716
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEkelaELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
.
gi 1343958102 1717 S 1717
Cdd:COG4942 254 K 254
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1577-1782 |
3.45e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.93 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1577 QAREEQGEEKRRQLLKQVRELEAELEEERKQRTLASAARKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQGQLKELHRE 1656
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1657 LEEGRAAHKEILA------------------SAREAERRCKNLEAEILQMQEMLAAAERARKQAETERDELSEEVAGGSS 1718
Cdd:COG4942 99 LEAQKEELAELLRalyrlgrqpplalllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1343958102 1719 GRSLLSDEKRRLEAKISQLEEELEEEQANVETLNER---LRKSQQLVDQLGAELTAERASSQNREGS 1782
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAElaeLQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1201-1882 |
3.91e-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: 61.91 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1201 VEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESE---RQRNELSER 1277
Cdd:TIGR00618 175 LDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHaylTQKREAQEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1278 VSKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQELLSEEtrqklnlsgRLRQLEEDKGCLMEQLEEEMEAKQA 1357
Cdd:TIGR00618 255 QLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIK---------AVTQIEQQAQRIHTELQSKMRSRAK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1358 VERQASSLSVQLSDLkkrlEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRgRLQQELEDVLMDLDSQRQ 1437
Cdd:TIGR00618 326 LLMKRAAHVKQQSSI----EEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIH-TLQQQKTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1438 LVSNLEKKQKKFDQMLAEERAVSAKSAEERDRAEAELREKETKVLALMKMLEDKQEALQEAERTVKALRvEMEDLISSKD 1517
Cdd:TIGR00618 401 ELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLK-EREQQLQTKE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1518 DVGKSVhdlERAKRGLEAFVEEMKTQMEELEDELqvaedaklrLEVNSQALRAQHERELQAREEQGEEKRRQLLKQVREL 1597
Cdd:TIGR00618 480 QIHLQE---TRKKAVVLARLLELQEEPCPLCGSC---------IHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDV 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1598 EAELEEERKQRtlasaarKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQGQLKELHRELEEgRAAHKEILASAREAERR 1677
Cdd:TIGR00618 548 YHQLTSERKQR-------ASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK-LSEAEDMLACEQHALLR 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1678 CKNLEAEILQMQEMLAAAERARKQAETERDELSEEVAGGSSGRSLLS---DEKR---RLEAKISQLEEELEEEQANVETL 1751
Cdd:TIGR00618 620 KLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSirvLPKEllaSRQLALQKMQSEKEQLTYWKEML 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1752 NERLRKSQQLVDQLGaELTAERASSQNREGSRLQ-LEKQTRDLKAKLQDVESQARSKLKSSVAA-------------LEA 1817
Cdd:TIGR00618 700 AQCQTLLRELETHIE-EYDREFNEIENASSSLGSdLAAREDALNQSLKELMHQARTVLKARTEAhfnnneevtaalqTGA 778
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1343958102 1818 KLREAEEQLEVESRERQASAKNLRQKEKKLKD--------LTAQMEDERKQAQDYKDQMEKSSARMKQLKHQL 1882
Cdd:TIGR00618 779 ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQeipsdediLNLQCETLVQEEEQFLSRLEEKSATLGEITHQL 851
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
966-1432 |
4.14e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 966 QLEKAAVEgRVKKLEENLLLSEDQNNKLQKERKLLEERLADMSSNLAEEEEKSKNLSKLKSKHESMisELEVRLKKEEKT 1045
Cdd:COG4717 50 RLEKEADE-LFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL--REELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1046 RQDVEKAKRKVEAELVDLQEQQADLQAQLA---ELRAQLAAKEEELQTTQACLDEESRQRG-AALKRVRDLEALLAELQE 1121
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEelrELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1122 DLEAEKVARGKAEAARRDLGEELNSLRSELEdsldttAAQQELRVKREQEMAMLkkamedegrshETQIQELRQKHGQAV 1201
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELE------AAALEERLKEARLLLLI-----------AAALLALLGLGGSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1202 EELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKM 1281
Cdd:COG4717 270 SLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1282 TVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQELLS--EETRQKLNLSGRLRQLEED---------KGCLMEQLEE 1350
Cdd:COG4717 350 QELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAalEQAEEYQELKEELEELEEQleellgeleELLEALDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1351 EMEAKQAVERQASSLSVQLSDLKKRLEELSAAVELLEEGKK---------RLQRELEAASGDYEEKAAAYDKLEKSRGRL 1421
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAELEAELEQLEEDGElaellqeleELKAELRELAEEWAALKLALELLEEAREEY 509
|
490
....*....|.
gi 1343958102 1422 QQELEDVLMDL 1432
Cdd:COG4717 510 REERLPPVLER 520
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1201-1595 |
4.28e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 61.89 E-value: 4.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1201 VEELREHLEQAKKVRAALEKAKQALEKE---AADLSADLRALSSTKQDVEQKKKKVEAQLNDLQ--LRFSES-ERQR--- 1271
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEqyrLVEMARELEELSARESDLEQDYQAASDHLNLVQtaLRQQEKiERYQedl 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1272 NELSERVSKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQELLSEETRQKLNLSGRLRQLEEDKGCLmeqleee 1351
Cdd:COG3096 357 EELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALC------- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1352 meakqaverQASSLSVqlSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEK-----SRGRLQQELE 1426
Cdd:COG3096 430 ---------GLPDLTP--ENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKiagevERSQAWQTAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1427 DVLMDLDSQRQLVSNLEKKQKKFDQmlAEERAVSAKSAEerdRAEAELREKETKVLALMKMLEDKQEALQEaertvkalr 1506
Cdd:COG3096 499 ELLRRYRSQQALAQRLQQLRAQLAE--LEQRLRQQQNAE---RLLEEFCQRIGQQLDAAEELEELLAELEA--------- 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1507 vEMEDLISSKDDVGKsvhdlerAKRGLEAFVEEMKTQMEELED---ELQVAEDAKLRLE-------VNSQALRA------ 1570
Cdd:COG3096 565 -QLEELEEQAAEAVE-------QRSELRQQLEQLRARIKELAArapAWLAAQDALERLReqsgealADSQEVTAamqqll 636
|
410 420
....*....|....*....|....*
gi 1343958102 1571 QHERELQAREEQGEEKRRQLLKQVR 1595
Cdd:COG3096 637 EREREATVERDELAARKQALESQIE 661
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
947-1123 |
8.69e-09 |
|
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: 58.01 E-value: 8.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 947 ELQLMEAHIVQEEDARQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLLEERLADMSSNLAEEEEKSKNLSKLKs 1026
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1027 khesmisELEVRLKKEEKtrqdVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQACLDEESRQRGAAL 1106
Cdd:COG1579 90 -------EYEALQKEIES----LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170
....*....|....*...
gi 1343958102 1107 KRVR-DLEALLAELQEDL 1123
Cdd:COG1579 159 EELEaEREELAAKIPPEL 176
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1050-1277 |
1.05e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.46 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1050 EKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQACLDEESRQRGAALKRVRDLEALLAELQEDLEaeKVA 1129
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG--ERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1130 RGKAEAarrdlGEELNSLRSELE-DSLDTTAAQqelrvkreqeMAMLKKAMEDEGRSHEtQIQELRQKHGQAVEELREHL 1208
Cdd:COG3883 93 RALYRS-----GGSVSYLDVLLGsESFSDFLDR----------LSALSKIADADADLLE-ELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1343958102 1209 EQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSER 1277
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1239-1871 |
1.26e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.03 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1239 LSSTKQDVEQKkkkvEAQLNDLQLRFSESERQRNELSERVSKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQE 1318
Cdd:TIGR04523 42 LKTIKNELKNK----EKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1319 llseetrQKLNLSGRLRQLEEDKGCLMEQLEEEMEAKQAVERQASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELE 1398
Cdd:TIGR04523 118 -------QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNID 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1399 AASGDYEEKAAAYDKLEKSRGRlQQELEDVLMDLDSQR-QLVSNLEKKQKKFDQMLAEERAVSAK---SAEERDRAEAEL 1474
Cdd:TIGR04523 191 KIKNKLLKLELLLSNLKKKIQK-NKSLESQISELKKQNnQLKDNIEKKQQEINEKTTEISNTQTQlnqLKDEQNKIKKQL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1475 REKETKVLALMKMLEDKQEALQEAERTVKALRVEMEDLISSkdDVGKSVHDLERAKRGLEAFVEEMKTQMEELEDELQVA 1554
Cdd:TIGR04523 270 SEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNK--ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1555 EDAKLRLEVNSQALR---AQHERELQAREEQGEEKRRQLLKQVRELEAELEEERKQRTLAsaarKKLEGEVKNTEEQLEA 1631
Cdd:TIGR04523 348 KKELTNSESENSEKQrelEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLN----QQKDEQIKKLQQEKEL 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1632 ASRGRDEALKQLRKNQGQLKELHRELEEGRAAHKEILASAREAERRCKNLEAEILQMQEMLAAAERARKQAETERD---- 1707
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKklne 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1708 ---ELSEEVAGGSSGRSLLSDEKRRLEAKISQLEEELEEEQANVETLNERLRKSQ--QLVDQLGAELTAERASSQNREGS 1782
Cdd:TIGR04523 504 ekkELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENleKEIDEKNKEIEELKQTQKSLKKK 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1783 RLQLEKQTRDLKAKLQDVESQARSKLKSsVAALEAKLREAEEqlevESRERQASAKNLRQKEKKLKDLTAQMEDERKQAQ 1862
Cdd:TIGR04523 584 QEEKQELIDQKEKEKKDLIKEIEEKEKK-ISSLEKELEKAKK----ENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
....*....
gi 1343958102 1863 DYKDQMEKS 1871
Cdd:TIGR04523 659 NKWPEIIKK 667
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
910-1433 |
1.28e-08 |
|
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: 60.52 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 910 EAKKQELEEVLHEMEARLEEEEERSISLQQEKKEMEQELQLMEAHIvqeedarqklqlekaavegrvKKLEENLLLSEDQ 989
Cdd:pfam15921 341 EDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADL---------------------HKREKELSLEKEQ 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 990 NNKLQKErklleerlaDMSSNLA------EEEEKSKNLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAelvdl 1063
Cdd:pfam15921 400 NKRLWDR---------DTGNSITidhlrrELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSS----- 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1064 qeqqadLQAQLAELRAQLAAKEEELQTTQACLDEESRQrgaalkrVRDLEALLAELQEDLEAEKVARGKAEaARRDLG-E 1142
Cdd:pfam15921 466 ------LTAQLESTKEMLRKVVEELTAKKMTLESSERT-------VSDLTASLQEKERAIEATNAEITKLR-SRVDLKlQ 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1143 ELNSLRSElEDSLDttaaqqelRVKREQEMAMLKKAMEDEgrshetQIQELRQKhgqaVEELREHLEQAKKVRAALEKAK 1222
Cdd:pfam15921 532 ELQHLKNE-GDHLR--------NVQTECEALKLQMAEKDK------VIEILRQQ----IENMTQLVGQHGRTAGAMQVEK 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1223 QALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLQLrfsESERQRNELSERVSKMTVELDSVTGLLNEAE-GRNI- 1300
Cdd:pfam15921 593 AQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLEL---EKVKLVNAGSERLRAVKDIKQERDQLLNEVKtSRNEl 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1301 -KLSKEASSISSQLQDAQELLSEETRQ-KLNLSGRLRQLEEDKGCLMEQLEEEMEAKQ---AVERQASSLSVQLSDLKKR 1375
Cdd:pfam15921 670 nSLSEDYEVLKRNFRNKSEEMETTTNKlKMQLKSAQSELEQTRNTLKSMEGSDGHAMKvamGMQKQITAKRGQIDALQSK 749
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1343958102 1376 LEELSAAV-------ELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLD 1433
Cdd:pfam15921 750 IQFLEEAMtnankekHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALD 814
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
857-1448 |
1.59e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.03 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 857 LKAVREAAAKAEADLKDI-------TQKHSQLVEEQAMLEAKLQAEAELYAEAEDMRVRLEAKKQELEEVLHEMEARLEE 929
Cdd:TIGR04523 42 LKTIKNELKNKEKELKNLdknlnkdEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 930 EEERSISLQQEKKEMEQELQLMEAHIVQEED-------ARQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLLEE 1002
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKeleklnnKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1003 RLadmsSNLAEEEEKSKNLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAE------ 1076
Cdd:TIGR04523 202 LL----SNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEkqkele 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1077 -LRAQLAAKEEELQTTQACLDEESRQRGAALkrVRDLEALLAELQEDLEAEKVARGKAEAARRDLGEELNSLRSELEDSL 1155
Cdd:TIGR04523 278 qNNKKIKELEKQLNQLKSEISDLNNQKEQDW--NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1156 DTTAAQQELRVKREQEMAMLKKAME---DEGRSHETQIQELRQKHgQAVEELREHLEQAKKVraaLEKAKQALEKEAADL 1232
Cdd:TIGR04523 356 SENSEKQRELEEKQNEIEKLKKENQsykQEIKNLESQINDLESKI-QNQEKLNQQKDEQIKK---LQQEKELLEKEIERL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1233 SADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVELDSVTGLLNEAEgrniklsKEASSISSQ 1312
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE-------KELKKLNEE 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1313 LQDAQELLSEETRQKLNLSGRLRQLEEDKgclmeqleeemeakqaverqaSSLSVQLSDLKKRLEELSAAV--ELLEEGK 1390
Cdd:TIGR04523 505 KKELEEKVKDLTKKISSLKEKIEKLESEK---------------------KEKESKISDLEDELNKDDFELkkENLEKEI 563
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1343958102 1391 KRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKK 1448
Cdd:TIGR04523 564 DEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1014-1284 |
1.63e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 59.75 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1014 EEEKSKNLSKLKSKHESMISElEVRLKKEEKTRQdVEKAKRKVEAElvdlQEQQADLQAQ---LAELRAQLAAKEEEL-- 1088
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQE-RLRQEKEEKARE-VERRRKLEEAE----KARQAEMDRQaaiYAEQERMAMERERELer 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1089 --QTTQACLDEESRQRGAALK--RVRDLEALLAELQEDLEAekvARGKAEAARRDLGEELNSLRSELEDSLDTTAAQQEL 1164
Cdd:pfam17380 353 irQEERKRELERIRQEEIAMEisRMRELERLQMERQQKNER---VRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1165 RVKREQEMAMLkkamEDEGRSHETQIQELRQKHGQAVEELREHLEQAKKVRAALEKAKQ----ALEKEAADLSADLRALS 1240
Cdd:pfam17380 430 EEARQREVRRL----EEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRdrkrAEEQRRKILEKELEERK 505
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1343958102 1241 STKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVE 1284
Cdd:pfam17380 506 QAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEME 549
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1104-1326 |
1.82e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1104 AALKRVRDLEALLAELQEDLEAEKVARGKAEAARRDLGEELNSLRSELEDSLDTTAAQQELRVKREQEMAMLKKAMEDEG 1183
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1184 RSHETQIQELR------QKHGQAVEEL----REHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKV 1253
Cdd:COG4942 97 AELEAQKEELAellralYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1343958102 1254 EAQLNDLQlrfseseRQRNELSERVSKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQELLSEETRQ 1326
Cdd:COG4942 177 EALLAELE-------EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
938-1228 |
2.72e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 58.98 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 938 QQEKKE-MEQE-LQLMEAHIVQEEDARQKLQLEKAAVEGRVKKleENLLLSEDQNNKLQKERKLleERLadmssnlaEEE 1015
Cdd:pfam17380 289 QQEKFEkMEQErLRQEKEEKAREVERRRKLEEAEKARQAEMDR--QAAIYAEQERMAMEREREL--ERI--------RQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1016 EKSKNLSKLKSKHESM----ISELE----VRLKKEEKTRQDVEKAKRKVEAElvdlQEQQADLQAQLAELRAQLAAKEEE 1087
Cdd:pfam17380 357 ERKRELERIRQEEIAMeisrMRELErlqmERQQKNERVRQELEAARKVKILE----EERQRKIQQQKVEMEQIRAEQEEA 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1088 LQTTQACLDEE-----------SRQRGAALKRVRDLEALLAELQEDLEAEKVARGKAEAARRDLgeelnsLRSELEDSLD 1156
Cdd:pfam17380 433 RQREVRRLEEEraremervrleEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI------LEKELEERKQ 506
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1343958102 1157 TTAAQQELRVKREQEMAMLKKAMEDEGRSHETQIQELRQKHGQAVEELREHLEQAKKVRAALEkakqALEKE 1228
Cdd:pfam17380 507 AMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE----AMERE 574
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
882-1139 |
3.33e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 58.60 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 882 VEEQAMLEAKLQAEAELYAEAEDmRVRLEAKKQELEEVLHEMEARLEEEEERSISLQQEKKE----MEQELQLMEAHIVQ 957
Cdd:pfam17380 329 MDRQAAIYAEQERMAMERERELE-RIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQknerVRQELEAARKVKIL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 958 EEDARQKLQLEKAAVEGrvkkleenlLLSEDQNNKLQKERKLLEERLADMSSNLAEEEEKSKNLSKLKSKHESMISElEV 1037
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQ---------IRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRK-KL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1038 RLKKEEKTRQDVEKAKRKVEAelvdlQEQQADLQAQLAELRAQlAAKEEELQTTQACLDEESRQRGAALKRVRDLE-ALL 1116
Cdd:pfam17380 478 ELEKEKRDRKRAEEQRRKILE-----KELEERKQAMIEEERKR-KLLEKEMEERQKAIYEEERRREAEEERRKQQEmEER 551
|
250 260
....*....|....*....|...
gi 1343958102 1117 AELQEDLEAEKVARGKAEAARRD 1139
Cdd:pfam17380 552 RRIQEQMRKATEERSRLEAMERE 574
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1038-1260 |
3.40e-08 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 58.55 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1038 RLKKEEKTRQDVEKAKRKVEAELVDLQEQ-----QADLQA----QLAELRAQLAAKEEELQTTQACLDEESRQRGAALKR 1108
Cdd:COG0497 166 AWRALKKELEELRADEAERARELDLLRFQleeleAAALQPgeeeELEEERRRLSNAEKLREALQEALEALSGGEGGALDL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1109 VRDLEALLAELQEdleaekvargkAEAARRDLGEELNSLRSELEDsldttaAQQELRVKREQemamlkkaME-DEGRSHE 1187
Cdd:COG0497 246 LGQALRALERLAE-----------YDPSLAELAERLESALIELEE------AASELRRYLDS--------LEfDPERLEE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1188 TQ-----IQELRQKHGQAVEELREHLEQAKKVRAALEKAKQ---ALEKEAADLSADLR----ALSSTKQDVEQK-KKKVE 1254
Cdd:COG0497 301 VEerlalLRRLARKYGVTVEELLAYAEELRAELAELENSDErleELEAELAEAEAELLeaaeKLSAARKKAAKKlEKAVT 380
|
....*.
gi 1343958102 1255 AQLNDL 1260
Cdd:COG0497 381 AELADL 386
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1363-1775 |
3.84e-08 |
|
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: 57.77 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1363 SSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVSNL 1442
Cdd:pfam19220 37 EAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1443 EKKQKKFDQMLAEERAVSAKSAEERDRAEAELREKETKVLALMKMLEDKQEALQEAERTVKALRVEMEDlisskddVGKS 1522
Cdd:pfam19220 117 TAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEE-------QAAE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1523 VHDLERAKRGLEAFVEEMKTQMEELEDELQVAEDAKLRLEvnsqalrAQHERELQAreeqgeekrrqllkqvreleaele 1602
Cdd:pfam19220 190 LAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAE-------AQLEEAVEA------------------------ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1603 eerkQRTLASAARKKLEGevknteeqLEAASRGRDEALKQLRKNQGQLKELHRELEegrAAHKEILASAREAERRCKNLE 1682
Cdd:pfam19220 239 ----HRAERASLRMKLEA--------LTARAAATEQLLAEARNQLRDRDEAIRAAE---RRLKEASIERDTLERRLAGLE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1683 AEILQMQEMLAAAERARKQAETERDELSEEVAGGSSGRSLLSDEKRRLEAKISQLEEELEEEQANVETLNERLRksqqlv 1762
Cdd:pfam19220 304 ADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEVERAALEQANRRLK------ 377
|
410
....*....|...
gi 1343958102 1763 dqlgAELTAERAS 1775
Cdd:pfam19220 378 ----EELQRERAE 386
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
846-1090 |
4.46e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 846 QEEEMGQKEEELKAVREAAAKAEADLKDITQKHSQLVEEQAMLEAKLQAEAELYAeaedmrvRLEAKKQELEEVLHEMEA 925
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR-------ALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 926 RLEEEEERSISLQQEKKEMEQELQLMEAH-----IVQEEDARQ---KLQLEKAAVEGRVKKLEEnllLSEDQnNKLQKER 997
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQpplalLLSPEDFLDavrRLQYLKYLAPARREQAEE---LRADL-AELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 998 KLLEERLADMSSNLAEEEEKSKNLSKLKSKHESMISELEVRLKKEektrqdvekakrkvEAELVDLQEQQADLQAQLAEL 1077
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL--------------AAELAELQQEAEELEALIARL 232
|
250
....*....|...
gi 1343958102 1078 RAQLAAKEEELQT 1090
Cdd:COG4942 233 EAEAAAAAERTPA 245
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
868-1223 |
4.58e-08 |
|
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: 57.77 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 868 EADLKDITQKHSQLVEEQAMLEAKLQAEAELYAEAEDMRVRLEAKKQELEEV---LHEMEARLEEEEERSISLQQEKKEM 944
Cdd:pfam19220 37 EAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELvarLAKLEAALREAEAAKEELRIELRDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 945 EQELQLMEAHIVQEEDARQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLLEE-------RLADMSSNLAEEEEK 1017
Cdd:pfam19220 117 TAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQenrrlqaLSEEQAAELAELTRR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1018 SKNLSKLKSKHESMISELEVRLKKEEKTRQdveKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQACLDE 1097
Cdd:pfam19220 197 LAELETQLDATRARLRALEGQLAAEQAERE---RAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRD 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1098 --------ESRQRGAALKRVRdLEALLAELQEDLEAEKVARGKAEAARRDLGEELNSLRSELEDSlDTTAAQQELRV-KR 1168
Cdd:pfam19220 274 rdeairaaERRLKEASIERDT-LERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAK-DAALERAEERIaSL 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1343958102 1169 EQEMAMLKKAMEDEgrshetqiqelRQKHGQAVEELREHLEQAKKVRA----ALEKAKQ 1223
Cdd:pfam19220 352 SDRIAELTKRFEVE-----------RAALEQANRRLKEELQRERAERAlaqgALEIARE 399
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1173-1633 |
4.58e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1173 AMLKKAMEDEGRSHETQIQELRQKHGQAVEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKK 1252
Cdd:COG4717 45 AMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1253 VEAQlnDLQLRFSESERQRNELSERVSKMTVELDSVTGLLNEAEgrniKLSKEASSISSQLQDAQELLSEETRQKLN-LS 1331
Cdd:COG4717 125 LQLL--PLYQELEALEAELAELPERLEELEERLEELRELEEELE----ELEAELAELQEELEELLEQLSLATEEELQdLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1332 GRLRQLEEdkgclmeqleeemeAKQAVERQASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGD-----YEE 1406
Cdd:COG4717 199 EELEELQQ--------------RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallalLGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1407 KAAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSAKSAEERDRAEAELREKETKVLALMK 1486
Cdd:COG4717 265 GGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1487 MLEDKQEALQEAERTVKALRVEMEDLISSKDDVGKSVHDLERAKRGLEAFVE--EMKTQMEELEDEL-QVAEDAKLRLEV 1563
Cdd:COG4717 345 RIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEyqELKEELEELEEQLeELLGELEELLEA 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1564 NSQALRAQHERELQAREEQGEEKRRQLLKQVRELEAELEEERKQRTLASAARKKLEGEVKNTEEQLEAAS 1633
Cdd:COG4717 425 LDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAA 494
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
905-1260 |
5.48e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 57.60 E-value: 5.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 905 MRVRLEAKKQELEEVLHEMEARLEEEEERSISLQQEKKEMEQELQLMEAHIvqeedarQKLQLEKAAVEGRVKKLEENLL 984
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRV-------AELKEELRQSREKHEELEEKYK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 985 LSEDQNNKLQKERKLLEERLADMSSNLAEEEEKSKNLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQ 1064
Cdd:pfam07888 105 ELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1065 EQQADLQAQLAELRAQLAAKEEELQTTQACLDEESRQRGAALKRVRDLEALLAELQEDLEAEKVARGKAEAARRDLgEEL 1144
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEEL-SSM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1145 NSLRSELEDSL---------------DTTAAQQELRVKREQEMAMLKKAMEDEGRSHETQIQELRQKHgqavEELREHLE 1209
Cdd:pfam07888 264 AAQRDRTQAELhqarlqaaqltlqlaDASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLE----ERLQEERM 339
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1343958102 1210 QAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDL 1260
Cdd:pfam07888 340 EREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
857-1340 |
6.17e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 58.13 E-value: 6.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 857 LKAVREAAAKAEADLKDITQKHSQLV---------EEQAMLEAKLQAEAELYAEAEDMRVRLEAKKQELEEVLHemearL 927
Cdd:TIGR00606 456 LKFVIKELQQLEGSSDRILELDQELRkaerelskaEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNH-----H 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 928 EEEEERSISLQQEKKEMEQELQLMEAHIVQE--------------EDARQKLQLEKAAVEGRVKKLEENLLLSEDQNNKL 993
Cdd:TIGR00606 531 TTTRTQMEMLTKDKMDKDEQIRKIKSRHSDEltsllgyfpnkkqlEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHI 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 994 QKERKLLEERLADMSSNLAE------EEEKSKNLS------------------------------------------KLK 1025
Cdd:TIGR00606 611 NNELESKEEQLSSYEDKLFDvcgsqdEESDLERLKeeieksskqramlagatavysqfitqltdenqsccpvcqrvfQTE 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1026 SKHESMISELEVRLK----KEEKTRQDVEKAKRKVEAELVDLQEQQADLQ---AQLAELRAQLAAKEEELQTTQACLDEE 1098
Cdd:TIGR00606 691 AELQEFISDLQSKLRlapdKLKSTESELKKKEKRRDEMLGLAPGRQSIIDlkeKEIPELRNKLQKVNRDIQRLKNDIEEQ 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1099 SRQRGAALKRVRDLEALLAE------LQEDLE--AEKVARGKAEAARRDLGEELNSLRSELEDS---LDTTAAQQELRVK 1167
Cdd:TIGR00606 771 ETLLGTIMPEEESAKVCLTDvtimerFQMELKdvERKIAQQAAKLQGSDLDRTVQQVNQEKQEKqheLDTVVSKIELNRK 850
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1168 ---REQEMAMLKKAMEDEGRSHETQIQELRQKHGQAVEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQ 1244
Cdd:TIGR00606 851 liqDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS 930
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1245 DVEQKKKKVEAQLNDLQLRFSESERQRNELSERVS--------KMTVELDSVTGLLNEAEGRNIKLSKE----ASSISSQ 1312
Cdd:TIGR00606 931 SKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQdgkddylkQKETELNTVNAQLEECEKHQEKINEDmrlmRQDIDTQ 1010
|
570 580
....*....|....*....|....*...
gi 1343958102 1313 LQDAQELLSEETRQKLNlsGRLRQLEED 1340
Cdd:TIGR00606 1011 KIQERWLQDNLTLRKRE--NELKEVEEE 1036
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1493-1926 |
7.38e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 7.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1493 EALQEAERTVKALRVEMEDLISSKDDVgksvHDLERAKRGLEAFVEEMKTQMEELEDELQVAED----AKLRLEVNSQAL 1568
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEEL----EELEEELEELEAELEELREELEKLEKLLQLLPLyqelEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1569 RAQHERELQAREEQGEEKRRQLLKQVRELEAELEEERKQRTLAsaarkklegevknTEEQLEAASRGRDEALKQLRKNQG 1648
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA-------------TEEELQDLAEELEELQQRLAELEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1649 QLKELHRELEEGRAAHKEILASAREAERRCKNLEAEILQMQEMLAAAERARKQAETERDELSEEVAGGSSGRSLLSDEKR 1728
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1729 RLEAKISQLEEELEEEQANVETLNERLRKSQQLVDQLGAELTAERAS---SQNREGSRLQLEKQTRDLKAKLQDVESQAR 1805
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLellDRIEELQELLREAEELEEELQLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1806 SKLKSSVAALEAKLREAEEQLEvesrerqasakNLRQKEKKLKDLTAQMEDERKQAQDYKDQMEKSS--ARMKQLKHQLE 1883
Cdd:COG4717 374 ALLAEAGVEDEEELRAALEQAE-----------EYQELKEELEELEEQLEELLGELEELLEALDEEEleEELEELEEELE 442
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1343958102 1884 EAEEEAQRVAAARRKLQRELdEALEANDALSR---EVSSLRSKLRR 1926
Cdd:COG4717 443 ELEEELEELREELAELEAEL-EQLEEDGELAEllqELEELKAELRE 487
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
933-1293 |
8.47e-08 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 57.52 E-value: 8.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 933 RSISLQQEKKEMEQELQLMEAHIVQEEDARQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLLEERLADMSSNLA 1012
Cdd:pfam10174 339 RAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1013 EEEEKSKNLSKLKSKHESMISELEVRLKKEEKT----RQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEE-- 1086
Cdd:pfam10174 419 GLKERVKSLQTDSSNTDTALTTLEEALSEKERIierlKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESsl 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1087 -ELQTTQACLDEESRQRGAALK--------RVRDLEALLAELQEDLEAEKVARGKAEAARR--DLGEELNSLRSEledsl 1155
Cdd:pfam10174 499 iDLKEHASSLASSGLKKDSKLKsleiaveqKKEECSKLENQLKKAHNAEEAVRTNPEINDRirLLEQEVARYKEE----- 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1156 dTTAAQQELrvkrEQEMAMLKKaMEDEGRSHETQIQELRQKhgqaveELREHLEQAKKVrAALEKAKQALEKEAADLSAD 1235
Cdd:pfam10174 574 -SGKAQAEV----ERLLGILRE-VENEKNDKDKKIAELESL------TLRQMKEQNKKV-ANIKHGQQEMKKKGAQLLEE 640
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1343958102 1236 LRALSSTKQDVEQKKkkveaQLNDLQLRFSESERQRNELSERVSKMTVELDSVTGLLN 1293
Cdd:pfam10174 641 ARRREDNLADNSQQL-----QLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLT 693
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1689-1942 |
8.61e-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: 56.70 E-value: 8.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1689 QEMLAAAERARKQAETERDELSEEVAGGSSGRSLLSDEKRRLEAKISQLEEELEEEQANVETLNERLRKSQQLVDQLGAE 1768
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1769 LTAERASSQNREGSRLQLEKQTRdLKAKLQDVESQARSKLKSSVAALEAKLREAEEQLEVESRERQASAKNLRQKEKKLK 1848
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPP-LALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1849 DLTAQMEDERKQAQDYKDQMEKssaRMKQLKHQLEEAEEEAQRVAAARRKLQRELDEALEANDALSREVSSLRSKLRRGG 1928
Cdd:COG4942 178 ALLAELEEERAALEALKAERQK---LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
250 260
....*....|....*....|.
gi 1343958102 1929 ------GEVLTS-GQRVGGGG 1942
Cdd:COG4942 255 lpwpvsGRVVRRfGERDGGGG 275
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1392-1924 |
9.62e-08 |
|
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: 57.29 E-value: 9.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1392 RLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLDSQRqLVSNLEKKQKKFDQMLAEeravsakSAEERDRAE 1471
Cdd:TIGR00618 98 RSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKT-FTRVVLLPQGEFAQFLKA-------KSKEKKELL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1472 AELREKETKVLALMKMLEDKQEALQEAERTVKALRVEMEDLISSKDDVGKSVHDLERAKRGLEAFVEEMKTQMEELEDEL 1551
Cdd:TIGR00618 170 MNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1552 QVAEdAKLRLEVNSQALRAQhERELQAREEQGEEKRRQLlkQVRELEAELEEERKQRTLASAARKKLEGEVKNTEEQLEA 1631
Cdd:TIGR00618 250 EAQE-EQLKKQQLLKQLRAR-IEELRAQEAVLEETQERI--NRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAK 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1632 ASRGRDEALKQ---LRKNQGQLKELHRELEEGRAAHkEILASAREAERRCKNLEAEILQMQEMLAAAERARKQAETERDE 1708
Cdd:TIGR00618 326 LLMKRAAHVKQqssIEEQRRLLQTLHSQEIHIRDAH-EVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDI 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1709 LSEEVAGGS---SGRSLLSDEKRRLEAKISQLEEELEEEQANVETLNERLRKSQQLVDQLGAELTAERASSQNREGSRLQ 1785
Cdd:TIGR00618 405 LQREQATIDtrtSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQ 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1786 LEKQTRDLKAKLQDVESQARsKLKSSVAALEAKLREAEEqLEVESRERQASAKNLRQKEKKLKDLTAQMEDERKQAQDYK 1865
Cdd:TIGR00618 485 ETRKKAVVLARLLELQEEPC-PLCGSCIHPNPARQDIDN-PGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLK 562
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1343958102 1866 DQMEKSSARMKQLKHQLEEAEEEAQRVAAARRKLQRELDEALEANDALSREVSSLRSKL 1924
Cdd:TIGR00618 563 EQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKL 621
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1368-1584 |
1.34e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.99 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1368 QLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVSN-LEKKQ 1446
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1447 KKFDQMLAEERAVSAKSAEE-RDRAEAelreketkvlaLMKMLEDKQEALQEAERTVKALRVEMEDLISSKDDVGKSVHD 1525
Cdd:COG3883 97 RSGGSVSYLDVLLGSESFSDfLDRLSA-----------LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1343958102 1526 LERAKRGLEAFVEEMKTQMEELEDELQVAEDAKLRLEVNSQALRAQHERELQAREEQGE 1584
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
842-1228 |
1.69e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 842 QVTRQEEEMGQKEEELKAVREAAAKAEADLKDITQKHSQLVEEQAMLEaKLQAEAELYAEAEDMRVRLEAKKQELEEvLH 921
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-KLLQLLPLYQELEALEAELAELPERLEE-LE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 922 EMEARLEEEEERSISLQQEKKEMEQEL-QLMEAHIVQEEDARQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLL 1000
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1001 EERLADmssnLAEEEEKSKN--------------------------------------------LSKLKSKHESMISELE 1036
Cdd:COG4717 233 ENELEA----AALEERLKEArlllliaaallallglggsllsliltiagvlflvlgllallfllLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1037 VRLKKEEKTRQDVEKAKRKVE----------AELVDLQEQQADLQAQLAELRAQLAAKEEE------LQTTQACLDEESR 1100
Cdd:COG4717 309 ALPALEELEEEELEELLAALGlppdlspeelLELLDRIEELQELLREAEELEEELQLEELEqeiaalLAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1101 QRGAALKRVRDLEALLAELQEDLEAEkvARGKAEAARRDLGEELNSLRSELEDSLDTTAAQQELRVKREQEMAMLKKAME 1180
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEEL--LGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1343958102 1181 DEGRshetqIQELRQKHGQAVEELREHLEQAKKVRAA---LEKAKQALEKE 1228
Cdd:COG4717 467 EDGE-----LAELLQELEELKAELRELAEEWAALKLAlelLEEAREEYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1302-1531 |
1.75e-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: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1302 LSKEASSISSQLQDAQELLSEETRQKLNLSGRLRQLEEDKGCLMEQLEEEMEAKQAVERQASSLSVQLSDLKKRLEELSA 1381
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1382 AVELLEEGKKRLQRELEaasgdyEEKAAAYDKLEKSRGRL---QQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERA 1458
Cdd:COG4942 91 EIAELRAELEAQKEELA------ELLRALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1343958102 1459 VSAKSAEERDRAEAELREKETKVLALMKMLEDKQEALQEAERTVKALRVEMEDLISSKDDVGKSVHDLERAKR 1531
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1624-1877 |
2.27e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.18 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1624 NTEEQLEAASRGRDEALKQLRKNQGQLKELHRELEEGRAAHKEILASAREaerrcKNLEAEILQMQEMLAAAERARKQAE 1703
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEA-----KLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1704 TERDELSEEVAGGSSGRSLLSDekrrleakisqleeeleeeqanvetlNERLRKSQQLVDQLGAELTAERASSQNREGSR 1783
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQ--------------------------SPVIQQLRAQLAELEAELAELSARYTPNHPDV 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1784 LQLEKQTRDLKAKLQDVESQARSKLKSSVAALEAKLREAEEQLEvesrERQASAKNLRQKEKKLKDLTAQMEDERKQAQD 1863
Cdd:COG3206 294 IALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLA----QLEARLAELPELEAELRRLEREVEVARELYES 369
|
250
....*....|....
gi 1343958102 1864 YKDQMEKSSARMKQ 1877
Cdd:COG3206 370 LLQRLEEARLAEAL 383
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1140-1873 |
2.43e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 56.39 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1140 LGEELNSLRSeLEDSLDTT----AAQQELRVKREQEMAMLKKAMEDEGRSHETQIQELRQKHGQAVEELREHLEQAKKVR 1215
Cdd:pfam12128 246 LQQEFNTLES-AELRLSHLhfgyKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSEL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1216 AALEKAKQALEKEAAD-LSADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVELDSvtGLLNE 1294
Cdd:pfam12128 325 EALEDQHGAFLDADIEtAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKD--KLAKI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1295 AEGRNiKLSKEASSISSQLQdaQELLSEETRQKLNLSGRLRQLEEDKGCLMEQLEEEMEAKQAVERQASSLSvqlsdlkk 1374
Cdd:pfam12128 403 REARD-RQLAVAEDDLQALE--SELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDE-------- 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1375 RLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLDSQR-QLVSNLEKKQKKFDQML 1453
Cdd:pfam12128 472 RIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAgTLLHFLRKEAPDWEQSI 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1454 AEeraVSAKSAEERDRAEAELREKETKVLALMKMLEDKQEALQEAERtvkalrVEMEDLISSKDDVGKSVHDLERAK-RG 1532
Cdd:pfam12128 552 GK---VISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEW------AASEEELRERLDKAEEALQSAREKqAA 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1533 LEAFVEEMKTQMEELEDELQVAEDAKLRLEVNSQALRAQHERELQAREEQGEEKRRQLLKQVRELeaeleeerkqrtlas 1612
Cdd:pfam12128 623 AEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSL--------------- 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1613 aarkklEGEVKNTEEQLEAASRGRDEalkQLRKNQGQLKELHRELEEGRAAHKEILASAREAERrcKNLEAEILQMQEML 1692
Cdd:pfam12128 688 ------EAQLKQLDKKHQAWLEEQKE---QKREARTEKQAYWQVVEGALDAQLALLKAAIAARR--SGAKAELKALETWY 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1693 AAAERARKQAETERDELSEEVAggSSGRSLLSDEKRRLEAKISQLEEELEEEQANvETLNERLRKSQQLVDQLGAELTAE 1772
Cdd:pfam12128 757 KRDLASLGVDPDVIAKLKREIR--TLERKIERIAVRRQEVLRYFDWYQETWLQRR-PRLATQLSNIERAISELQQQLARL 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1773 RASSQNRegsRLQLEKQtRDLKAKLQDVESQARSKLKSSVAALeAKLREAE--EQLEVESRERQASAKNLRQKEKKLkdl 1850
Cdd:pfam12128 834 IADTKLR---RAKLEME-RKASEKQQVRLSENLRGLRCEMSKL-ATLKEDAnsEQAQGSIGERLAQLEDLKLKRDYL--- 905
|
730 740
....*....|....*....|...
gi 1343958102 1851 taqMEDERKQAQDYKDQMEKSSA 1873
Cdd:pfam12128 906 ---SESVKKYVEHFKNVIADHSG 925
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1638-1926 |
2.85e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1638 EALKQLRKNQGQLKELHRELEEGRAAhKEILASAREAERRCKNLEAEILQMQEMLAAAERARkqAETERDELSEEVAGgs 1717
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQ-IELLEPIRELAERYAAARERLAELEYLRAALRLWF--AQRRLELLEAELEE-- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1718 sgrslLSDEKRRLEAKISQLEEELEEEQANVETLNERLRKSQ-QLVDQLGAELTAERASSQNREGSRLQLEKQTRDLKAK 1796
Cdd:COG4913 300 -----LRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLP 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1797 LQDvesqarsklksSVAALEAKLREAEEQLEVESRERQASAKNLRQKEKKLKDLTAQmederkqaqdykdqmekssarmk 1876
Cdd:COG4913 375 LPA-----------SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE----------------------- 420
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1343958102 1877 qlkhqleeaeeeaqrvaaaRRKLQRELdEALEAND-ALSREVSSLRSKLRR 1926
Cdd:COG4913 421 -------------------LRELEAEI-ASLERRKsNIPARLLALRDALAE 451
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1360-1825 |
3.22e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1360 RQASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELEAAsgdyeEKAAAYDKLEKSRGRLQQELEDVLMDLDSqrqlv 1439
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAELPERLEE----- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1440 snLEKKQKKFDQMLAEERAVSAKSAEERDRAEAELREKETKVLALMKMLEDKQEALQEA----ERTVKALRVEMEDLISS 1515
Cdd:COG4717 151 --LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRlaelEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1516 KDDVGKSVHDLERAKR---------GLEAFVEEMKTQMEELEDELQVAEDAKLRLEVNSQALRAQHERELQAREEQGEEK 1586
Cdd:COG4717 229 LEQLENELEAAALEERlkearllllIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1587 RRQLLKQVRelEAELEEERKQRTLASAARKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQgQLKELHRELEEGRAAHKE 1666
Cdd:COG4717 309 ALPALEELE--EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE-LEQEIAALLAEAGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1667 ILASAREAERRCKNLEAEILQMQEMLAAAERARKQAETERDElseevaggssgrsllsdekRRLEAKISQLEEELEEEQA 1746
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-------------------EELEEELEELEEELEELEE 446
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1343958102 1747 NVETLNERLRKSQQLVDQLGAELTAErassqnregsrlQLEKQTRDLKAKLQDVEsQARSKLKSSVAALEAKLREAEEQ 1825
Cdd:COG4717 447 ELEELREELAELEAELEQLEEDGELA------------ELLQELEELKAELRELA-EEWAALKLALELLEEAREEYREE 512
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1021-1234 |
3.47e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1021 LSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKV---EAELVDLQEQQADLQAQLAELRAQLAAKEEELqttqaclde 1097
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYnelQAELEALQAEIDKLQAEIAEAEAEIEERREEL--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1098 esRQRGAALKR----VRDLEALL-AELQEDLEAEKVARGKAEAARRDLGEELNSLRSELEDSLDTTAAQQELRVKREQEM 1172
Cdd:COG3883 89 --GERARALYRsggsVSYLDVLLgSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1343958102 1173 AMLKKAMEDEGRSHETQIQELRQKHGQAVEELREHLEQAKKVRAALEKAKQALEKEAADLSA 1234
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1438-1906 |
3.48e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1438 LVSNLEKKQKKFDQMLAEERAVSAKSAEERDRAEAELREKETKVLALMKMLEDKQEALQEAERTVKALRVEMEDLisskd 1517
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL----- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1518 DVGKSVHDLERAKRGLEAFVEEMKTQMEELEDELQVAEDAKLRLEvnsqALRAQHERELQAREEQGEEKRRQLLKQVREL 1597
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE----ELEAELAELQEELEELLEQLSLATEEELQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1598 EAELEEERKQRTLASAARKKLEGEVKNTEEQLEAASRG--RDEALKQLRKNQGQLKelhreleeGRAAHKEILASAREAE 1675
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENEleAAALEERLKEARLLLL--------IAAALLALLGLGGSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1676 RRCKNLEAEILQMQEMLAAAERARKQAETERDELSEEVAGGSSGRSL----LSDEKRRLEAKISQLEEELEEEQANVETL 1751
Cdd:COG4717 270 SLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELeeeeLEELLAALGLPPDLSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1752 NERLRKSQQL-----VDQLGAELTA--ERASSQNREG--SRLQLEKQTRDLKAKLQDVESQARSKLKSSVAAL----EAK 1818
Cdd:COG4717 350 QELLREAEELeeelqLEELEQEIAAllAEAGVEDEEElrAALEQAEEYQELKEELEELEEQLEELLGELEELLealdEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1819 LREAEEQLEVESRERQASAKNLRQKEKKLKDLTAQMEDERKQAQDYKDQmekssarmKQLKHQLEEAEEEAQRVAAARRK 1898
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQEL--------EELKAELRELAEEWAALKLALEL 501
|
....*...
gi 1343958102 1899 LQRELDEA 1906
Cdd:COG4717 502 LEEAREEY 509
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
858-1305 |
4.55e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 858 KAVREAAAKAEADLKDITQKHSQLVEEQAMLEAKlqaEAELYAEAEDMRVRLEAKKQELEEVLHEMEARLEEEEERSISL 937
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK---KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKK 1559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 938 QQEKKEMEQELQLMEAHIVQEEDARQKLQLEKAAVEGRVKKLEEnlllseDQNNKLQKERKLLEERLADMSSNLAEEEEK 1017
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE------EKKMKAEEAKKAEEAKIKAEELKKAEEEKK 1633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1018 SKNLSKLKSKHESMISElEVRlKKEEKTRQDVEKAKRKVE-----AELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQ 1092
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAE-ELK-KAEEENKIKAAEEAKKAEedkkkAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1093 acldEESRQRGAALKRVRDLEALLAElQEDLEAEKVARgKAEAARRDLGE--ELNSLRSELEDSLDTTAAQQELRVKREQ 1170
Cdd:PTZ00121 1712 ----AEEKKKAEELKKAEEENKIKAE-EAKKEAEEDKK-KAEEAKKDEEEkkKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1171 EMAMLKKAMEDEGRSHETQ-----IQELRQKHGQAVEELREHLEQAKKVRA-----------ALEKAKQALEKEA----- 1229
Cdd:PTZ00121 1786 DEEDEKRRMEVDKKIKDIFdnfanIIEGGKEGNLVINDSKEMEDSAIKEVAdsknmqleeadAFEKHKFNKNNENgedgn 1865
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1343958102 1230 --ADLSADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVElDSVTGLLNEAEGRNIKLSKE 1305
Cdd:PTZ00121 1866 keADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKD-EYIKRDAEETREEIIKISKK 1942
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1032-1173 |
4.65e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.00 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1032 ISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQACLDEESRQR--------- 1102
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyealqkei 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1343958102 1103 GAALKRVRDLEALLAELQEDLEAEKVARGKAEAARRDLGEELNSLRSELEDSLDTTAAQQELRVKREQEMA 1173
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
857-1407 |
4.82e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.11 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 857 LKAVREAAAKAEADLKDITQKHSQLVEEQAMLEAKLQAEAELYAEAEDMRvrlEAKKQELEEVLHEMEARLEEEEERSIS 936
Cdd:pfam05483 284 LKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEK---EAQMEELNKAKAAHSFVVTEFEATTCS 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 937 LQQEKKEMEQELqlmeahivqeEDARQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLLEERladmSSNLAEEEE 1016
Cdd:pfam05483 361 LEELLRTEQQRL----------EKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAED----EKLLDEKKQ 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1017 KSKNLSKLKSKHESMISELEVRlkkeektrqdvEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQACLD 1096
Cdd:pfam05483 427 FEKIAEELKGKEQELIFLLQAR-----------EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCD 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1097 EESRQRGAALKRVRDLEALLAELQEDLEAEKVARGKAEAARRDLGEELNSLRSELEdsldttAAQQELRVKREQEMAMLK 1176
Cdd:pfam05483 496 KLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELE------SVREEFIQKGDEVKCKLD 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1177 KAMEDEGRSHETQIQELRQKH--GQAVEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRA----LSSTKQDVEQKK 1250
Cdd:pfam05483 570 KSEENARSIEYEVLKKEKQMKilENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAyeikVNKLELELASAK 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1251 KKVEAQLNDLQLRFSESERQRNELSERVSKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQELLSEETRQKLNL 1330
Cdd:pfam05483 650 QKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGL 729
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1343958102 1331 SGRLRQleedkgclmeqleEEMEAKQAVERQASSLSVQLSDLKKRLeelsaavELLEEGKKRLQRELEAASGDYEEK 1407
Cdd:pfam05483 730 YKNKEQ-------------EQSSAKAALEIELSNIKAELLSLKKQL-------EIEKEEKEKLKMEAKENTAILKDK 786
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1034-1341 |
6.97e-07 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 53.96 E-value: 6.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1034 ELEVRLKKEEKTRQDVEKAKRKVEAELvdlqeqqadlQAQLAELRAQLAAKEEELQTTQACLDEESRQRGAalkrvrdLE 1113
Cdd:pfam03528 5 DLQQRVAELEKENAEFYRLKQQLEAEF----------NQKRAKFKELYLAKEEDLKRQNAVLQEAQVELDA-------LQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1114 ALLAELQEDLE--------AEKVARGKAEAARRDLGEELNSLRSELEDSLDTTAAQQELRVkrEQEMAMLKKAMEdegrS 1185
Cdd:pfam03528 68 NQLALARAEMEnikavatvSENTKQEAIDEVKSQWQEEVASLQAIMKETVREYEVQFHRRL--EQERAQWNQYRE----S 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1186 HETQIQELRQK--HGQAVEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKK-----VEAQLN 1258
Cdd:pfam03528 142 AEREIADLRRRlsEGQEEENLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEASKMKelnhyLEAEKS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1259 ---DLQLRFSESERQRNELSERVSKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQELLSEETRQKLNL--SGR 1333
Cdd:pfam03528 222 crtDLEMYVAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLMRDMQRMESVltSEQ 301
|
....*...
gi 1343958102 1334 LRQLEEDK 1341
Cdd:pfam03528 302 LRQVEEIK 309
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1142-1864 |
7.12e-07 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 54.81 E-value: 7.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1142 EELNSLRSELEDSLDTTAAQQELRVKREQEMAMLKKAMEDEGRSHETQiQELRQKHGQAVEELREHLEQAKKVRAALEKA 1221
Cdd:PRK10246 191 EQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLLTA-QQQQQQSLNWLTRLDELQQEASRRQQALQQA 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1222 KQALEKEAADLSA--------DLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNEL----SERVSKMTVELDSVT 1289
Cdd:PRK10246 270 LAAEEKAQPQLAAlslaqparQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIrhhaAKQSAELQAQQQSLN 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1290 GLLNEAEGRNIKLSKEA---------SSISSQLQDAQELLSEETRQKLNLSGRLRQLEEDkgcLMEQLEEEMEAKQAVER 1360
Cdd:PRK10246 350 TWLAEHDRFRQWNNELAgwraqfsqqTSDREQLRQWQQQLTHAEQKLNALPAITLTLTAD---EVAAALAQHAEQRPLRQ 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1361 QASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLeksrgRLQQELEDVLMDLDSQRQLvs 1440
Cdd:PRK10246 427 RLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADV-----KTICEQEARIKDLEAQRAQ-- 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1441 nLEKKQKKFDQMLAEERAVSAKSAEE-------RDRAEAELREKETKVLALMKMLEDKQEALQEAERTVKALRVEMEDLI 1513
Cdd:PRK10246 500 -LQAGQPCPLCGSTSHPAVEAYQALEpgvnqsrLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALT 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1514 SskddvgksvhdlerAKRGLEAFVEEMKTQMEELEDELQVAEDAKLRLEVNSQALraqherELQAREEQGEEKRRQLLKQ 1593
Cdd:PRK10246 579 Q--------------QWQAVCASLNITLQPQDDIQPWLDAQEEHERQLRLLSQRH------ELQGQIAAHNQQIIQYQQQ 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1594 VRELEAELEEERKQRTLaSAARKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQGQLKELHRELEEGRAAHKE----ILA 1669
Cdd:PRK10246 639 IEQRQQQLLTALAGYAL-TLPQEDEEASWLATRQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSeetvALD 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1670 SAREAERRCKNLEAEI--LQMQEMLAAAERARKQAETERDELSEEVAGGSSG-RSLLSDEKR-RLEAKisqleeeleeeq 1745
Cdd:PRK10246 718 NWRQVHEQCLSLHSQLqtLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFlAALLDEETLtQLEQL------------ 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1746 anVETLNERLRKSQQLVDQlgAELTAERASSQNREGSRLQLEKQTrdLKAKLQDVESQARSKLKSsvaalEAKLREAEEQ 1825
Cdd:PRK10246 786 --KQNLENQRQQAQTLVTQ--TAQALAQHQQHRPDGLDLTVTVEQ--IQQELAQLAQQLRENTTR-----QGEIRQQLKQ 854
|
730 740 750
....*....|....*....|....*....|....*....
gi 1343958102 1826 lEVESRERQASaknlrqkekklkdLTAQMEDERKQAQDY 1864
Cdd:PRK10246 855 -DADNRQQQQA-------------LMQQIAQATQQVEDW 879
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1087-1260 |
7.43e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 52.23 E-value: 7.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1087 ELQTTQACLDEESRQRGAALKRVRDLEALLAELQEDLEAEKVARGKAEAARRDLGEELNSLRSELEdsldttaaqqelrv 1166
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1167 KREQEMAMLKKAMEDEGRSHETQIQELRQkhGQAVEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDV 1246
Cdd:COG1579 77 KYEEQLGNVRNNKEYEALQKEIESLKRRI--SDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
170
....*....|....
gi 1343958102 1247 EQKKKKVEAQLNDL 1260
Cdd:COG1579 155 EAELEELEAEREEL 168
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1046-1708 |
8.90e-07 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 53.99 E-value: 8.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1046 RQDVEKAKRKVEAELVDLQEQQADLQA-QLAELRAqlaakeeelqttqacLDEESRQ-RGAALKRVRDLEALLAELQEDL 1123
Cdd:pfam07111 43 GQGPGRRGRSLELEGSQALSQQAELISrQLQELRR---------------LEEEVRLlRETSLQQKMRLEAQAMELDALA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1124 EAEKVARGKAEAARRDL-GEELnsLRSELEDS-------LDTTAAQQELRVKREQEMAMLKKAMEDEGRshETQIQELRQ 1195
Cdd:pfam07111 108 VAEKAGQAEAEGLRAALaGAEM--VRKNLEEGsqreleeIQRLHQEQLSSLTQAHEEALSSLTSKAEGL--EKSLNSLET 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1196 KHGQAVEELREHLEQAKKVRAALEKAKQALEKEAAdLSADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELS 1275
Cdd:pfam07111 184 KRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVT-LVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1276 ERVSKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQELLSEETRQKLnlSGRLRQLEEDKGCLMEQLEEEMEAK 1355
Cdd:pfam07111 263 ATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKV--FALMVQLKAQDLEHRDSVKQLRGQV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1356 QAVERQASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELeaasgdyeekaaayDKLEKSRGRLQQELEDVLMDLdsq 1435
Cdd:pfam07111 341 AELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMEL--------------SRAQEARRRQQQQTASAEEQL--- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1436 RQLVSNLEKKQKKFDQMLAEERAVSAKSAEERDRAEAELREKETkvlalMKMLEDKQEALQEaertvkaLRVEMEDLISS 1515
Cdd:pfam07111 404 KFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHT-----IKGLMARKVALAQ-------LRQESCPPPPP 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1516 KDDVGKsvhdlerakrgleafveemktqmeELEDELQVAEDAKLRLEVNSQALRAQHERELQAREEQGEEKRRQLLKQVR 1595
Cdd:pfam07111 472 APPVDA------------------------DLSLELEQLREERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQ 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1596 elEAELEEERKQRTLASAArKKLEGEVKNTEEQLEAASRGRDEALKQLR---------------KNQGQLKELHRELEEG 1660
Cdd:pfam07111 528 --QLEQELQRAQESLASVG-QQLEVARQGQQESTEEAASLRQELTQQQEiygqalqekvaevetRLREQLSDTKRRLNEA 604
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1343958102 1661 RAAHKEILASAREAERRC-----KNLEAEILQMQEMLAAAER-ARKQAETERDE 1708
Cdd:pfam07111 605 RREQAKAVVSLRQIQHRAtqekeRNQELRRLQDEARKEEGQRlARRVQELERDK 658
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1258-1464 |
9.09e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 9.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1258 NDLQLRFSESERQRNELSERVSKMTVELDSVTGLLNEAEGRN--IKLSKEASSISSQLQDAQELLSEETRQKLNLSGRLR 1335
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1336 QLEE--DKGCLMEQLEEEMEAKQAVERQASSLSVQLSDLKKRLEELSAAV--------ELLEEGKKRLQRELEAASGDYE 1405
Cdd:COG3206 244 ALRAqlGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVialraqiaALRAQLQQEAQRILASLEAELE 323
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1343958102 1406 EKAAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSAKSA 1464
Cdd:COG3206 324 ALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1043-1279 |
9.89e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 9.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1043 EKTRQDVEKAKRKVEA-----ELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQAcldeesrqrgaalkRVRDLEALLA 1117
Cdd:COG3206 185 PELRKELEEAEAALEEfrqknGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEA--------------RLAALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1118 elqedLEAEKVARGKAEAARRDLGEELNSLRSELEDSLDTTAAQQELRVKREQEMAMLKKAMEDEGRshetqiqelrqkh 1197
Cdd:COG3206 251 -----SGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ------------- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1198 gQAVEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKkkkvEAQLNDLQLRFSESERQRNELSER 1277
Cdd:COG3206 313 -RILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVA----RELYESLLQRLEEARLAEALTVGN 387
|
..
gi 1343958102 1278 VS 1279
Cdd:COG3206 388 VR 389
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1058-1204 |
1.20e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 52.66 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1058 AELVDL----QEQQADLQAQLAELRAQLAAKEEELQTTQACLDEESRQRGAALKRVRDLEALLAElQEDLEAEkvARGKA 1133
Cdd:PRK09039 63 AELADLlsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDS-EKQVSAR--ALAQV 139
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1343958102 1134 EaarrDLGEELNSLRSEL---EDSLDttaaqqelrvkreqemamlkkAMEDEGRSHETQIQELRQKH----GQAVEEL 1204
Cdd:PRK09039 140 E----LLNQQIAALRRQLaalEAALD---------------------ASEKRDRESQAKIADLGRRLnvalAQRVQEL 192
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1054-1205 |
1.95e-06 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 52.04 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1054 RKVEAELVDLQEQQADLQAQLAELRA---QLAAKEEELQTTQACLDEESRQRGAALKRVRDLEALLAELQEDLEAEKVAR 1130
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAQAQVARLQAeldRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLA 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1343958102 1131 GKAEAARRDLGEELNSLRSELEDSLDTTAAQQELRVKREQEMAMLKKAMEDEGRSHETQIQELRQKHGQAVEELR 1205
Cdd:pfam00529 134 PIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1356-1504 |
2.01e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.08 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1356 QAVERQASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAaydKLEKSRGRLQQ-----ELEDVLM 1430
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA---RIKKYEEQLGNvrnnkEYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1343958102 1431 DLDSQRQLVSNLEKKQKKFDQMLAEERAVSAKSAEERDRAEAELREKETKVLALMKMLEDKQEALQEAERTVKA 1504
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1263-1590 |
2.47e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.82 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1263 RFSESERQRNELSERVSKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQD------AQELLSEETRQKLNLSGRLRQ 1336
Cdd:pfam17380 238 RRKESFNLAEDVTTMTPEYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQekfekmEQERLRQEKEEKAREVERRRK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1337 LEEDKGCLMEQLEEE-----MEAKQAVERQASSLSVQLSDLKK-----RLEELSAAVELLEEGKK----------RLQRE 1396
Cdd:pfam17380 318 LEEAEKARQAEMDRQaaiyaEQERMAMERERELERIRQEERKReleriRQEEIAMEISRMRELERlqmerqqkneRVRQE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1397 LEAASG-----DYEEKAAAYDKLEKSRGRLQQE----LEDVLMDLDSQRQLVSNLEKKQKKFDQM-------LAEERAVS 1460
Cdd:pfam17380 398 LEAARKvkileEERQRKIQQQKVEMEQIRAEQEearqREVRRLEEERAREMERVRLEEQERQQQVerlrqqeEERKRKKL 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1461 AKSAEERDRAEAElrekETKVLALMKMLEDKQEALQEAERTVKALRVEMEDLisskddvGKSVHDLERAKRGleafvEEM 1540
Cdd:pfam17380 478 ELEKEKRDRKRAE----EQRRKILEKELEERKQAMIEEERKRKLLEKEMEER-------QKAIYEEERRREA-----EEE 541
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1541 KTQMEELEDELQVAEDAKLRLEVNSQALRAQHERELQAREEQGEEKRRQL 1590
Cdd:pfam17380 542 RRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEY 591
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1471-1905 |
2.63e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.80 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1471 EAELREKETKVLALMKMLEDKQEALQEAERTVKALRVEMEDLISSKDDVGK----SVHDLERAKRGLEAFVEEMKTQMEE 1546
Cdd:pfam05483 98 EAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKennaTRHLCNLLKETCARSAEKTKKYEYE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1547 LEDELQVAED----------AKLRLEVNSQALRAQHERELQAREEQGEEKRRQLLKQVRELEAELEEERKQRTLASAARK 1616
Cdd:pfam05483 178 REETRQVYMDlnnniekmilAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMK 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1617 KLE---GEVKNTEEQLEAASRGRDEALKQLRKNQGQLKelhRELEEGRAAHKEILASAREAERRCKNLEAEILQM-QEML 1692
Cdd:pfam05483 258 DLTfllEESRDKANQLEEKTKLQDENLKELIEKKDHLT---KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLtEEKE 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1693 AAAERARKQAETERDELSEEVAGGSSGRSLLSDEKRRLEAKISQLEEELEEEQANVETLNERLRKSQQLVDQLgAELTAE 1772
Cdd:pfam05483 335 AQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVEL-EELKKI 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1773 RASSQNREGSRLQLEKQTRDLKAKLQDVES--QARSK-----------LKSSVAALEAKLREAEEQLEVE---SRERQAS 1836
Cdd:pfam05483 414 LAEDEKLLDEKKQFEKIAEELKGKEQELIFllQAREKeihdleiqltaIKTSEEHYLKEVEDLKTELEKEklkNIELTAH 493
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1837 AKNLRQKEKKLKDLTAQMEDERKQAQDYKDQMEKSSARM-KQLKHQLEEAEEEAQRVAAARRKLQRELDE 1905
Cdd:pfam05483 494 CDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMlKQIENLEEKEMNLRDELESVREEFIQKGDE 563
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
937-1083 |
3.01e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 937 LQQEKKEMEQELQLMEAHIVQEEDARQKLQLEKAAVEGRVKKLEENLllsedQNNKLQKERKLLEERLADMSSNLAEEEE 1016
Cdd:COG1579 36 LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL-----GNVRNNKEYEALQKEIESLKRRISDLED 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1343958102 1017 KSKNLSKLKSKHESMISELEVRLKKEEKtrqDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAA 1083
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEA---ELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
937-1226 |
3.31e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.33 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 937 LQQEKKEMEQELQLMEAHIVQEEDARQKLQLEK---AAVEGRVKKLEENLLLSEDQNNKLQKERKLLEERLADMSSNLAE 1013
Cdd:TIGR04523 372 IEKLKKENQSYKQEIKNLESQINDLESKIQNQEklnQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSV 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1014 EEEKSKNLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELR---AQLAAKEEELQT 1090
Cdd:TIGR04523 452 KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTkkiSSLKEKIEKLES 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1091 TQACLDEEsrqrgaalkrVRDLEALLAELQEDLEAEKVargkaEAARRDLGEELNSLRSELEDSLDTTAAQQELRVKREQ 1170
Cdd:TIGR04523 532 EKKEKESK----------ISDLEDELNKDDFELKKENL-----EKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK 596
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1343958102 1171 EMAMLKKAMEdegrSHETQIQELRQKHGQAVEELREHLEQAKKVRAALEKAKQALE 1226
Cdd:TIGR04523 597 EKKDLIKEIE----EKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVK 648
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
915-1498 |
3.31e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 52.13 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 915 ELEEVLHEMEARLEEEEERSISLQQEKKEMEQelqlmeahiVQEEDARQK-LQLEKAAVEGRVKKLEENLLLSEDQNNKL 993
Cdd:pfam10174 189 EAEMQLGHLEVLLDQKEKENIHLREELHRRNQ---------LQPDPAKTKaLQTVIEMKDTKISSLERNIRDLEDEVQML 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 994 QKERKLleerladmssNLAEEEEKSKNLSKLKSKHESMISelevrlkKEEKTRQDVEKAkrkvEAELVDLQ-------EQ 1066
Cdd:pfam10174 260 KTNGLL----------HTEDREEEIKQMEVYKSHSKFMKN-------KIDQLKQELSKK----ESELLALQtkletltNQ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1067 QADLQAQLAELRAQLAAKEEELQTTQACLDeesrqrgAALKRVRDLEALLAELQEDLeaekvargkaeaarRDLGEELNS 1146
Cdd:pfam10174 319 NSDCKQHIEVLKESLTAKEQRAAILQTEVD-------ALRLRLEEKESFLNKKTKQL--------------QDLTEEKST 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1147 LRSELEDSLDTtaaqqeLRVKREQEMAMLKK--AMEDEGRSHETQIQELRQK----------HGQAVEELREHLEQAKKV 1214
Cdd:pfam10174 378 LAGEIRDLKDM------LDVKERKINVLQKKieNLQEQLRDKDKQLAGLKERvkslqtdssnTDTALTTLEEALSEKERI 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1215 RAALEKAKQALEKEAADLSADLRalsstkqdveQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVELDSVTGLLNE 1294
Cdd:pfam10174 452 IERLKEQREREDRERLEELESLK----------KENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKS 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1295 AEGRNIKLSKEASSISSQLQDAQElLSEETRQKLNLSGRLRQLEEDkgcLMEQLEEEMEAKQAVERQASSL---SVQLSD 1371
Cdd:pfam10174 522 LEIAVEQKKEECSKLENQLKKAHN-AEEAVRTNPEINDRIRLLEQE---VARYKEESGKAQAEVERLLGILrevENEKND 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1372 LKKRLEELSAAVelLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRlqqelEDVLMDLDSQRQ---LVSNLEKKQKK 1448
Cdd:pfam10174 598 KDKKIAELESLT--LRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRR-----EDNLADNSQQLQleeLMGALEKTRQE 670
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1449 FDQMLAEERAVSaKSAEERDRAEAELREKETKvlALMKMLEDKQEALQEA 1498
Cdd:pfam10174 671 LDATKARLSSTQ-QSLAEKDGHLTNLRAERRK--QLEEILEMKQEALLAA 717
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
993-1184 |
3.88e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 51.63 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 993 LQKERKLLEErlADMSSNLAEEEEKSKNLSKLKSKHESMISElevRLKKEEKTRQDVEKAKRKVEaELVDLQEQQADLQA 1072
Cdd:PRK12705 25 LKKRQRLAKE--AERILQEAQKEAEEKLEAALLEAKELLLRE---RNQQRQEARREREELQREEE-RLVQKEEQLDARAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1073 QLAELRAQLAAKEEELQTTQACLDEESRQRGAALKRVRDLEA------LLAELQEDLEAEKVARGKAEAARRDLGEE--- 1143
Cdd:PRK12705 99 KLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPeqarklLLKLLDAELEEEKAQRVKKIEEEADLEAErka 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1343958102 1144 LNSLRSELEDSLDTTAAQQELRVKREQEMAMLKKAMEDEGR 1184
Cdd:PRK12705 179 QNILAQAMQRIASETASDLSVSVVPIPSDAMKGRIIGREGR 219
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1679-1923 |
4.43e-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: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1679 KNLEAEILQMQEMLAAAERARKQAETERdelseevaggssgrsllsdEKRRLEAKISQLEEELEEEQANVETLNE----- 1753
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAR-------------------EQIELLEPIRELAERYAAARERLAELEYlraal 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1754 RLRKSQQLVDQLGAELTAERASSQNREGSRLQLEKQTRDLKAKLQDVESQARSKLKSSVAALEAKLREAEEQLEVESRER 1833
Cdd:COG4913 282 RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRR 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1834 QASAKNLRQKEKKLKDLTAQMEDERKQAQDYKDQMEKSSARMKQLKHQLEEAeeeaqrvaaaRRKLQRELDEaleandaL 1913
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAA----------LRDLRRELRE-------L 424
|
250
....*....|
gi 1343958102 1914 SREVSSLRSK 1923
Cdd:COG4913 425 EAEIASLERR 434
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1201-1846 |
5.44e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.83 E-value: 5.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1201 VEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLqlrfseserqrNELSERVSK 1280
Cdd:PRK01156 185 IDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNEL-----------SSLEDMKNR 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1281 MTVELDSVTGLLNEAEGRNIKLSKeassissqlqdaqellSEEtrqklnlsgRLRQLEEDKgclmeqleeeMEAKQAVER 1360
Cdd:PRK01156 254 YESEIKTAESDLSMELEKNNYYKE----------------LEE---------RHMKIINDP----------VYKNRNYIN 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1361 QASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQrELEAASGDYEEKAAAYDKLEKSRgrlqQELEDVLMDLDSqrqLVS 1440
Cdd:PRK01156 299 DYFKYKNDIENKKQILSNIDAEINKYHAIIKKLS-VLQKDYNDYIKKKSRYDDLNNQI----LELEGYEMDYNS---YLK 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1441 NLEKKQKKFDQMLAEERAVSAKSAEERDRAEAELREketkvlaLMKMLEDKQEALQEAERTVKALRVEMEDLISSKDDVG 1520
Cdd:PRK01156 371 SIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDA-------IKKELNEINVKLQDISSKVSSLNQRIRALRENLDELS 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1521 KSVHDL---------------ERAKRGLEAFVEE---MKTQMEELEDELQVAEDAKLRLEVNSQALRAQHERELQAREEQ 1582
Cdd:PRK01156 444 RNMEMLngqsvcpvcgttlgeEKSNHIINHYNEKksrLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNK 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1583 GEEKRRQLLKQVRELEAELEEERKQRTLASAARK-KLEG-EVKNTEE----------QLEAASRGRDEALKQLRKNQGQL 1650
Cdd:PRK01156 524 IESARADLEDIKIKINELKDKHDKYEEIKNRYKSlKLEDlDSKRTSWlnalavisliDIETNRSRSNEIKKQLNDLESRL 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1651 KELHRELEEGRAAhkeILASAREAERRCKNLEAEILQMQEMLAAAERARKQAETERDElseevaggSSGRSLLSDEKRRL 1730
Cdd:PRK01156 604 QEIEIGFPDDKSY---IDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQ--------IAEIDSIIPDLKEI 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1731 EAKISQleeeleeeqanvetLNERLRKSQQLVDQLGAELTAERASSQNREGSRLQLEKQTRDLKAKLQDVEsqarsKLKS 1810
Cdd:PRK01156 673 TSRIND--------------IEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMK-----KIKK 733
|
650 660 670
....*....|....*....|....*....|....*.
gi 1343958102 1811 SVAALEaKLREAEEQLEVESRERQASAKNLRQKEKK 1846
Cdd:PRK01156 734 AIGDLK-RLREAFDKSGVPAMIRKSASQAMTSLTRK 768
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1187-1424 |
7.65e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 7.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1187 ETQIQELRQKHGQAVEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSE 1266
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1267 SerQRNELSERVSKMTVELDSVTGLLNEAEGrnikLSKEASSISSQLQDAQELLSEETRQKLNLSGRLRQLEEDKgclme 1346
Cdd:COG3883 95 L--YRSGGSVSYLDVLLGSESFSDFLDRLSA----LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK----- 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1343958102 1347 qlEEEMEAKQAVERQASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQE 1424
Cdd:COG3883 164 --AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1435-1798 |
8.12e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.89 E-value: 8.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1435 QRQLVSNLEKKQKKFDQMlaeeravsaksAEERDRAEAELREKEtkvLALMKMLEDKQEALQEAERTVKALRVEMEDLIS 1514
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKM-----------EQERLRQEKEEKARE---VERRRKLEEAEKARQAEMDRQAAIYAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1515 SKDdvgksvHDLERAKRgleafvEEMKTQMEELEDELQVAEDAKLRlevnsqalraQHEReLQAREEQGEEKRRQLLKqv 1594
Cdd:pfam17380 345 ERE------RELERIRQ------EERKRELERIRQEEIAMEISRMR----------ELER-LQMERQQKNERVRQELE-- 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1595 releaeleEERKQRTLASAARKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQGQLKELHRELEEGRAAHKEILASaREA 1674
Cdd:pfam17380 400 --------AARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQ-QEE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1675 ERRCKNLEAEILQMQEMLAAAERaRKQAETERDELSEEVAGGSSGRSLLSDE-KRRLEAKISQLEEELEEEQANVETLNE 1753
Cdd:pfam17380 471 ERKRKKLELEKEKRDRKRAEEQR-RKILEKELEERKQAMIEEERKRKLLEKEmEERQKAIYEEERRREAEEERRKQQEME 549
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1343958102 1754 RLRKSQQLVDQLGAELTAERASSQNREGSR--LQLEKQTRDLKAKLQ 1798
Cdd:pfam17380 550 ERRRIQEQMRKATEERSRLEAMEREREMMRqiVESEKARAEYEATTP 596
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1044-1244 |
1.05e-05 |
|
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: 49.84 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1044 KTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQAcldEESRQRGAALKRVRDLEALLAELQEDL 1123
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQA---EEAKAKQAAEAKAKAEAEAERKAKEEA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1124 E--AEKVARGKAEAARRdlgeelnslrseledsldttAAQQELRVKREQEMamLKKAMEDEGRSHETQIQELRQKHGQAV 1201
Cdd:TIGR02794 149 AkqAEEEAKAKAAAEAK--------------------KKAEEAKKKAEAEA--KAKAEAEAKAKAEEAKAKAEAAKAKAA 206
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1343958102 1202 EELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQ 1244
Cdd:TIGR02794 207 AEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQ 249
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
908-1530 |
1.09e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 50.52 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 908 RLEAKKQELEEVLHEMEARLEEEEERSISLQQEKKEMEQELQLMEAHIVQEEDARQKLQlekaavEGRVKKLEENLLLSE 987
Cdd:pfam07111 77 RLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLE------EGSQRELEEIQRLHQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 988 DQNNKLQKERkllEERLADMSSNlAEEEEKSknLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQ 1067
Cdd:pfam07111 151 EQLSSLTQAH---EEALSSLTSK-AEGLEKS--LNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLR 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1068 ADLQAQ-LAELRAQLAAKE-EELQTTQACLDEESRQRGAALK----RVRDLEALLAeLQEDLEAEKVargkaeaarrdlg 1141
Cdd:pfam07111 225 KYVGEQvPPEVHSQTWELErQELLDTMQHLQEDRADLQATVEllqvRVQSLTHMLA-LQEEELTRKI------------- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1142 EELNSLRSELedsldTTAAQQELRVKREQEMAMLKKaMEDEGRSHETQIQELRQKhgqaVEELREHLEQAKKVRAALEka 1221
Cdd:pfam07111 291 QPSDSLEPEF-----PKKCRSLLNRWREKVFALMVQ-LKAQDLEHRDSVKQLRGQ----VAELQEQVTSQSQEQAILQ-- 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1222 kQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQlndlQLRFSESERQRNELSERVSKMTVELDSVTGLLNEAEGRNIK 1301
Cdd:pfam07111 359 -RALQDKAAEVEVERMSAKGLQMELSRAQEARRRQ----QQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPS 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1302 LSKEASSISSQLQDAQELLSeetrQKLNLSgRLRQleedKGCLMEQLEEEMEAKQAVERQasslsvQLSDLKKRLE---E 1378
Cdd:pfam07111 434 LSNRLSYAVRKVHTIKGLMA----RKVALA-QLRQ----ESCPPPPPAPPVDADLSLELE------QLREERNRLDaelQ 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1379 LSAAVELLEEGKKRLQRELEAasgdyEEKAAAYDKLEKSRGRLQQELEDVLMDLDSQRQ-----------LVSNLEKKQK 1447
Cdd:pfam07111 499 LSAHLIQQEVGRAREQGEAER-----QQLSEVAQQLEQELQRAQESLASVGQQLEVARQgqqesteeaasLRQELTQQQE 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1448 KFDQMLAEERA-VSAKSAEERDRAEAELRE-KETKVLALMKMLEDKQEALQEAERTVKALRVEMEDLISSKDDVGKSVHD 1525
Cdd:pfam07111 574 IYGQALQEKVAeVETRLREQLSDTKRRLNEaRREQAKAVVSLRQIQHRATQEKERNQELRRLQDEARKEEGQRLARRVQE 653
|
....*
gi 1343958102 1526 LERAK 1530
Cdd:pfam07111 654 LERDK 658
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1029-1164 |
1.14e-05 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 49.85 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1029 ESMISELEVRLKKE--EKTRQDVEKAKRKVEA---ELVDLQEQ------QADLQAQ---LAELRAQLAAKEEELQTTQAC 1094
Cdd:COG3524 164 EELVNQLSERAREDavRFAEEEVERAEERLRDareALLAFRNRngildpEATAEALlqlIATLEGQLAELEAELAALRSY 243
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1343958102 1095 LDEESRQRGAALKRVRDLEALLAELQEDLeaekvargkaeaARRDLGEELNSLRSELED-SLDTTAAQQEL 1164
Cdd:COG3524 244 LSPNSPQVRQLRRRIAALEKQIAAERARL------------TGASGGDSLASLLAEYERlELEREFAEKAY 302
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1656-1931 |
1.19e-05 |
|
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: 50.45 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1656 ELEEGRAAHKEILASAREAERRCKNLEAEILQMQEMLaaaERARKQAETERDELSE--EVAGgssgrSLLSDEKRRLEAK 1733
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERL---RREREKAERYQALLKEkrEYEG-----YELLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1734 ISQLeeeleeeQANVETLNERLRKSQQLVDQLGAELTA--ERASSQNREGSRLQLEKQTRdLKAKLQDVESQarsklkss 1811
Cdd:TIGR02169 239 KEAI-------ERQLASLEEELEKLTEEISELEKRLEEieQLLEELNKKIKDLGEEEQLR-VKEKIGELEAE-------- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1812 VAALEAKLREAEEQLEVESRERQASAKNLRQKEKKLKDLTAQMEDERKQAQDYKDQMEKSSARMKQLKHQLEEAEEEAQR 1891
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1343958102 1892 VAAARRKLQRELDEALEANDALSREVSSLRSKLRRGGGEV 1931
Cdd:TIGR02169 383 TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL 422
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1038-1255 |
1.98e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.56 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1038 RLKKEEKTRQdvEKAKRKVEAelvdLQEQQAD-LQAQLAELRAQLAAKEEELQTTQACLDEESRQRGAALKRVRDLEALL 1116
Cdd:PRK05035 461 RLEREKAARE--ARHKKAAEA----RAAKDKDaVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1117 AELQEDLEAEK--------VARGKAEAArrdlgeELNSLRSELEDSLDTTAAQQELRVKREQEMAMLKKAMEDEGRSHET 1188
Cdd:PRK05035 535 AEKQAAAAADPkkaavaaaIARAKAKKA------AQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVA 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1189 QIQELR------------QKHGQAVEELREHLEQAKK--VRAALEKAKqalekeaADLSADLRALSSTKQDVEQKKKKVE 1254
Cdd:PRK05035 609 EVDPKKaavaaaiarakaKKAEQQANAEPEEPVDPRKaaVAAAIARAK-------ARKAAQQQANAEPEEAEDPKKAAVA 681
|
.
gi 1343958102 1255 A 1255
Cdd:PRK05035 682 A 682
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
936-1223 |
2.27e-05 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 49.26 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 936 SLQQEKKEMEQEL--QLMEAHIVQEEDARQKLQ-LEKAAVEgrvkKLEENLLLSEDQNNKLQKERKLLEERLADMSSNLA 1012
Cdd:pfam05667 214 AELAAAQEWEEEWnsQGLASRLTPEEYRKRKRTkLLKRIAE----QLRSAALAGTEATSGASRSAQDLAELLSSFSGSST 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1013 EEEEKSKNLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAA-------KE 1085
Cdd:pfam05667 290 TDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKlessikqVE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1086 EELQTTQ---ACLDEESRQRGAALKRVRDLEALLAELQEDLEA--EKVAR--GKAEAARRDLGEELNSLRSEledsldtt 1158
Cdd:pfam05667 370 EELEELKeqnEELEKQYKVKKKTLDLLPDAEENIAKLQALVDAsaQRLVElaGQWEKHRVPLIEEYRALKEA-------- 441
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1343958102 1159 AAQQELRVKREQEmamlkkamedegrshetQIQELRQKHGQAVEELREHLEQAKKVRAALEKAKQ 1223
Cdd:pfam05667 442 KSNKEDESQRKLE-----------------EIKELREKIKEVAEEAKQKEELYKQLVAEYERLPK 489
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1367-1555 |
2.66e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1367 VQLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVSNLeKKQ 1446
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1447 KKFDQMLAEEravsaksaeerDRAEAELREKETKVLALMKMLEDKQEALQEAERTVKALRVEmedlisskddvgksvhdL 1526
Cdd:COG1579 89 KEYEALQKEI-----------ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE-----------------L 140
|
170 180
....*....|....*....|....*....
gi 1343958102 1527 ERAKRGLEAFVEEMKTQMEELEDELQVAE 1555
Cdd:COG1579 141 EEKKAELDEELAELEAELEELEAEREELA 169
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
934-1236 |
2.66e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 49.52 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 934 SISLQQEKKEMEQELQLMEAhiVQEEDARQKLQLEKaaVEGRVKKLEENLLL-------SEDQNNKLQKERKLLEERLAD 1006
Cdd:PLN02939 99 RASMQRDEAIAAIDNEQQTN--SKDGEQLSDFQLED--LVGMIQNAEKNILLlnqarlqALEDLEKILTEKEALQGKINI 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1007 MSSNLAEEEEKSKNLSKLKSKHESMISELEvRLKKEEKTRQDVEKA-KRKVEAELVDLQEQQADLQAQLAELRAQLAake 1085
Cdd:PLN02939 175 LEMRLSETDARIKLAAQEKIHVEILEEQLE-KLRNELLIRGATEGLcVHSLSKELDVLKEENMLLKDDIQFLKAELI--- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1086 eELQTTQACLDEESRQRGAALKRVRDLEALLAELQEDLEA----------EKV---------ARGKAEAARRDLG--EEL 1144
Cdd:PLN02939 251 -EVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKlsplqydcwwEKVenlqdlldrATNQVEKAALVLDqnQDL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1145 NSLRSELEDSLDTTAAQQELRVKREQEMAMLKKAMEDEGRSHEtQIQELRQKHGQAVEELREHLEQAKKvraalEKAKQA 1224
Cdd:PLN02939 330 RDKVDKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDH-EIHSYIQLYQESIKEFQDTLSKLKE-----ESKKRS 403
|
330
....*....|..
gi 1343958102 1225 LEKEAADLSADL 1236
Cdd:PLN02939 404 LEHPADDMPSEF 415
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
935-1447 |
2.81e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.25 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 935 ISLQQEKKEMEQELQLMEAHIVQEEDARQKLQlekaavegrvKKLEENLLLSEDQNNKLqkerklleerladmssnlaee 1014
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEQNKIK----------KQLSEKQKELEQNNKKI--------------------- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1015 EEKSKNLSKLKSKHESMISELEVRLKKEEKTR-QDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQA 1093
Cdd:TIGR04523 284 KELEKQLNQLKSEISDLNNQKEQDWNKELKSElKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1094 CLDEESRQrgaalkrvrdLEALLAELQEDLEAEKvargkaeaarrDLGEELNSLRSELEDsldttaaQQELRVKREQEMa 1173
Cdd:TIGR04523 364 ELEEKQNE----------IEKLKKENQSYKQEIK-----------NLESQINDLESKIQN-------QEKLNQQKDEQI- 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1174 mlkKAMEDEGRSHETQIQELRQKHGQAVEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKV 1253
Cdd:TIGR04523 415 ---KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEL 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1254 EAQLNDLqlrfSESERQRNELSERVSKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQELLSEET--RQKLNLS 1331
Cdd:TIGR04523 492 KSKEKEL----KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENleKEIDEKN 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1332 GRLRQLEEDKgclmeqlEEEMEAKQAVERQASSLSVQLSDLKKRLEELSAAVELLEegkkrlqRELEAASGDYEEKAAAY 1411
Cdd:TIGR04523 568 KEIEELKQTQ-------KSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLE-------KELEKAKKENEKLSSII 633
|
490 500 510
....*....|....*....|....*....|....*.
gi 1343958102 1412 DKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQK 1447
Cdd:TIGR04523 634 KNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIK 669
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
945-1193 |
2.93e-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: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 945 EQELQLMEAHIVQEEDARQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKL--LEERLADM---SSNLAEEEEKSK 1019
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIaeLEAELERLdasSDDLAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1020 NLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQACLDEES 1099
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERI 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1100 RQRGAALKRVRD-LEALLAELQEDLEAEKVARGKAEAARRDLGEELNSLRS----ELEDSLdttaaQQELRVKREQEMAM 1174
Cdd:COG4913 776 DALRARLNRAEEeLERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEdglpEYEERF-----KELLNENSIEFVAD 850
|
250
....*....|....*....
gi 1343958102 1175 LKKAMEDEGRSHETQIQEL 1193
Cdd:COG4913 851 LLSKLRRAIREIKERIDPL 869
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1693-1952 |
3.27e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1693 AAAERARKQAETERDELSEEVAGGSSGRSLLSDEKRRLEAKISQLEEELEEEQANVETLNERLRKSQQLVDQLGAELtAE 1772
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL-GE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1773 RASSQNREGSRLQLEKQTrdLKAK-LQDV--ESQARSKLKSSVAALEAKLREAEEQLEVESRERQASAKNLRQKEKKLKD 1849
Cdd:COG3883 91 RARALYRSGGSVSYLDVL--LGSEsFSDFldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1850 LTAQMEDERKQAQDYKDQMEKSSARMKQLKHQLEEAEEEAQRVAAARRKLQRELDEALEANDALSREVSSLRSKLRRGGG 1929
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
250 260
....*....|....*....|...
gi 1343958102 1930 EVLTSGQRVGGGGSIRNFGGGGS 1952
Cdd:COG3883 249 AGAAGAAGAAAGSAGAAGAAAGA 271
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1062-1443 |
3.59e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.07 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1062 DLQEQQADLQAQLAE-LRAQLAAKEEELQTTQACLDEESRQRGAALKRVRDLEAllaelqedleAEKVARGKAEAARRDL 1140
Cdd:pfam12128 586 DLKRIDVPEWAASEEeLRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASR----------EETFARTALKNARLDL 655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1141 GEELNSLRSELEDSLDTTAAQQELRVKREQEMAMLKKAMEDEGRSHETQIQELRQKHGQAVEELREHLEQAKKvrAALEK 1220
Cdd:pfam12128 656 RRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALD--AQLAL 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1221 AKQALEKEAADLSADLRALSS------TKQDV-EQKKKKVEAQLNDLQLRFSESERQRNE------------------LS 1275
Cdd:pfam12128 734 LKAAIAARRSGAKAELKALETwykrdlASLGVdPDVIAKLKREIRTLERKIERIAVRRQEvlryfdwyqetwlqrrprLA 813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1276 ERVSKMTVEL----DSVTGLLNEAEGRNIKLSKEASSissqLQDAQELLSEETRQKLNLSGRLRQLEEDkgclmeqleee 1351
Cdd:pfam12128 814 TQLSNIERAIselqQQLARLIADTKLRRAKLEMERKA----SEKQQVRLSENLRGLRCEMSKLATLKED----------- 878
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1352 MEAKQAvERQASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELeAASGDYEEKAAAYDKLeksrgrlqQELEDVLMD 1431
Cdd:pfam12128 879 ANSEQA-QGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIADH-SGSGLAETWESLREED--------HYQNDKGIR 948
|
410
....*....|..
gi 1343958102 1432 LDSQRQLVSNLE 1443
Cdd:pfam12128 949 LLDYRKLVPYLE 960
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1641-1909 |
4.55e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.58 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1641 KQLRKNQGQLKELHRELEEGRAAHKEIlasAREAERRCKNLEAEILQMQEMlaaAERARKQAETERDELSEEvagGSSGR 1720
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLRQEKEEK---AREVERRRKLEEAEKARQAEM---DRQAAIYAEQERMAMERE---RELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1721 SLLSDEKRRLEAKISQLEEELEEEQANVETLN-ERLRKSQQLVDQLGAeltAERASSQNREGSRLQLEKQTRDLKAKLQD 1799
Cdd:pfam17380 353 IRQEERKRELERIRQEEIAMEISRMRELERLQmERQQKNERVRQELEA---ARKVKILEEERQRKIQQQKVEMEQIRAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1800 VESQARSklkssVAALEAKLREAEEQLEVESRERQASAKNLRQKEKKLKDLTAQMEDERKQAQDYKDQmekssaRMKQLK 1879
Cdd:pfam17380 430 EEARQRE-----VRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQ------RRKILE 498
|
250 260 270
....*....|....*....|....*....|
gi 1343958102 1880 HQLEEAEEEAQRVAAARRKLQRELDEALEA 1909
Cdd:pfam17380 499 KELEERKQAMIEEERKRKLLEKEMEERQKA 528
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1199-1614 |
4.86e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 48.14 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1199 QAVEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLQlrfSESERQRNELSERV 1278
Cdd:pfam19220 41 RELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAE---AAKEELRIELRDKT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1279 SKmtveLDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQELLSEETRQKLNLSGRLRQLEEDKgclmeqleeemeakQAV 1358
Cdd:pfam19220 118 AQ----AEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQEN--------------RRL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1359 ERQASSLSVQLSDLKKRLEELSAAVELLeegkKRLQRELEAA-SGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLDSqrq 1437
Cdd:pfam19220 180 QALSEEQAAELAELTRRLAELETQLDAT----RARLRALEGQlAAEQAERERAEAQLEEAVEAHRAERASLRMKLEA--- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1438 lvsnLEKKQKKFDQMLAEERAvsaksaeerdraeaELREKETKVLALMKMLEDKQEALQEAERTVKALRVEMEDLISSkd 1517
Cdd:pfam19220 253 ----LTARAAATEQLLAEARN--------------QLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQ-- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1518 dvgksVHDLERAKRGLEAFVEEMKTQMEELEDELQVAEDAKLRLEVNSQALRAQHERELQAREEQGEEKRRQLlkqvrel 1597
Cdd:pfam19220 313 -----FQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEVERAALEQANRRLKEEL------- 380
|
410
....*....|....*..
gi 1343958102 1598 eaelEEERKQRTLASAA 1614
Cdd:pfam19220 381 ----QRERAERALAQGA 393
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1022-1843 |
5.30e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 48.28 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1022 SKLKSKHESMISELEVRLKKEektrqdveKAKRKVEAelvdlqeqqadlqAQLAELRAQLAAKEEELQ----TTQACLDE 1097
Cdd:pfam10174 24 SKLGSSMNSIKTFWSPELKKE--------RALRKEEA-------------ARISVLKEQYRVTQEENQhlqlTIQALQDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1098 esrqrgaaLKRVRDLEALLaelQEDLEAEKVARGKAEAARRDLGEELNSLRSELEdsldttaaqqelrvKREQEMAMLKK 1177
Cdd:pfam10174 83 --------LRAQRDLNQLL---QQDFTTSPVDGEDKFSTPELTEENFRRLQSEHE--------------RQAKELFLLRK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1178 AMEDegrsHETQIQELRQKHGQAVEELREHLE--QAKKVRAALEKAKQALEKEAADLSADLRALSSTkqdVEQKKKKvea 1255
Cdd:pfam10174 138 TLEE----MELRIETQKQTLGARDESIKKLLEmlQSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVL---LDQKEKE--- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1256 qlndlQLRFSESERQRNELSERVSKmTVELDSVTgllneaEGRNIKLSKEASSISSQLQDAQELLSEETRQKLNLSGRLR 1335
Cdd:pfam10174 208 -----NIHLREELHRRNQLQPDPAK-TKALQTVI------EMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIK 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1336 QLEEDKGCLMEQLEEEMEAKQAVERQAS----------SLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYE 1405
Cdd:pfam10174 276 QMEVYKSHSKFMKNKIDQLKQELSKKESellalqtkleTLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1406 EKAAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKK----QKKFDQMLAEERAVSAKSAEERDRAEAELREKETKV 1481
Cdd:pfam10174 356 EKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKinvlQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTD 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1482 LALMKMledkQEALQEAERTVKALRVEmedlisskddvgksvHDLERAKRGLEafVEEMKTQMEELEDELQVaedaklrl 1561
Cdd:pfam10174 436 TALTTL----EEALSEKERIIERLKEQ---------------REREDRERLEE--LESLKKENKDLKEKVSA-------- 486
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1562 evnSQALRAQHERELQAREEQGEEKRRQLLKQVRELEAELEEERKQRTLASaarkKLEGEVKNTEEQlEAASRGRDEALK 1641
Cdd:pfam10174 487 ---LQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECS----KLENQLKKAHNA-EEAVRTNPEIND 558
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1642 QLRKNQgqlKELHRELEEGRAAHKEI---LASAREAERRCKNLEAEILQMQEMlaAAERARKQAETERDELSEEVAGGSS 1718
Cdd:pfam10174 559 RIRLLE---QEVARYKEESGKAQAEVerlLGILREVENEKNDKDKKIAELESL--TLRQMKEQNKKVANIKHGQQEMKKK 633
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1719 GRSLLSDEKRRleakisQLEEELEEEQANVETLNERLRKSQQLVDQLGAELTAERASSQNREGS----RLQLEKQTRDLK 1794
Cdd:pfam10174 634 GAQLLEEARRR------EDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHltnlRAERRKQLEEIL 707
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 1343958102 1795 AKLQDVESQARSKLKSSVAALE---AKLREAEEQLEVESRERQASAKNLRQK 1843
Cdd:pfam10174 708 EMKQEALLAAISEKDANIALLElssSKKKKTQEEVMALKREKDRLVHQLKQQ 759
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1022-1127 |
5.72e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 48.15 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1022 SKLKSKHESM---ISELEVRLKKEEKTRQDVEKAKRKVEAE-LVDLQEQQADLQAQLAELRAQLAAKEEELQTTQACLDE 1097
Cdd:COG0542 400 ARVRMEIDSKpeeLDELERRLEQLEIEKEALKKEQDEASFErLAELRDELAELEEELEALKARWEAEKELIEEIQELKEE 479
|
90 100 110
....*....|....*....|....*....|
gi 1343958102 1098 ESRQRGaalkRVRDLEALLAELQEDLEAEK 1127
Cdd:COG0542 480 LEQRYG----KIPELEKELAELEEELAELA 505
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1679-1926 |
8.67e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.83 E-value: 8.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1679 KNLEAEILQMQEMLAAAERARKQAETERDELSEEVAGGSSGRSLLSDEKRRLEAKISQLEEELEEEQANV----ETLNER 1754
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVkelkEERDEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1755 LRKSQQLVDQLgAELTAERASSQNREGSRLQLEKQTRDLKAKLQ--DVESQARSKLKSSVAALEAKLREAEEQLEvesre 1832
Cdd:COG1340 84 NEKLNELREEL-DELRKELAELNKAGGSIDKLRKEIERLEWRQQteVLSPEEEKELVEKIKELEKELEKAKKALE----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1833 rqasaknlrqKEKKLKDLTAQMEDERKQAQDYKDQMEKSSARMKQLKHQLEEAEEEAQRVAAARRKLQRELDEALEANDA 1912
Cdd:COG1340 158 ----------KNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADE 227
|
250
....*....|....
gi 1343958102 1913 LSREVSSLRSKLRR 1926
Cdd:COG1340 228 LHEEIIELQKELRE 241
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
836-1073 |
8.86e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 8.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 836 KVKPLLQVTRQEEEMGQKEEELKAVREAAAKAEADLKDITQKHSQLVEEQAMLEAKLQAEAELYAEAEDMRVRLEAKKQE 915
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 916 LEEVLHEMEARLEEEEERSISLQQEKKEMEQELQLMEAHIVQEEDARQKLQLEKAAVEgRVKKLEENLLLSEDQNNKLQK 995
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE-EAKKAEELKKKEAEEKKKAEE 1720
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1343958102 996 ERKLLEERLADMSSNLAEEEEKSKNLSKLKsKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQ 1073
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEEDKKKAEEAK-KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
963-1170 |
9.65e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.74 E-value: 9.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 963 QKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLLEErladmSSNLAEEEEK----SKNLSKLKSKHES---MISEL 1035
Cdd:PRK10929 82 AELRQQLNNERDEPRSVPPNMSTDALEQEILQVSSQLLEK-----SRQAQQEQDRareiSDSLSQLPQQQTEarrQLNEI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1036 EVRLK----------KEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEE-----LQTTQACLDEEsR 1100
Cdd:PRK10929 157 ERRLQtlgtpntplaQAQLTALQAESAALKALVDELELAQLSANNRQELARLRSELAKKRSQqldayLQALRNQLNSQ-R 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1101 QRGA--ALKRVRdleaLLAELQEDLEAEKVARGKAEaarRDLGEELN--SLRSELEDSLDTTAAQQELRVK------REQ 1170
Cdd:PRK10929 236 QREAerALESTE----LLAEQSGDLPKSIVAQFKIN---RELSQALNqqAQRMDLIASQQRQAASQTLQVRqalntlREQ 308
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1411-1855 |
1.02e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 47.21 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1411 YDKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSAKSAEERDRAEAELREKETKVLALMKMLED 1490
Cdd:COG5278 81 YEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1491 KQEALQEAERTVKALRVEMEDLISSKDDVGKSVHDLERAKRGLEAFVEEMKTQMEELEDELQVAEDAKLRLEVNSQALRA 1570
Cdd:COG5278 161 LALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALAL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1571 QHERELQAREEQGEEKRRQLLKQVRELEAELEEERKQRTLASAARKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQGQL 1650
Cdd:COG5278 241 ALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1651 KELHRELEEGRAAHKEILASAREAERRCKNLEAEILQMQEMLAAAERARKQAETERDELSEEVAGGSSGRSLLSDEKRRL 1730
Cdd:COG5278 321 AAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAA 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1731 EAKISQLEEELEEEQANVETLNERLRKSQQLVDQLGAELTAERASSQNREGSRLQLEKQTRDLKAKLQDVESQARSKLKS 1810
Cdd:COG5278 401 AAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAA 480
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1343958102 1811 SVAALEAKLREAEEQLEVESRERQASAKNLRQKEKKLKDLTAQME 1855
Cdd:COG5278 481 AAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAAL 525
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1492-1851 |
1.05e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.20 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1492 QEALQEAERTVKALRVEMEDLISSKDDVGKSVHDLERAKRGLEAFVEEMKTQMEELEDELQVAEDAKLRLEVNSQALRAQ 1571
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1572 HERELQAREE------QGEEKRRQLLKQVRELEAELEEERKQRTLASAARKKLEGEVKNTE---EQLEAASRGRDEALKQ 1642
Cdd:pfam07888 117 KDALLAQRAAhearirELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQaklQQTEEELRSLSKEFQE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1643 LRKNQGQLKELHRELEEGRAAHKEILASAREAERRCKNLEAEILQMQEMLAAAERArkqAETERDELSEEVAGGSSGRSL 1722
Cdd:pfam07888 197 LRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERK---VEGLGEELSSMAAQRDRTQAE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1723 LsdEKRRLEA-----KISQLEEELEEEQANVETLNERLRKSQQLVDQLGAELTAERASSQNR-EGSRLQLEKQTRDLkAK 1796
Cdd:pfam07888 274 L--HQARLQAaqltlQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERlQEERMEREKLEVEL-GR 350
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1343958102 1797 LQDVESQARSKLKSSVAALEAKLREAEEQLEVESRERQASAKNLRQKEKKLKDLT 1851
Cdd:pfam07888 351 EKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVA 405
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
862-1151 |
1.06e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.59 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 862 EAAAKAEADLKDITQKHSQLVEEQAMLEAKLQAEAELYAEAEDMRVRLEAKKQELEEVLHEMEARLEEEEERSISLQQEK 941
Cdd:PLN02939 149 QARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKEL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 942 KEMEQELQLMEAHIvqeEDARQKLQlekaavegRVKKLEENLLlsedqnnKLQKERKLLEERLADMSSNLAEEEEKSKNL 1021
Cdd:PLN02939 229 DVLKEENMLLKDDI---QFLKAELI--------EVAETEERVF-------KLEKERSLLDASLRELESKFIVAQEDVSKL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1022 SKLKskhesmiseLEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQaDLQAQLAELRAQLAAKEE--------ELQTTQA 1093
Cdd:PLN02939 291 SPLQ---------YDCWWEKVENLQDLLDRATNQVEKAALVLDQNQ-DLRDKVDKLEASLKEANVskfssykvELLQQKL 360
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1094 CLDEESRQRGAA--LKRVRDLEALLAELQEDLEaekvaRGKAEAARRDLGEELNSLRSEL 1151
Cdd:PLN02939 361 KLLEERLQASDHeiHSYIQLYQESIKEFQDTLS-----KLKEESKKRSLEHPADDMPSEF 415
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1514-1721 |
1.20e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1514 SSKDDVGKSVHDLERAKRGLEAFVEEMKTQMEELEDELQVAEDAKLRLEVNSQALraqhERELQAREEQGEEKRRQLLKQ 1593
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1594 VRELEAELEEE-------------------RKQRTLASAARKKLEgEVKNTEEQLEAASRGRDEALKQLRKNQGQLKELH 1654
Cdd:COG3883 92 ARALYRSGGSVsyldvllgsesfsdfldrlSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1343958102 1655 RELEEGRAAHKEILASAREAERRcknLEAEILQMQEMLAAAERARKQAETERDELSEEVAGGSSGRS 1721
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAA---AEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1007-1268 |
1.24e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1007 MSSNLAEEEEKSKNLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEE 1086
Cdd:COG1340 6 LSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1087 ELQTTQACLDEESRQRGAALKRVRDLEALLAELqEDLEAEKVARGKAEAARRDLGEELNSLRSELEdsldttAAQQELRV 1166
Cdd:COG1340 86 KLNELREELDELRKELAELNKAGGSIDKLRKEI-ERLEWRQQTEVLSPEEEKELVEKIKELEKELE------KAKKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1167 KRE-QEMAMLKKAMEDEGRSHETQIQELRQKHGQAVEELREHLEQAKKVRAALEKAKQA---LEKEAADLSADLRALSST 1242
Cdd:COG1340 159 NEKlKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEiveAQEKADELHEEIIELQKE 238
|
250 260
....*....|....*....|....*.
gi 1343958102 1243 KQDVEQKKKKVEAQLNDLQLRFSESE 1268
Cdd:COG1340 239 LRELRKELKKLRKKQRALKREKEKEE 264
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1627-1938 |
1.34e-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: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1627 EQLEAASRGRDEALKQLRKNQGQLKELHRELEEGRAAHKEI----------LASAREAER------RCK----NLEAEIL 1686
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLeqdyqaasdhLNLVQTALRqqekieRYQedleELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1687 QMQEMLAAAERARKQAETERDELSEEVaggSSGRSLLSDEKRRLEAkisQLEEELEEEQANvetlnERLRKSQQL----- 1761
Cdd:COG3096 365 EQEEVVEEAAEQLAEAEARLEAAEEEV---DSLKSQLADYQQALDV---QQTRAIQYQQAV-----QALEKARALcglpd 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1762 --VDQLGAELTAERASSQNREGSRLQLEKQTRDLKAKLQDVES--QARSKLKSSVAALEAkLREAEEQLEvESRERQASA 1837
Cdd:COG3096 434 ltPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKayELVCKIAGEVERSQA-WQTARELLR-RYRSQQALA 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1838 KNLRQKEKKLKDLTaQMEDERKQAQDYKDQMEKSSAR-----------MKQLKHQLEEAEEEAQRVAAARRKLQRELDEA 1906
Cdd:COG3096 512 QRLQQLRAQLAELE-QRLRQQQNAERLLEEFCQRIGQqldaaeeleelLAELEAQLEELEEQAAEAVEQRSELRQQLEQL 590
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1343958102 1907 --------------LEANDALSRevsslrskLRRGGGEVLTSGQRV 1938
Cdd:COG3096 591 rarikelaarapawLAAQDALER--------LREQSGEALADSQEV 628
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1135-1444 |
1.52e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1135 AARRDLGEELNSLR--SELeDSLDTT---AAQQELrvkreQEMAMLKKAMEDEGRSHETQIQELRQKHGQAVEELR---- 1205
Cdd:PHA02562 150 PARRKLVEDLLDISvlSEM-DKLNKDkirELNQQI-----QTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQnkyd 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1206 EHLEQAKKVRAALEKAKQAL---EKEAADLSADLRALSstkqdveQKKKKVEAQLNDLQlrfseserqrnelseRVSKMT 1282
Cdd:PHA02562 224 ELVEEAKTIKAEIEELTDELlnlVMDIEDPSAALNKLN-------TAAAKIKSKIEQFQ---------------KVIKMY 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1283 VELDsvtgllneaegrniklskEASSISSQLQDAQELLSEETRQKLNLSGRLRQLEEDKGclmeqleeemeakQAVER-- 1360
Cdd:PHA02562 282 EKGG------------------VCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAID-------------ELEEImd 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1361 QASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLDsQRQLVS 1440
Cdd:PHA02562 331 EFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKY-HRGIVT 409
|
....
gi 1343958102 1441 NLEK 1444
Cdd:PHA02562 410 DLLK 413
|
|
| COG4192 |
COG4192 |
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ... |
1066-1334 |
1.67e-04 |
|
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];
Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 46.60 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1066 QQADLQAQLAELRAQLAAKEEELQTTQACLDEESRQRGAALKRVRDLEALLAELQE------DLEAEKV-ARGKAEAARR 1138
Cdd:COG4192 75 AAATNTTERSQLRNQLNTQLADIEELLAELEQLTQDAGDLRAAVADLRNLLQQLDSlltqriALRRRLQeLLEQINWLHQ 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1139 DLGEELNSLRSELEDSLDTTAAQQELRVKREQEMAMLkkamedegrsheTQIQELRQKHGQAVEELREHLEQAKkvRAAL 1218
Cdd:COG4192 155 DFNSELTPLLQEASWQQTRLLDSVETTESLRNLQNEL------------QLLLRLLAIENQIVSLLREVAAARD--QADV 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1219 EKAKQALEKEAADLSADLRALSSTKQDVEQKkkkveaQLNDLQLRFSESErqrNELSERVSKmtvELDSVTGLLNEAEGR 1298
Cdd:COG4192 221 DNLFDRLQYLKDELDRNLQALKNYPSTITLR------QLIDELLAIGSGE---GGLPSLRRD---ELAAQATLEALAEEN 288
|
250 260 270
....*....|....*....|....*....|....*....
gi 1343958102 1299 NIKLSKEASSISSQLQDAQELLSE---ETRQKLNLSGRL 1334
Cdd:COG4192 289 NSILEQLRTQISGLVGNSREQLVAlnqETAQLVQQSGIL 327
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1032-1145 |
1.89e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.73 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1032 ISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQACLDEESRQRGAALKRVRD 1111
Cdd:PRK09039 62 IAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVEL 141
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1343958102 1112 L----EAL---LAELQEDLEAEKvARGKAEAAR-RDLGEELN 1145
Cdd:PRK09039 142 LnqqiAALrrqLAALEAALDASE-KRDRESQAKiADLGRRLN 182
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1254-1473 |
1.95e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1254 EAQLNDLQLRFSESERQRNELSERVSKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQELLSEETRQklnLSGR 1333
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE---LGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1334 LRQLEEDkGCLMEQLEEEMEAKQAVE--RQASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELeaasgdyeekaaay 1411
Cdd:COG3883 92 ARALYRS-GGSVSYLDVLLGSESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL-------------- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1343958102 1412 DKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSAKSAEERDRAEAE 1473
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
653-677 |
1.98e-04 |
|
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: 43.87 E-value: 1.98e-04
10 20
....*....|....*....|....*
gi 1343958102 653 YKESLGKLMATLHNTQPNFVRCIIP 677
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1199-1316 |
2.01e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 46.48 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1199 QAVEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLQlrfSESERQRNELSERV 1278
Cdd:PRK11448 142 NLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQ---EKAAETSQERKQKR 218
|
90 100 110
....*....|....*....|....*....|....*...
gi 1343958102 1279 SKMTVELDSVTgLLNEAEGRNIklskeassISSQLQDA 1316
Cdd:PRK11448 219 KEITDQAAKRL-ELSEEETRIL--------IDQQLRKA 247
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1669-1882 |
2.07e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1669 ASAREAERRCKNLEAEILQMQEMLAAAERARKQAETERDELSeevaggssgrslLSDEKRRLEAKISQLEEELEEEQANV 1748
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVD------------LSEEAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1749 ETLNERLrksQQLVDQLGAELTAERASSQNREGSrlQLEKQTRDLKAKLQDVESQARSKlKSSVAALEAKLREAEEQLEV 1828
Cdd:COG3206 236 AEAEARL---AALRAQLGSGPDALPELLQSPVIQ--QLRAQLAELEAELAELSARYTPN-HPDVIALRAQIAALRAQLQQ 309
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1343958102 1829 ESRERQASAKNLRQK-EKKLKDLTAQMEDERKQAQdykdQMEKSSARMKQLKHQL 1882
Cdd:COG3206 310 EAQRILASLEAELEAlQAREASLQAQLAQLEARLA----ELPELEAELRRLEREV 360
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
858-1195 |
2.23e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 858 KAVREAAAKAEADLKDITQKHSQLVEEQAMLEAKLQAEAELYAEAEDMRVRLEAKKQELEEVLHemearleeeeersiSL 937
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIK--------------TL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 938 QQEKKEMEQELQLMEahivqeeDARQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLLEERLADMSSNLAEEEEK 1017
Cdd:pfam07888 142 TQRVLERETELERMK-------ERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1018 SKNLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEA---ELVDLQEQQADLQAQLAELRAQLAakEEELQTTQAC 1094
Cdd:pfam07888 215 ITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGlgeELSSMAAQRDRTQAELHQARLQAA--QLTLQLADAS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1095 L-----------DEESRQRGAALKRVRdLEALLAELQEDLEAEKVARGKAEAARRDLGEELNSLRSELEDSldttaaqqe 1163
Cdd:pfam07888 293 LalregrarwaqERETLQQSAEADKDR-IEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSES--------- 362
|
330 340 350
....*....|....*....|....*....|...
gi 1343958102 1164 lrvKRE-QEMAMLKKAMEDEGRSHETQIQELRQ 1195
Cdd:pfam07888 363 ---RRElQELKASLRVAQKEKEQLQAEKQELLE 392
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1538-1923 |
2.30e-04 |
|
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: 46.17 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1538 EEMKTQMEELEDELQVAEDAKLRLEVNSQALRAQHERELQ--AREEQGEEKRRQLLKQVRELEAELEEERKQRTLASAAR 1615
Cdd:TIGR04523 162 NDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELllSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEI 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1616 KKLEGEVKNTEEQLEAASRGRDEALKQLRKNQGQLKELHRELEEgraahkeilasareAERRCKNLEAEILQM-----QE 1690
Cdd:TIGR04523 242 NEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE--------------LEKQLNQLKSEISDLnnqkeQD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1691 MLAAAERARKQAETERDELSEEVAGGSSGRSllsdekrRLEAKISQLEEELEEEQANVETLNERLRKSQQLVDQLGAELT 1770
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIQNQISQNNKIIS-------QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1771 AERASSQNregsrlqLEKQTRDLKAKLQDVESQARsKLKSSVAALEAKLREAEEQLEVESRERQASAKNLR-------QK 1843
Cdd:TIGR04523 381 SYKQEIKN-------LESQINDLESKIQNQEKLNQ-QKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKdltnqdsVK 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1844 EKKLKDLTAQMEDERKQAQDYKDQMEKSSARMKQLKHQLEEAEEEAQRVAAARRKLQRELDEaleandaLSREVSSLRSK 1923
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKD-------LTKKISSLKEK 525
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
843-1453 |
2.68e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 45.90 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 843 VTRQEEEMGQKEEELKAVREAAAKAEADLKDITQKHSQLVEEQAMLEAKLQAEAELYAEAEDMRVRL-EAKKQELEEVlh 921
Cdd:pfam07111 68 ISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLeEGSQRELEEI-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 922 emearleeeeersislqqEKKEMEQELQLMEAHivqeEDARQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLLE 1001
Cdd:pfam07111 146 ------------------QRLHQEQLSSLTQAH----EEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1002 ERLADMSSNLAEEEEKSKNLSKLKSkhESMISELEvrlkkeektRQDVEKAKRKVEAELVDLQEQQADLQA--QLAELRA 1079
Cdd:pfam07111 204 KQLSKTQEELEAQVTLVESLRKYVG--EQVPPEVH---------SQTWELERQELLDTMQHLQEDRADLQAtvELLQVRV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1080 Q-----LAAKEEELQTTQACLDEESRQrgaalkRVRDLEALLAELQEDLEAEKVARGKAEAARRDLGEELNslrseleds 1154
Cdd:pfam07111 273 QslthmLALQEEELTRKIQPSDSLEPE------FPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLR--------- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1155 lDTTAAQQELRVKREQEMAMLKKAMEDEGRSHE-------------TQIQELRQKHGQ----AVEELREHLEQAKKVRAA 1217
Cdd:pfam07111 338 -GQVAELQEQVTSQSQEQAILQRALQDKAAEVEvermsakglqmelSRAQEARRRQQQqtasAEEQLKFVVNAMSSTQIW 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1218 LEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSES-------------ERQRNELSERVSKMTVE 1284
Cdd:pfam07111 417 LETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLRQESCpppppappvdadlSLELEQLREERNRLDAE 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1285 LDSVTGLLNEAEGR--------NIKLSKEASSISSQLQDAQELLSEETRQ-KLNLSGRLRQLEEDKGCLMEQLEEEMEAK 1355
Cdd:pfam07111 497 LQLSAHLIQQEVGRareqgeaeRQQLSEVAQQLEQELQRAQESLASVGQQlEVARQGQQESTEEAASLRQELTQQQEIYG 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1356 QAVERQASS----LSVQLSDLKKRLEEL----SAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELE- 1426
Cdd:pfam07111 577 QALQEKVAEvetrLREQLSDTKRRLNEArreqAKAVVSLRQIQHRATQEKERNQELRRLQDEARKEEGQRLARRVQELEr 656
|
650 660
....*....|....*....|....*..
gi 1343958102 1427 DVLMDLDSQRQLVSNLEKKQKKFDQML 1453
Cdd:pfam07111 657 DKNLMLATLQQEGLLSRYKQQRLLAVL 683
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1236-1595 |
2.72e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.66 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1236 LRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVELDSVTGLLNEAEgrniKLSKEASSISSQLQD 1315
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELE----EKYKELSASSEELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1316 AQELLSEETRQKLnlsGRLRQLEEDKGCLMEQLEEEMEAKQAVERQASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQR 1395
Cdd:pfam07888 116 EKDALLAQRAAHE---ARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1396 ELEAASGDYEEKAAAYDKLEKSRGRLQQ----------ELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEeravsakSAE 1465
Cdd:pfam07888 193 EFQELRNSLAQRDTQVLQLQDTITTLTQklttahrkeaENEALLEELRSLQERLNASERKVEGLGEELSS-------MAA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1466 ERDRAEAELREKETKVLALMKMLEDKQEALQEA------ERTVKALRVEMEdlissKDDVGKSVHDLERakrgLEAFVEE 1539
Cdd:pfam07888 266 QRDRTQAELHQARLQAAQLTLQLADASLALREGrarwaqERETLQQSAEAD-----KDRIEKLSAELQR----LEERLQE 336
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1540 MKTQMEELEDELQVAEDAKLRLEVNS----QALRAQhERELQAREEQGEEKRRQLLKQVR 1595
Cdd:pfam07888 337 ERMEREKLEVELGREKDCNRVQLSESrrelQELKAS-LRVAQKEKEQLQAEKQELLEYIR 395
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
993-1124 |
2.78e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.34 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 993 LQKERKL-LEERLADMSSNLAEEEEKSKNLSKLKSKHESMISELEVRLkkeektrQDVEKAKRKVEAELVDLQEQQADLQ 1071
Cdd:PRK09039 71 LERQGNQdLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRA-------GELAQELDSEKQVSARALAQVELLN 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1343958102 1072 AQLAELRAQLAAKEEELQTTQAcLDEESRQRGAALKrvRDLEALLAELQEDLE 1124
Cdd:PRK09039 144 QQIAALRRQLAALEAALDASEK-RDRESQAKIADLG--RRLNVALAQRVQELN 193
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1116-1863 |
2.78e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 46.36 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1116 LAELQEDLEAEKVARGKAEAARRDLGEELNSLRSELEDSLDTTAAQ-----QELRVKREQemaMLKKAMEDEGRSHETQI 1190
Cdd:NF041483 17 LSRFEAEMDRLKTEREKAVQHAEDLGYQVEVLRAKLHEARRSLASRpaydgADIGYQAEQ---LLRNAQIQADQLRADAE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1191 QELRQKHGQAVEELREHLEQAKKVRAALE----KAKQALEKEAADLSADLRA-LSSTKQDVEQKKKKVEAQLNDLqLRFS 1265
Cdd:NF041483 94 RELRDARAQTQRILQEHAEHQARLQAELHteavQRRQQLDQELAERRQTVEShVNENVAWAEQLRARTESQARRL-LDES 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1266 ESERQRNELSERVSKMTVELDSVTGLLNEAEGRNiklsKEASSISSQL-QDAQELLSEETRQKLNLSGRLRQLEedkgcl 1344
Cdd:NF041483 173 RAEAEQALAAARAEAERLAEEARQRLGSEAESAR----AEAEAILRRArKDAERLLNAASTQAQEATDHAEQLR------ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1345 meqLEEEMEAKQAvERQASSLS----VQLSDLKKRLEELSAAVE-LLEEGKKRLQRELEAASGDYEEK--------AAAY 1411
Cdd:NF041483 243 ---SSTAAESDQA-RRQAAELSraaeQRMQEAEEALREARAEAEkVVAEAKEAAAKQLASAESANEQRtrtakeeiARLV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1412 DKLEKSRGRLQQELEDVLMDL--DSQRQLVSNLEKKQKKFDQMLAEERAVSAKSAEE-RDRAEAElrEKETKVLALMKML 1488
Cdd:NF041483 319 GEATKEAEALKAEAEQALADAraEAEKLVAEAAEKARTVAAEDTAAQLAKAARTAEEvLTKASED--AKATTRAAAEEAE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1489 EDKQEALQEAERtvkaLRVEMEDLI-----SSKDDV----GKSVHDLERAKRgleafveeMKTQMEELEDElQVAEDAKL 1559
Cdd:NF041483 397 RIRREAEAEADR----LRGEAADQAeqlkgAAKDDTkeyrAKTVELQEEARR--------LRGEAEQLRAE-AVAEGERI 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1560 RLEVNSQALRAQHERELQAREEQGeeKRRQLLKQVRELEAELEEerKQRTLASAARKKLEGEVKNTEEQLEA-ASRGRDE 1638
Cdd:NF041483 464 RGEARREAVQQIEEAARTAEELLT--KAKADADELRSTATAESE--RVRTEAIERATTLRRQAEETLERTRAeAERLRAE 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1639 ALKQLRKNQGQLKELHRELEEgrAAHKEILASAREAERRCKNLEAEilqMQEMLAAAERARKQAETERDELSEEVAggss 1718
Cdd:NF041483 540 AEEQAEEVRAAAERAARELRE--ETERAIAARQAEAAEELTRLHTE---AEERLTAAEEALADARAEAERIRREAA---- 610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1719 grsllsDEKRRLEAKISQleeELEEEQANVETLNERLRksqqlvDQLGAELTAERASSQNrEGSRLQLE--KQTRDLKAK 1796
Cdd:NF041483 611 ------EETERLRTEAAE---RIRTLQAQAEQEAERLR------TEAAADASAARAEGEN-VAVRLRSEaaAEAERLKSE 674
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1343958102 1797 LQDVESQARSKlkssvaALEAKLREAEEQLEVESRERQASAKNLRQKEKKLKDLTAQMEDERKQAQD 1863
Cdd:NF041483 675 AQESADRVRAE------AAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERARE 735
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1301-1504 |
2.82e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1301 KLSKEASSISSQLQDAQELLSEETRQKLNLSGRLRQLEEdkgclmeQLEEEMEAKQAVERQASSLSVQLSDLKKRLEELS 1380
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-------RIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1381 AAvelLEEGKKRLQRELEAA-----------------SGDYEEKAAAYDKLEKSRGRL-------QQELEDVLMDLDSQR 1436
Cdd:COG4942 97 AE---LEAQKEELAELLRALyrlgrqpplalllspedFLDAVRRLQYLKYLAPARREQaeelradLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1343958102 1437 Q----LVSNLEKKQKKFDQMLAEERAVSAKSAEERDRAEAELREKETKVLALMKMLEDKQEALQEAERTVKA 1504
Cdd:COG4942 174 AeleaLLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1409-1659 |
2.84e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1409 AAYDKLEKSRGR-LQQELEDVLMDLDSQRQLVS----NLEKKQKKFDQMLAEERAVSAKSAEERDRAEAELREKETKVLA 1483
Cdd:PHA02562 166 SEMDKLNKDKIReLNQQIQTLDMKIDHIQQQIKtynkNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1484 LMKMLEDKQEALqeaertvKALRVEMEDLISSKDDVGKSVHDLERAkrgleafvEEMKTQMEELEDELQVAEDAKLRLEV 1563
Cdd:PHA02562 246 LVMDIEDPSAAL-------NKLNTAAAKIKSKIEQFQKVIKMYEKG--------GVCPTCTQQISEGPDRITKIKDKLKE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1564 NSQALraqheRELQAREEQGEEKRRQLLKQVRELEAELEEERKQRTLASAARKKLEgEVKNTEEQLEAASRGRDEALKQL 1643
Cdd:PHA02562 311 LQHSL-----EKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAK-KVKAAIEELQAEFVDNAEELAKL 384
|
250
....*....|....*.
gi 1343958102 1644 RKNQGQLKELHRELEE 1659
Cdd:PHA02562 385 QDELDKIVKTKSELVK 400
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1035-1324 |
2.96e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.95 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1035 LEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQACLDEESrqrgaalkRVRDLEA 1114
Cdd:PRK10246 424 LRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTICEQEA--------RIKDLEA 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1115 LLAELQED-------------LEAEKVARGKAEAARRD-LGEELNSLRSE---LEDSLDTTAAQ-----QELRVKREQEM 1172
Cdd:PRK10246 496 QRAQLQAGqpcplcgstshpaVEAYQALEPGVNQSRLDaLEKEVKKLGEEgaaLRGQLDALTKQlqrdeSEAQSLRQEEQ 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1173 AMLKKAME-------------------DEGRSHETQIQELRQKHG-QAveELREHLEQAKKVRAALEKAKQALEkeaadl 1232
Cdd:PRK10246 576 ALTQQWQAvcaslnitlqpqddiqpwlDAQEEHERQLRLLSQRHElQG--QIAAHNQQIIQYQQQIEQRQQQLL------ 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1233 sADLRALSSTKQDVEQKKKKVEAQLNDLQlRFSESERQRNELSERVSKMTVELDSV--TGLLNEAEGRNI-----KLSKE 1305
Cdd:PRK10246 648 -TALAGYALTLPQEDEEASWLATRQQEAQ-SWQQRQNELTALQNRIQQLTPLLETLpqSDDLPHSEETVAldnwrQVHEQ 725
|
330
....*....|....*....
gi 1343958102 1306 ASSISSQLQDAQELLSEET 1324
Cdd:PRK10246 726 CLSLHSQLQTLQQQDVLEA 744
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
868-1193 |
3.18e-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: 45.52 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 868 EADLKDITQKHSQLVEEQAMLEAKLQAEAELYAEAEDMRVrlEAKKQELEEVLHEMEARLEEEEERSISLQQEKKEMEQE 947
Cdd:pfam09731 84 EEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSE--QEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 948 -LQLMEAHIVQEEDARQK-----LQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLLEERLADMSSNLAEEEEKSKNL 1021
Cdd:pfam09731 162 hTDSLKEASDTAEISREKatdsaLQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1022 SKLKSKH---------------ESMISELEVRLKKEEKTRQD-----VEKAKRKVEAelvdLQEQQADLQAQlAELRAQL 1081
Cdd:pfam09731 242 AKLVDQYkelvaserivfqqelVSIFPDIIPVLKEDNLLSNDdlnslIAHAHREIDQ----LSKKLAELKKR-EEKHIER 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1082 AAKEEELQttqacLDEESRQRGAALKRVRDLEallaELQEDLEAEKVARGKAEAARRDLGEELNSLRSELEDSLDTTAAQ 1161
Cdd:pfam09731 317 ALEKQKEE-----LDKLAEELSARLEEVRAAD----EAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLVE 387
|
330 340 350
....*....|....*....|....*....|..
gi 1343958102 1162 QELRVKREQeMAMLKKAMEDEGRSHETQIQEL 1193
Cdd:pfam09731 388 QEIELQREF-LQDIKEKVEEERAGRLLKLNEL 418
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1074-1318 |
3.49e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1074 LAELRAQLAAKEEELQTTQACLDEESRQRGAALKRVRDLEALLAELQEDLEaekvargKAEAARRDLGEELNSLRSELEd 1153
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-------ELQAELEALQAEIDKLQAEIA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1154 sldttAAQQELRVKREQemamLKKAMEDEgrshetqiqelrQKHGQAVEELrEHLEQAKKVRAALEKAkQALEKEAADLS 1233
Cdd:COG3883 76 -----EAEAEIEERREE----LGERARAL------------YRSGGSVSYL-DVLLGSESFSDFLDRL-SALSKIADADA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1234 ADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQL 1313
Cdd:COG3883 133 DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
....*
gi 1343958102 1314 QDAQE 1318
Cdd:COG3883 213 AAAAA 217
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
857-1037 |
3.57e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 857 LKAVREAAAKAEADLKDITQKHS--QLVEEQAMLEAKLQAEAELYAEAEDMRVRLEAKKQELEEVLHEMEARLEEEEERS 934
Cdd:COG3206 184 LPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 935 I--SLQQEKKEMEQELQLMEAHIVQEEDARQKLQLEKAAVEGRVKKLEENLLLSedqnnkLQKERKLLEERLADMSSNLA 1012
Cdd:COG3206 264 ViqQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS------LEAELEALQAREASLQAQLA 337
|
170 180
....*....|....*....|....*
gi 1343958102 1013 EEEEKSKNLSKLKSKHESMISELEV 1037
Cdd:COG3206 338 QLEARLAELPELEAELRRLEREVEV 362
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1611-1853 |
3.64e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1611 ASAARKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQGQLKELHRELEEgraahkeilasareaerrcknLEAEILQMQE 1690
Cdd:COG3883 28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE---------------------AEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1691 MLaaAERARKQAETERDELSEEVAGGSSGrslLSDEKRRLEAkisqleeeleeeqanVETLNERLRKSQQLVDQLGAELT 1770
Cdd:COG3883 87 EL--GERARALYRSGGSVSYLDVLLGSES---FSDFLDRLSA---------------LSKIADADADLLEELKADKAELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1771 AERASSQNREGsrlQLEKQTRDLKAKLQDVESQaRSKLKSSVAALEAKLREAEEQLEVESRERQASAKNLRQKEKKLKDL 1850
Cdd:COG3883 147 AKKAELEAKLA---ELEALKAELEAAKAELEAQ-QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
...
gi 1343958102 1851 TAQ 1853
Cdd:COG3883 223 AAA 225
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
909-1121 |
3.79e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 909 LEAKKQELEEVLHEMEARLEEEEERSISLQqekkeMEQELQLMEAHIVQEEDARQKLQLEKAAVEGRVKKLEENLLLSED 988
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNGLVD-----LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 989 QNNKLQKERKL--LEERLADMSSNLAEEeeksknLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQ 1066
Cdd:COG3206 255 ALPELLQSPVIqqLRAQLAELEAELAEL------SARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAR 328
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1343958102 1067 QADLQAQLAELRAQLAakeeELQTTQACLDEESRQRGAALKRvrdLEALLAELQE 1121
Cdd:COG3206 329 EASLQAQLAQLEARLA----ELPELEAELRRLEREVEVAREL---YESLLQRLEE 376
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1354-1555 |
3.89e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1354 AKQAVERQASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLD 1433
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1434 SQRQLVSNLEKK---------------QKKFDQMLAEERAVSAKSAEERDRAE---AELREKETKVLALMKMLEDKQEAL 1495
Cdd:COG4942 101 AQKEELAELLRAlyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEelrADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1496 QEAErtvkALRVEMEDLISSKDDVgksVHDLERAKRGLEAFVEEMKTQMEELEDELQVAE 1555
Cdd:COG4942 181 AELE----EERAALEALKAERQKL---LARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1682-1946 |
4.50e-04 |
|
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: 45.55 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1682 EAEILQMQEMLAAAERARKQAETERDELSEEVAGgssgrslLSDEKRRLEAKISQLEEELEEEQANVETLNERLRKSQQL 1761
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQ-------LCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1762 VDQLGAELTAERASSQNREGSRLQLEKQTRDLKAKLqDVESQARSKLKSSVAALEAKLREAEEQLEVESRERQASAKNLR 1841
Cdd:pfam01576 77 LHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQL-DEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1842 QKEKKLKDLTAQMEDERKQAQDYKDQMEKSSARMKQLKHQLEEAEEEAQRVAAARRKLQRELDEALEANDALSREVSSLR 1921
Cdd:pfam01576 156 LLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELR 235
|
250 260
....*....|....*....|....*
gi 1343958102 1922 SKLRRGGGEVLTSGQRVGGGGSIRN 1946
Cdd:pfam01576 236 AQLAKKEEELQAALARLEEETAQKN 260
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1576-1925 |
4.50e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.89 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1576 LQAREEQGEEKRRQLLKQVRELEAELEEERKQRTLASAARKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQGQLKELHR 1655
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1656 ELEEGR----AAHKEILASAREAERRCKNL-------EAEILQMQEMLAAAERARKQAETERDELSEEVAGGSSGRSLLS 1724
Cdd:pfam07888 112 ELSEEKdallAQRAAHEARIRELEEDIKTLtqrvlerETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1725 DEKRRLEAKISQLEEELEEEQANVETLNERLRKSQQLVDQLGAELTAERASSQNREGSrlqlEKQTRDLKAKLQDVESQ- 1803
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNAS----ERKVEGLGEELSSMAAQr 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1804 --ARSKL-KSSVAALEAKLREAEEQLEVesRERQASAknlrQKEKKLKDLTAQMEderkqaqdyKDQMEKSSARMKQLKH 1880
Cdd:pfam07888 268 drTQAELhQARLQAAQLTLQLADASLAL--REGRARW----AQERETLQQSAEAD---------KDRIEKLSAELQRLEE 332
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1343958102 1881 QLeeaEEEAQRVAAARRKLQRELDEALEANDALSREVSSLRSKLR 1925
Cdd:pfam07888 333 RL---QEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLR 374
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1615-1877 |
4.90e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.68 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1615 RKKLEGEVKNTEEQLEAASRgrdealkQLRKNQGQLKELHRELeegraahKEILASAREAERRCKnleaeilQMQEMLAA 1694
Cdd:PRK11637 70 RASLLAQLKKQEEAISQASR-------KLRETQNTLNQLNKQI-------DELNASIAKLEQQQA-------AQERLLAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1695 A-ERARKQAETERDELseevaggssgrsLLSDEKRRLEAKIsqleeeleeeQANVETLNERLRKSQQLVDQLGAELTAER 1773
Cdd:PRK11637 129 QlDAAFRQGEHTGLQL------------ILSGEESQRGERI----------LAYFGYLNQARQETIAELKQTREELAAQK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1774 ASSQNREGSRLQLEKQTRDLKAKLQdvesQARSKLKSSVAALEAKLREAEEQLeVEsrerqasaknLRQKEKKLKDLTAQ 1853
Cdd:PRK11637 187 AELEEKQSQQKTLLYEQQAQQQKLE----QARNERKKTLTGLESSLQKDQQQL-SE----------LRANESRLRDSIAR 251
|
250 260
....*....|....*....|....
gi 1343958102 1854 MEDERKqAQDYKDQMEKSSARMKQ 1877
Cdd:PRK11637 252 AEREAK-ARAEREAREAARVRDKQ 274
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1637-1774 |
5.25e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1637 DEALKQLRKNQGQLKELHRELEEGRAAHKEILASAREAERRCKNLEAEILQMQEMLAAAERARKQAETERD--ELSEEVA 1714
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyeALQKEIE 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1715 GGSSGRSLLSDEKRRLEAKISQLEEELEEEQANVETLNERLRKSQQLVDQLGAELTAERA 1774
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1039-1484 |
5.28e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 44.90 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1039 LKKEEKTRQDVEKAKRKVEAELVDLQEQQAD---LQAQLAELRAQLAAKEEELQTTQACLDEESRQRGAALKRVRDLEAL 1115
Cdd:COG5278 71 LTGDESFLEPYEEARAEIDELLAELRSLTADnpeQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKAL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1116 LAELQEDLEAEKVARGKAEAARRDLGEELNSLRSELEDSLDTTAAQQELRVKREQEMAMLKKAMEDEGRSHETQIQELRQ 1195
Cdd:COG5278 151 MDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1196 KHGQAVEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELS 1275
Cdd:COG5278 231 ALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1276 ERVSKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQELLSEETRQKLNLSGRLRQLEEDKGCLMEQLEEEMEAK 1355
Cdd:COG5278 311 AAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVEL 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1356 QAVERQASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLDSQ 1435
Cdd:COG5278 391 EVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAA 470
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1343958102 1436 RQLVSNLEKKQKKFDQMLAEERAVSAKSAEERDRAEAELREKETKVLAL 1484
Cdd:COG5278 471 VAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAA 519
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1058-1937 |
5.99e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 45.20 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1058 AELVDLQEQQADLQAQLAELRAQLAAKEEELQTtQACLDEESRQRGAAlkrvRDLEALLAELQEDL-EAEKVARGKAEAA 1136
Cdd:NF041483 433 AKTVELQEEARRLRGEAEQLRAEAVAEGERIRG-EARREAVQQIEEAA----RTAEELLTKAKADAdELRSTATAESERV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1137 RRDLGEELNSLRSELEDSLDTTAAQQE-LRVKREQEMAMLKKAMEDEGRS-HETQIQELRQKHGQAVEEL-REHLEQAKK 1213
Cdd:NF041483 508 RTEAIERATTLRRQAEETLERTRAEAErLRAEAEEQAEEVRAAAERAARElREETERAIAARQAEAAEELtRLHTEAEER 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1214 VRAALEKAKQA------LEKEAADLSADLRAlsstkqDVEQKKKKVEAQLNdlqlrfSESERQRNELSERVSKMTVELDS 1287
Cdd:NF041483 588 LTAAEEALADAraeaerIRREAAEETERLRT------EAAERIRTLQAQAE------QEAERLRTEAAADASAARAEGEN 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1288 VTGLL-----NEAEGRNIKLSKEASSISSQLQDAQELLSEETRQKLN-----LSGRLRQLEEDKGclmeqlEEEMEAKQA 1357
Cdd:NF041483 656 VAVRLrseaaAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAaaqeeAARRRREAEETLG------SARAEADQE 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1358 VERQASSLSVQLSDLKKRLEELSA-AVELLEEGKKRLQRELEAAsgdyEEKAAaydKLEKSRGRLQQELEDVLMDLDSQR 1436
Cdd:NF041483 730 RERAREQSEELLASARKRVEEAQAeAQRLVEEADRRATELVSAA----EQTAQ---QVRDSVAGLQEQAEEEIAGLRSAA 802
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1437 QLVSNLEKK--QKKFDQMLAEERAVSAKSAEERDRAEAELREKETKVLALmkmledkqealqeAERTVkalrvemedlis 1514
Cdd:NF041483 803 EHAAERTRTeaQEEADRVRSDAYAERERASEDANRLRREAQEETEAAKAL-------------AERTV------------ 857
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1515 skddvGKSVHDLERAKRGLEAFVEEMKTqmeELEDELQVAED--AKLRLEVNSQALRAQHERELQAREEQGEEKRrqllK 1592
Cdd:NF041483 858 -----SEAIAEAERLRSDASEYAQRVRT---EASDTLASAEQdaARTRADAREDANRIRSDAAAQADRLIGEATS----E 925
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1593 QVRELEAELEEERKQRTLASAARKKLEGEVKNTEEQLEAASRGRDEALkqlrknqgqlkelhreleegRAAHKEILASAR 1672
Cdd:NF041483 926 AERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERL--------------------RAEAAETVGSAQ 985
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1673 EAERRCKNlEAEILQmQEMLAAAERARKQAETERDELSEEVAGGSSGRSLLSDEKRRLEAKISQLEEELEEEQANVETLN 1752
Cdd:NF041483 986 QHAERIRT-EAERVK-AEAAAEAERLRTEAREEADRTLDEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALR 1063
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1753 ERLRKSQQLVDQLGAELT-AERASSQNREGSRLQLEKQTRDLKAKLQDVESQARSKLKSsvaALEAKLREAEEQLEVESR 1831
Cdd:NF041483 1064 TTTEAEAQADTMVGAARKeAERIVAEATVEGNSLVEKARTDADELLVGARRDATAIRER---AEELRDRITGEIEELHER 1140
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1832 ERQASAKNLRQKEKKLKDLTAQMEDERKQAQDYKDQM------EKSSARMKQLKhqleeaeeeaqrvaaarrKLQRELDE 1905
Cdd:NF041483 1141 ARRESAEQMKSAGERCDALVKAAEEQLAEAEAKAKELvsdansEASKVRIAAVK------------------KAEGLLKE 1202
|
890 900 910
....*....|....*....|....*....|..
gi 1343958102 1906 ALEANDALSREVSSLRSKLRRGGGEVLTSGQR 1937
Cdd:NF041483 1203 AEQKKAELVREAEKIKAEAEAEAKRTVEEGKR 1234
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1638-1925 |
6.25e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.07 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1638 EALKQLRKNQG---QLKELHRELEEGRAAHKEILASAREAERRCKNLEAEILQMQEMLAAaERARKQAETERDELSEEVA 1714
Cdd:COG5022 769 KRIKKIQVIQHgfrLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKR-EKKLRETEEVEFSLKAEVL 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1715 GGSSGRSLLSDEKRRLEAKisqlEEELEEEQANVETLNERLRksqqlvdqlgaELTAERASSQNREGSRLQLEKQTRDLK 1794
Cdd:COG5022 848 IQKFGRSLKAKKRFSLLKK----ETIYLQSAQRVELAERQLQ-----------ELKIDVKSISSLKLVNLELESEIIELK 912
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1795 AKLQDVEsQARSKLKSSVAALEAKL---REAEEQLEVEsRERQASAKNLRQKEKKLKDLTAQMEDERKQAQDYKDQMEKS 1871
Cdd:COG5022 913 KSLSSDL-IENLEFKTELIARLKKLlnnIDLEEGPSIE-YVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKA 990
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1343958102 1872 SARMKQLKhqleeaeeeaqrvaaarrklqRELDEALEANDALSREVSSLRSKLR 1925
Cdd:COG5022 991 NSELKNFK---------------------KELAELSKQYGALQESTKQLKELPV 1023
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
976-1653 |
6.26e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 976 VKKLEENLLLSEDQNNKLQKERKLLeerladmssNLAEEEEKSKNLSklkskhesmISELEVRLKKEEKTRQDVEKAKRK 1055
Cdd:PRK01156 161 INSLERNYDKLKDVIDMLRAEISNI---------DYLEEKLKSSNLE---------LENIKKQIADDEKSHSITLKEIER 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1056 VEAELVDLQEQQADLQAQLAELRAQLAAKEEelqttqacLDEESRQRGAALKRVRDLEALLAELQEDLeaEKVARGKAEA 1135
Cdd:PRK01156 223 LSIEYNNAMDDYNNLKSALNELSSLEDMKNR--------YESEIKTAESDLSMELEKNNYYKELEERH--MKIINDPVYK 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1136 ARRDLGEELNsLRSELEDsldttaaqqelrvkreqemamLKKAMEDegrsHETQIQELRQKHGQAVEELREHLEQAKKvr 1215
Cdd:PRK01156 293 NRNYINDYFK-YKNDIEN---------------------KKQILSN----IDAEINKYHAIIKKLSVLQKDYNDYIKK-- 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1216 aalEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLndlqlrfSESERQRNELSERVSKMTVELDSVTGLLNEA 1295
Cdd:PRK01156 345 ---KSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYS-------KNIERMSAFISEILKIQEIDPDAIKKELNEI 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1296 EGRNIKLSKEASSISSQLQDAQELLSEETRQKLNLSGRLR------QLEEDKgclmeqleeemeakqaVERQASSLSVQL 1369
Cdd:PRK01156 415 NVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgtTLGEEK----------------SNHIINHYNEKK 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1370 SDLKKRLEELSAAVELLEEGKKRLQRELE-AASGDYEEKAAAYDKLEKSRgrlqQELEDVLMDLdsqrqlvSNLEKKQKK 1448
Cdd:PRK01156 479 SRLEEKIREIEIEVKDIDEKIVDLKKRKEyLESEEINKSINEYNKIESAR----ADLEDIKIKI-------NELKDKHDK 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1449 FDQMLAEERAVSAKSAEER--DRAEAELREKETKVLALMKMLEDKQEALQEAERTVKALRVEMEDLISSKDDVGKSVHDL 1526
Cdd:PRK01156 548 YEEIKNRYKSLKLEDLDSKrtSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENE 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1527 ERAKRGLEAFVEEMKTQMEELEDELQvaedaKLRLEVNSQALRAQHERELQAREEQGEEKRRQLLKQVreleaeleeerk 1606
Cdd:PRK01156 628 ANNLNNKYNEIQENKILIEKLRGKID-----NYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKAL------------ 690
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1343958102 1607 QRTLASAARKKLEGEV---KNTEEQLEAASRGRD-EALKQLRKNQGQLKEL 1653
Cdd:PRK01156 691 DDAKANRARLESTIEIlrtRINELSDRINDINETlESMKKIKKAIGDLKRL 741
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1008-1305 |
6.75e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.03 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1008 SSNLAEEEEKSKNLSKLKSKHESMISELEVRLKKEEKTRQD-----VEKAKRKVEAELVDLQEQQADLQAQLAELRAQLA 1082
Cdd:pfam15905 53 ARKVKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQDkrlqaLEEELEKVEAKLNAAVREKTSLSASVASLEKQLL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1083 AKEEELQTTQACLDEESRQrgaalKRVRDLEALLAELQEDLEAEKVArgkAEAARRDLGEELNSLRSELEDSLDTTAAQQ 1162
Cdd:pfam15905 133 ELTRVNELLKAKFSEDGTQ-----KKMSSLSMELMKLRNKLEAKMKE---VMAKQEGMEGKLQVTQKNLEHSKGKVAQLE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1163 ELRVKREQEMAmlkkamedEGRSHetqiqelrqkhgqaVEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSST 1242
Cdd:pfam15905 205 EKLVSTEKEKI--------EEKSE--------------TEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESL 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1343958102 1243 KQDVEQKKKKVEAQLNDL----QLRFSESERQRNELSERVSKMTVELDSVTGLLNEAEGRNIKLSKE 1305
Cdd:pfam15905 263 KQSLEEKEQELSKQIKDLnekcKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
993-1294 |
7.01e-04 |
|
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: 44.56 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 993 LQKERKLLEERLADMSSNLAEEEEKSKNLSKLKSKHESMISELEVRLKKEEKTR------------QDVEKAKRKVEAEL 1060
Cdd:COG5185 259 VEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATEsleeqlaaaeaeQELEESKRETETGI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1061 VDLQEQQADLQAQLAELRAQLAAKEEELQTTQAcLDEESRQRGAALKRVRDL-EALLAELQEDLEAEKVARGKAEAARRD 1139
Cdd:COG5185 339 QNLTAEIEQGQESLTENLEAIKEEIENIVGEVE-LSKSSEELDSFKDTIESTkESLDEIPQNQRGYAQEILATLEDTLKA 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1140 LGEELNSLRSELEDSLDTTAAQQELRVKREQEMAMLKKAMEDEGRSHETQiqelrqkhgqaveelrEHLEQAKKVRAALE 1219
Cdd:COG5185 418 ADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEE----------------AYDEINRSVRSKKE 481
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1343958102 1220 KAKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVELDSVTGLLNE 1294
Cdd:COG5185 482 DLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNA 556
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1791-1929 |
7.08e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1791 RDLKAKLQDVESQA-----RSKLKSSV---AALEAKLREAEEQL-----EVESRERQASAKNLRQKEKKLKDLTAQMEDE 1857
Cdd:COG2433 346 DAYKNKFERVEKKVppdvdRDEVKARVirgLSIEEALEELIEKElpeeePEAEREKEHEERELTEEEEEIRRLEEQVERL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1858 RKQAQDYKDQMEKSSARMKQLKHQLEEAEEEAQRVAAARRK----------LQRELDEALEANDALSREVSSLRS---KL 1924
Cdd:COG2433 426 EAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREisrldreierLERELEEERERIEELKRKLERLKElwkLE 505
|
....*
gi 1343958102 1925 RRGGG 1929
Cdd:COG2433 506 HSGEL 510
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
842-1336 |
7.58e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.72 E-value: 7.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 842 QVTRQEEEMGQKEEELKAVREAAAKAEADLKDITQKHSQLVEEQAMLEAKLQAEAELYAEAEDMRVRLEAKKQELEEvlh 921
Cdd:pfam15921 445 QMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITK--- 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 922 emearleeeeersisLQQEKKEMEQELQlmeaHIVQEEDARQKLQLEKAAVegRVKKLEENLLLsedqnnklqkerKLLE 1001
Cdd:pfam15921 522 ---------------LRSRVDLKLQELQ----HLKNEGDHLRNVQTECEAL--KLQMAEKDKVI------------EILR 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1002 ERLADMSSNLAEEEEKSKNLSKLKSKHESMISELEVRLkKEEKTRQDVEKAK-RKVEAELVDLQEQQADL-QAQLAELRA 1079
Cdd:pfam15921 569 QQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLEL-QEFKILKDKKDAKiRELEARVSDLELEKVKLvNAGSERLRA 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1080 QLAAKEEelqttqacldeesrqRGAALKRVRDLEALLAELQEDLEAEKvargkaeAARRDLGEELNSLRSELEDSLDTta 1159
Cdd:pfam15921 648 VKDIKQE---------------RDQLLNEVKTSRNELNSLSEDYEVLK-------RNFRNKSEEMETTTNKLKMQLKS-- 703
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1160 AQQELrvkrEQEMAMLKKAMEDEGRSHETQI---QELRQKHGQaVEELREHLEQAKKVRAALEKAKQALEKEAADLSADL 1236
Cdd:pfam15921 704 AQSEL----EQTRNTLKSMEGSDGHAMKVAMgmqKQITAKRGQ-IDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQEL 778
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1237 RALSStkqdveqKKKKVEAQLNDLQlrfseseRQRNELSERVSKMTVELDSVTglLNEAEGRNIKLSKEASSISSQLQ-- 1314
Cdd:pfam15921 779 STVAT-------EKNKMAGELEVLR-------SQERRLKEKVANMEVALDKAS--LQFAECQDIIQRQEQESVRLKLQht 842
|
490 500
....*....|....*....|...
gi 1343958102 1315 -DAQELLSEETRQKLNLSGRLRQ 1336
Cdd:pfam15921 843 lDVKELQGPGYTSNSSMKPRLLQ 865
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1210-1425 |
7.73e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1210 QAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVELDSVT 1289
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1290 GLLNEAEGRNIKLSK--EASSISSQLQDAQeLLSEETRQKLNLsgrLRQLEEDKgclmeqleeemeakQAVERQASSLSV 1367
Cdd:COG3883 93 RALYRSGGSVSYLDVllGSESFSDFLDRLS-ALSKIADADADL---LEELKADK--------------AELEAKKAELEA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1343958102 1368 QLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQEL 1425
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1096-1502 |
8.12e-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: 43.90 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1096 DEESRQR-GAALKRVRDLEAL----------LAELQEDLEAEKVARGKAEAARRDLGEELNSLRSELED-SLDTTAAQQE 1163
Cdd:pfam19220 5 NELLRVRlGEMADRLEDLRSLkadfsqliepIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGlTRRLSAAEGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1164 LrvkreqemamlkKAMEDEGRSHETQIQELRQkhgqAVEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTK 1243
Cdd:pfam19220 85 L------------EELVARLAKLEAALREAEA----AKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1244 QDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVELDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQELlsee 1323
Cdd:pfam19220 149 QAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAE---- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1324 tRQKLnlsgrLRQLEEdkgclmeqleeemeAKQAVERQASSLSVQLSDLKKRLeelsAAVELLEEGKKRLQRELEAASGD 1403
Cdd:pfam19220 225 -RERA-----EAQLEE--------------AVEAHRAERASLRMKLEALTARA----AATEQLLAEARNQLRDRDEAIRA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1404 YEEKAAaydKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKKFDQ---MLAeeRAVSAK-----SAEER-----DRA 1470
Cdd:pfam19220 281 AERRLK---EASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEEraeMLT--KALAAKdaaleRAEERiaslsDRI 355
|
410 420 430
....*....|....*....|....*....|....
gi 1343958102 1471 EAELREKETKVLALMKMLEDKQEALQ--EAERTV 1502
Cdd:pfam19220 356 AELTKRFEVERAALEQANRRLKEELQreRAERAL 389
|
|
| fliD |
PRK08724 |
flagellar filament capping protein FliD; |
956-1226 |
8.13e-04 |
|
flagellar filament capping protein FliD;
Pssm-ID: 236335 [Multi-domain] Cd Length: 673 Bit Score: 44.48 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 956 VQEEDARQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLLEERLADMSSNLAEEEEksknlsklkskhesmisel 1035
Cdd:PRK08724 190 VDAEYGNPLKRFEYKTLEDRVRALEKARAAAQQVIAPLTPEEQKVAPELSDEEGNAIPPAD------------------- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1036 evrlKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTtqACLDEESRQRGAALKRVRDLEAL 1115
Cdd:PRK08724 251 ----QEVAEEIQDAAQIAQQQEATAALAALEEPISAGGATAAAAGQAAIDAAEAK--AYLRPEDRIPGWTETASGTLLDS 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1116 LAELQEDLEAEKVARGKAEAARRDLGEelnslrSELEDSLDTTA-AQQELRVKREQEMAMLKKAMEdEGRSHETQIQELR 1194
Cdd:PRK08724 325 YPEPEEELDEAAIAKAPDVPGWSNTAS------GTLTDSYVTPKeAQAEIEQKLAQEKAQLDAAVE-KGELTPEQAKQIA 397
|
250 260 270
....*....|....*....|....*....|..
gi 1343958102 1195 QKHGQAVEelREHLEQAKKVRAALEKAKQALE 1226
Cdd:PRK08724 398 RAKLEPEE--RERLEKIDKAQAALKQAQSAFD 427
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
939-1057 |
8.46e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 939 QEKKEMEQELQLMEAHIVQEEDARQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLLEERLADMSSNLAEEEEKS 1018
Cdd:COG2433 385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKD 464
|
90 100 110
....*....|....*....|....*....|....*....
gi 1343958102 1019 KNLSKLkskhESMISELEVRLKKEEKTrqdVEKAKRKVE 1057
Cdd:COG2433 465 REISRL----DREIERLERELEEERER---IEELKRKLE 496
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1569-1879 |
8.56e-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: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1569 RAQHERELQAREEQGEEKRRQLLKQVRELEAELEEERKQRTLASAARKKLEGEVKNTEEQLEAASRGRDEALKQ-LRKNQ 1647
Cdd:pfam17380 295 KMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEeIAMEI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1648 GQLKELHReLEEGRAAHKEILASAREAERRCKNLEAE-ILQMQEMLAAAERARKQAETERDElseevaggssgrsllsdE 1726
Cdd:pfam17380 375 SRMRELER-LQMERQQKNERVRQELEAARKVKILEEErQRKIQQQKVEMEQIRAEQEEARQR-----------------E 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1727 KRRLEAKISQLEEELEEEQANVETLNERLRKSQQLVDQLGAELTAE-RASSQNREGSRLQLEKQTRDLKAKLqdVESQAR 1805
Cdd:pfam17380 437 VRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEkRDRKRAEEQRRKILEKELEERKQAM--IEEERK 514
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1343958102 1806 SKLkssvaaLEAKLREAEEQLEVESRERQASAKNLRQKEKKLKDLTAQMEDERKQAQDYKDQMEKSSARMKQLK 1879
Cdd:pfam17380 515 RKL------LEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIV 582
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1488-1675 |
9.15e-04 |
|
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: 9.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1488 LEDKQEALQEAERTVKALRVE--MEDLISSKDDVGKSVHDLERAKRGLEAFVEEMKTQMEELEDELQVAEDAKLRLeVNS 1565
Cdd:COG3206 184 LPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL-LQS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1566 QALRAQHERELQAREEQGEEKRR--------QLLKQVRELEAELEEERKQRTLAS--AARKKLEGEVKNTEEQLEAASrg 1635
Cdd:COG3206 263 PVIQQLRAQLAELEAELAELSARytpnhpdvIALRAQIAALRAQLQQEAQRILASleAELEALQAREASLQAQLAQLE-- 340
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1343958102 1636 rdEALKQLRKNQGQLKELHRELEEGRAAHKEILASAREAE 1675
Cdd:COG3206 341 --ARLAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1041-1255 |
9.21e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.82 E-value: 9.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1041 KEEKTRQDVEKAKRKVEAELVdlqeqqADLQAQLAELRAQLAAKEEELQTTQACLDEESRQRGAALKRVRdlEALLAElQ 1120
Cdd:PRK07735 7 LEDLKKEAARRAKEEARKRLV------AKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAK--AAALAK-Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1121 EDLEAEKVARGKAEAARRDLGEELNSLRSELEDSLDTTAAQQElrvKREQEMAMLKKAMEDEGRSHETQIQELRQKHGQA 1200
Cdd:PRK07735 78 KREGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVT---EEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1343958102 1201 VEELREHLEQAKKVRAALEKAK-QALEKEAADLSADLRALSSTKQDVEQKKKKVEA 1255
Cdd:PRK07735 155 EEEEETDKEKAKAKAAAAAKAKaAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAA 210
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1500-1940 |
1.09e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1500 RTVKALRVEMEDLISSKDDVGKSVHDLERAKRGLEAFVEEMKTQME---ELEDELQVAEDaklRLEVNSQALRAQhEREL 1576
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEaesDLEQDYQAASD---HLNLVQTALRQQ-EKIE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1577 QAREEQgEEKRRQLLKQvreleaeleeerkqrtlaSAARKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQGQLKELHRe 1656
Cdd:PRK04863 352 RYQADL-EELEERLEEQ------------------NEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQT- 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1657 leegRA-AHKEILASAREAERRCKNLEAEILQMQEMLAAAERARKQAETERDELSEEVAGGSSGRSLLsDEKRRLEAKIS 1735
Cdd:PRK04863 412 ----RAiQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQF-EQAYQLVRKIA 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1736 QLEEELEEEQANVETLnERLRKSQQLVDQLG---AEL-TAERASSQNREGSRL----------------QLEKQTRDLKA 1795
Cdd:PRK04863 487 GEVSRSEAWDVARELL-RRLREQRHLAEQLQqlrMRLsELEQRLRQQQRAERLlaefckrlgknlddedELEQLQEELEA 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1796 KLQDVESQarsklKSSVAALEAKLREAEEQLEVESRERQASAKNLRQKEKKLKDLTAQMEDERKQAQDYkdqmekssarM 1875
Cdd:PRK04863 566 RLESLSES-----VSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDV----------T 630
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1343958102 1876 KQLKHQLEEAeeeaqrvaaarRKLQRELDEALEANDALSREVSSLrskLRRGGGE---VLTSGQRVGG 1940
Cdd:PRK04863 631 EYMQQLLERE-----------RELTVERDELAARKQALDEEIERL---SQPGGSEdprLNALAERFGG 684
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1012-1271 |
1.15e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1012 AEEEEKSKNLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTT 1091
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1092 QACLDEESRQRGAALKRVRDLEALLAELQEDLEAEKVARGKAEAARRDLGEELNSLRSELEDSLDTTAAQQELRVKREQE 1171
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1172 MAMLKKAMEDEGRSH-ETQIQELRQKHGQAVEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKK 1250
Cdd:COG4372 166 LAALEQELQALSEAEaEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260
....*....|....*....|.
gi 1343958102 1251 KKVEAQLNDLQLRFSESERQR 1271
Cdd:COG4372 246 EDKEELLEEVILKEIEELELA 266
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
1312-1772 |
1.23e-03 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 43.80 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1312 QLQDAQELLSEETRQKLNLSGRLRQLEEDKGCLMEQLEEEMEAKQAVERQASSLSVQLSDLKKRLEELSAAVELLEEGKK 1391
Cdd:COG4995 6 LLALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1392 RLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSAKSAEERDRAE 1471
Cdd:COG4995 86 ALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1472 AELREKETKVLALMKMLEDKQEALQEAERTVKALRVEMEDLISSKDDVGKSVHDLERAKRGLEAFVEEMKTQMEELEDEL 1551
Cdd:COG4995 166 LALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1552 QVAEDAKLRLEVNSQALRAQHERELQAREEQGEEKRRQLLKQVRELEAELEEERKQRTLASAARKKLEgevkNTEEQLEA 1631
Cdd:COG4995 246 AAAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALA----ALALLLLA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1632 ASRGRDEALKQLRKNQGQLKELHRELEEGRAAHKEILASAREAERRCKNLEAEILQMQEMLAAAERARKQAETERDELSE 1711
Cdd:COG4995 322 ALLLLLAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALL 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1343958102 1712 EVAGGSSGRSLLSDEKRRLEAKISQLEEELEEEQANVETLNERLRKSQQLVDQLGAELTAE 1772
Cdd:COG4995 402 ALAAAQLLRLLLAALALLLALAAYAAARLALLALIEYIILPDRLYAFVQLYQLLIAPIEAE 462
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1561-1874 |
1.23e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 43.86 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1561 LEVNSQALRAQherelQAREEQGEEKRRQllkqvRELEAELEEERKQRTLASAARKKLEGEVKNTEEQLEAASRGRDEAL 1640
Cdd:pfam05667 209 LERNAAELAAA-----QEWEEEWNSQGLA-----SRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1641 KQLRKNQGQLKELHRELEEGRAAHKEILASAREA--------------ERRCKNLEAEILQMQEMLaaaerarkqaeter 1706
Cdd:pfam05667 279 ELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEApaatsspptkveteEELQQQREEELEELQEQL-------------- 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1707 DELSEEVAggssgrsLLSDEKRRLEAKISQLEEELEEEQANVETLNERLRKSQQLVDQLgaeltaerassQNREGSRLQL 1786
Cdd:pfam05667 345 EDLESSIQ-------ELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLL-----------PDAEENIAKL 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1787 EKQTRDLKAKLQDVESQARSKLKSSVAALEAkLREAEEQLEVESRERQASAKNLRQKEKKLKDLTAQMEDERKQAQDYKD 1866
Cdd:pfam05667 407 QALVDASAQRLVELAGQWEKHRVPLIEEYRA-LKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYE 485
|
....*...
gi 1343958102 1867 QMEKSSAR 1874
Cdd:pfam05667 486 RLPKDVSR 493
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1068-1216 |
1.24e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 43.11 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1068 ADLQAQLAELRAQLAAKEEELQTTQACLDEESrQRGAALKRVRDLEALLAELQEDLE-AEKVARGKAEAArrdlgEELNS 1146
Cdd:COG1566 79 TDLQAALAQAEAQLAAAEAQLARLEAELGAEA-EIAAAEAQLAAAQAQLDLAQRELErYQALYKKGAVSQ-----QELDE 152
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1343958102 1147 LRSELEdsldttAAQQELRVKREQ-EMAMLKKAMEDEGRSHETQIQELRqkhgQAVEELREHLEQAkKVRA 1216
Cdd:COG1566 153 ARAALD------AAQAQLEAAQAQlAQAQAGLREEEELAAAQAQVAQAE----AALAQAELNLART-TIRA 212
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1570-1938 |
1.49e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1570 AQHERELQAREEQGEEKRRQLLKQVRELEAEleeerkQRTLASAARK--KLEGEVKNTEEQLEAASRGRD---EAL---K 1641
Cdd:PRK04863 275 MRHANERRVHLEEALELRRELYTSRRQLAAE------QYRLVEMARElaELNEAESDLEQDYQAASDHLNlvqTALrqqE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1642 QLRKNQGQLKELHRELEEGRAAHKEILASAREAERRCKNLEAEILQMQEMLAAAERARKQAETERDELSEEVAGGSSGRS 1721
Cdd:PRK04863 349 KIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1722 LLSD---EKRRLEAKISQLEEELEEEQANVETLNERLRKSQ----------QLVDQLGAELTAERASSQNREgsrlqLEK 1788
Cdd:PRK04863 429 LCGLpdlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQaahsqfeqayQLVRKIAGEVSRSEAWDVARE-----LLR 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1789 QTRDLKAKLQDVEsQARSKLKssvaALEAKLREAEEQLEVESRERQASAKNLrQKEKKLKDLTAQMEDERKQAQDYKDQM 1868
Cdd:PRK04863 504 RLREQRHLAEQLQ-QLRMRLS----ELEQRLRQQQRAERLLAEFCKRLGKNL-DDEDELEQLQEELEARLESLSESVSEA 577
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1869 EKSSARMKQLKHQLeeaeeeaqrvAAARRKLQRELDEALEANDALSRevsslrskLRRGGGEVLTSGQRV 1938
Cdd:PRK04863 578 RERRMALRQQLEQL----------QARIQRLAARAPAWLAAQDALAR--------LREQSGEEFEDSQDV 629
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1356-1902 |
1.65e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 43.59 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1356 QAVERQASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQ----------RELEAASGDYEEKAAAYDKLEKSRGRLQQEL 1425
Cdd:pfam07111 59 QALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEaqameldalaVAEKAGQAEAEGLRAALAGAEMVRKNLEEGS 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1426 EDVLMDLDS--QRQLVSNLEKKQKKFDQML--AEERAVSAKSAEERDRAEA-ELREKETKVLALMKMLEDKQEALQEAER 1500
Cdd:pfam07111 139 QRELEEIQRlhQEQLSSLTQAHEEALSSLTskAEGLEKSLNSLETKRAGEAkQLAEAQKEAELLRKQLSKTQEELEAQVT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1501 TVKALRVEMEDLISS----------KDDVGKSVHDLERAKRGLEAFVEEMKTQMEELEDELQVAEDAKLRLEVNSQALRA 1570
Cdd:pfam07111 219 LVESLRKYVGEQVPPevhsqtweleRQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEP 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1571 QHERELQAREEQGEEKRRQLLKQVREleaeleeerkQRTLASAARKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQGQL 1650
Cdd:pfam07111 299 EFPKKCRSLLNRWREKVFALMVQLKA----------QDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1651 -------KELHREL---EEGRAAHKEILASAREAERRCKN-LEAEILQMQEMLAAAERARKQAETERDELSEEVAGGSSG 1719
Cdd:pfam07111 369 evermsaKGLQMELsraQEARRRQQQQTASAEEQLKFVVNaMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTI 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1720 RSLLSDEKR--RLEAKISQLEEELEEEQANVETLNERLRKSQQLVD---QLGAELTAE---RASSQNrEGSRLQLEKQTR 1791
Cdd:pfam07111 449 KGLMARKVAlaQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDaelQLSAHLIQQevgRAREQG-EAERQQLSEVAQ 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1792 DLKAKLQdvesQARSKLKSSVAALEAKLREAEEQLEVESRERQASAKNLRQKEKKLKD--------LTAQMEDERKQAQD 1863
Cdd:pfam07111 528 QLEQELQ----RAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEkvaevetrLREQLSDTKRRLNE 603
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1343958102 1864 YKDQMEKSSARMKQLKH---------------QLEEAEEEAQRVAAARRKLQRE 1902
Cdd:pfam07111 604 ARREQAKAVVSLRQIQHratqekernqelrrlQDEARKEEGQRLARRVQELERD 657
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1015-1124 |
1.65e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1015 EEKSKNLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQL---------AAKE 1085
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAekeaqqaikEAKK 584
|
90 100 110
....*....|....*....|....*....|....*....
gi 1343958102 1086 EELQTTQAcLDEESRQRGAALKRvRDLEALLAELQEDLE 1124
Cdd:PRK00409 585 EADEIIKE-LRQLQKGGYASVKA-HELIEARKRLNKANE 621
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
955-1092 |
1.70e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 42.73 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 955 IVQEEDARQKLQLEKAavEGRVKKLEENLLLSEDQNNkLQKERKLLEERLADMSSNLAEEEEKSKNLSKLKSKHesMIS- 1033
Cdd:COG1566 73 LARLDPTDLQAALAQA--EAQLAAAEAQLARLEAELG-AEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKG--AVSq 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1343958102 1034 -ELEVRLKKEEKTRQDVEKAKRKVEA--ELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQ 1092
Cdd:COG1566 148 qELDEARAALDAAQAQLEAAQAQLAQaqAGLREEEELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1336-1725 |
1.98e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1336 QLEEDKGCLMEQLEEEMEAKQAVERQASSLSVQLSDLKKRLEELSAAVElleegkkRLQRELEAASGDYEEKAAAYDKLE 1415
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVA-------ELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1416 KSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSAKSAEERDRAEAELREKETKVLALMKMLEDKQEAL 1495
Cdd:pfam07888 108 ASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1496 QEAERTVKALRVEMEDLISS----KDDVGKSVHDLERAKRG---LEAFVEEMKTQMEELEDELQVAEDAKLRL-EVNSQA 1567
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQvlqlQDTITTLTQKLTTAHRKeaeNEALLEELRSLQERLNASERKVEGLGEELsSMAAQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1568 LRAQ---HERELQAREEQGEEKRRQL-LKQVRELEAELEEERKQRTLASAAR-KKLEGEVKNTEEQLEAASRGRDEALKQ 1642
Cdd:pfam07888 268 DRTQaelHQARLQAAQLTLQLADASLaLREGRARWAQERETLQQSAEADKDRiEKLSAELQRLEERLQEERMEREKLEVE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1643 LRK----NQGQLKELHRELEEGRaahkeilASAREAERRCKNLEAEIlqmQEMLAAAERARKQAETERDELSEEVAGGSS 1718
Cdd:pfam07888 348 LGRekdcNRVQLSESRRELQELK-------ASLRVAQKEKEQLQAEK---QELLEYIRQLEQRLETVADAKWSEAALTST 417
|
....*....
gi 1343958102 1719 GR--SLLSD 1725
Cdd:pfam07888 418 ERpdSPLSD 426
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
957-1147 |
2.06e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 957 QEEDARQKLQL-----EKAAVEGRVKKLEENLLLSEDQNNKL--QKERKLLEE--RLADMSSNLAEEE-EKSKNLSKLKS 1026
Cdd:PRK09510 70 QQKSAKRAEEQrkkkeQQQAEELQQKQAAEQERLKQLEKERLaaQEQKKQAEEaaKQAALKQKQAEEAaAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1027 KHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQA-QLAELRAQLAAKEEElqttqaclDEESRQRGAA 1105
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAaAEAKKKAEAEAKKKA--------AAEAKKKAAA 221
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1343958102 1106 LKRVRDLEAlLAELQEDLEAEKVARGKAEAARRDLGEELNSL 1147
Cdd:PRK09510 222 EAKAAAAKA-AAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDL 262
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1476-1643 |
2.07e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 43.09 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1476 EKETKVLALMKMLEDKQEALQEAErtVKALRVEMEDLISSKDDVGKSVHDLERAKRGLEAFVEEMKTQMEELEDELQVAE 1555
Cdd:pfam05667 313 PAATSSPPTKVETEEELQQQREEE--LEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKK 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1556 DAKLRL---EVNSQALRA---QHERELQAREEQGEEKRRQLLKQVRELEAeleeerKQRTLASAARKKLEgEVKNTEEQL 1629
Cdd:pfam05667 391 KTLDLLpdaEENIAKLQAlvdASAQRLVELAGQWEKHRVPLIEEYRALKE------AKSNKEDESQRKLE-EIKELREKI 463
|
170
....*....|....*..
gi 1343958102 1630 EAAS---RGRDEALKQL 1643
Cdd:pfam05667 464 KEVAeeaKQKEELYKQL 480
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1635-1805 |
2.25e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.65 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1635 GRDEALKQLrknQGQLKELHR--ELEEGRAAhkeilasareaerrckNLEAEILQMQEMLAAAErarkqaeTERDELSEE 1712
Cdd:PRK09039 50 GKDSALDRL---NSQIAELADllSLERQGNQ----------------DLQDSVANLRASLSAAE-------AERSRLQAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1713 VAGGSSGRSLLSDEKRRLEAKISQLEEELEEEQANVETLNERLrksQQLVDQLGAELTAERASSQNREGSRLQLEKQTRD 1792
Cdd:PRK09039 104 LAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI---AALRRQLAALEAALDASEKRDRESQAKIADLGRR 180
|
170
....*....|....
gi 1343958102 1793 LKAKL-QDVESQAR 1805
Cdd:PRK09039 181 LNVALaQRVQELNR 194
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1046-1325 |
2.40e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 43.28 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1046 RQDVEKAKRKVEAElVDLQEQQADLQAQLAELRAQLAAKEEELQTTQACldeESRQRGAAlkrvRDLEALLAELQEDL-- 1123
Cdd:NF041483 519 RRQAEETLERTRAE-AERLRAEAEEQAEEVRAAAERAARELREETERAI---AARQAEAA----EELTRLHTEAEERLta 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1124 --EAEKVARGKAEAARRDLGEELNSLRSELEDSLDTTAAQQELRVKR-EQEMAMLKKAMEDEGrshETQIQELRQKHGQA 1200
Cdd:NF041483 591 aeEALADARAEAERIRREAAEETERLRTEAAERIRTLQAQAEQEAERlRTEAAADASAARAEG---ENVAVRLRSEAAAE 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1201 VEELR-EHLEQAKKVRAALEKAKQALEKEAADlsadlrALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVs 1279
Cdd:NF041483 668 AERLKsEAQESADRVRAEAAAAAERVGTEAAE------ALAAAQEEAARRRREAEETLGSARAEADQERERAREQSEEL- 740
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1343958102 1280 kmtveLDSVTGLLNEAEGRNIKLSKEASSISSQLQDAQELLSEETR 1325
Cdd:NF041483 741 -----LASARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVR 781
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1043-1154 |
2.42e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 42.34 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1043 EKTRQDVEKAKRKVEA--ELVDLQEQQADLQAQLAELRAQLAAKEEELQ----------TTQACLDEESRQRGAALKRVR 1110
Cdd:COG1566 86 AQAEAQLAAAEAQLARleAELGAEAEIAAAEAQLAAAQAQLDLAQRELEryqalykkgaVSQQELDEARAALDAAQAQLE 165
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1343958102 1111 DLEALLAELQEDLeAEKVARGKAEAARRDLGEELNSLRSELEDS 1154
Cdd:COG1566 166 AAQAQLAQAQAGL-REEEELAAAQAQVAQAEAALAQAELNLART 208
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1373-1732 |
2.61e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.52 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1373 KKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKsrgrLQQEL-EDVLMDLDSQRQLVSNLEKKQKKFDQ 1451
Cdd:PRK04778 104 KHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKD----LYRELrKSLLANRFSFGPALDELEKQLENLEE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1452 MLAEerAVSAKSAEERDRAEAELREKETKVLALMKMLEDKQEALQEAERTVKAlrvEMEDLISSKDDVGKSVHDLEraKR 1531
Cdd:PRK04778 180 EFSQ--FVELTESGDYVEAREILDQLEEELAALEQIMEEIPELLKELQTELPD---QLQELKAGYRELVEEGYHLD--HL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1532 GLEAFVEEMKTQMEELED-----ELQVAEDAKLRLEVNSQALRAQHERELQAR---EEQGEEKRRQLLKQvreleaeleE 1603
Cdd:PRK04778 253 DIEKEIQDLKEQIDENLAlleelDLDEAEEKNEEIQERIDQLYDILEREVKARkyvEKNSDTLPDFLEHA---------K 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1604 ERKQRTLASAARKKLEGEVKNTEEQLeaaSRGRDEALKQLRKnqgQLKELHRELEEGRAAHKEILASAREAERRCKNLEA 1683
Cdd:PRK04778 324 EQNKELKEEIDRVKQSYTLNESELES---VRQLEKQLESLEK---QYDEITERIAEQEIAYSELQEELEEILKQLEEIEK 397
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1343958102 1684 EILQMQEMLAAAERARKQAETERDELseevaggssgRSLLSDEKRRLEA 1732
Cdd:PRK04778 398 EQEKLSEMLQGLRKDELEAREKLERY----------RNKLHEIKRYLEK 436
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1581-1865 |
2.64e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1581 EQGEEKRRQLLKQVRELEAELEEERKQRTLASAARKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQGQLKELHRELEEG 1660
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1661 RAAHKEILASAREAERRCKNLEAEILQMQEMLAAAERARKQAETERDELSEEVAGGSSGRSLLSDEKRRLEAKISQLEEE 1740
Cdd:COG4372 114 QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEAN 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1741 LEEEQANVETLNERLRKSQQLVDQLGAELTAERASSQNREGSRLQLEKQTRDLKAKLQDVESQARSKLKSSVAALEAKLR 1820
Cdd:COG4372 194 RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDT 273
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1343958102 1821 EAEEQLEVESRERQASAKNLRQKEKKLKDLTAQMEDERKQAQDYK 1865
Cdd:COG4372 274 EEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALL 318
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
971-1196 |
2.79e-03 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 41.93 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 971 AVEGRVKKLEENLLLSEDQNNKLQKERKLLEERLADMSSNLAEEEEKSKNLSKLKSKHESMISE-------LEVRLKK-E 1042
Cdd:pfam04849 98 VLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSLHgcvqldaLQEKLRGlE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1043 EKTRQDVEKAKR-KVEAELVDLQEQQ--ADLQAQLAELRAQLAAKEEELQTtqaCLDEESRQRgaalkrvRDLEALLAEL 1119
Cdd:pfam04849 178 EENLKLRSEASHlKTETDTYEEKEQQlmSDCVEQLSEANQQMAELSEELAR---KMEENLRQQ-------EEITSLLAQI 247
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1343958102 1120 QeDLEaekvARGKAEAARRdlgEELNS-LRSELEDSLDTTAAQQELRVKREQEMAMLKKAMEdegrshetQIQELRQK 1196
Cdd:pfam04849 248 V-DLQ----HKCKELGIEN---EELQQhLQASKEAQRQLTSELQELQDRYAECLGMLHEAQE--------ELKELRKK 309
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
857-1087 |
2.87e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 857 LKAVREAAAKAEADLKDITQKHSQLVEEQAMLEAKLQAEAELYAEAEDMRVRLEAKKQELEEVLHEMEARLEEEEERSIS 936
Cdd:TIGR02169 800 LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 937 LQQEKKEMEQElqlmeahivqeedaRQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLLEERLADMSSNLAEEEE 1016
Cdd:TIGR02169 880 LESRLGDLKKE--------------RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1343958102 1017 KSKNLSKLKsKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEE 1087
Cdd:TIGR02169 946 IPEEELSLE-DVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
996-1200 |
2.93e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 43.00 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 996 ERKLLEERLADMssnlaEEEEKSKNLSklkskhESMISELEVRLKKEEKTRQDVEKAKRKVEaELVDLQEQQADLQAQLA 1075
Cdd:PLN03188 1046 EKKLEQERLRWT-----EAESKWISLA------EELRTELDASRALAEKQKHELDTEKRCAE-ELKEAMQMAMEGHARML 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1076 ELRAQLAAKEEELQTTQACLDE--ESRQRGAALKRVRDLEA-LLAELQEDLEAEKVARgkaEAARRDLGEELNSLRSELE 1152
Cdd:PLN03188 1114 EQYADLEEKHIQLLARHRRIQEgiDDVKKAAARAGVRGAESkFINALAAEISALKVER---EKERRYLRDENKSLQAQLR 1190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1343958102 1153 DSLDTTAAQQELRVK-REQEMAML---KKAMEDE-------------GRSHETQIQELRQKHGQA 1200
Cdd:PLN03188 1191 DTAEAVQAAGELLVRlKEAEEALTvaqKRAMDAEqeaaeaykqidklKRKHENEISTLNQLVAES 1255
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1430-1594 |
3.01e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1430 MDLDSQRQLV--SNLEKKQKKFDQMLAEERAVSAKSAEERDRAEAELREKETKVLALMKMLEDKQEALQEAERTVKALRV 1507
Cdd:COG1579 1 AMPEDLRALLdlQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1508 EMEDLISSKD--DVGKSVHDLERAKRGLEAFVEEMKTQMEELEDELQVAEDAKLRLEVNSQALRAQHER---ELQAREEQ 1582
Cdd:COG1579 81 QLGNVRNNKEyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEelaELEAELEE 160
|
170
....*....|..
gi 1343958102 1583 GEEKRRQLLKQV 1594
Cdd:COG1579 161 LEAEREELAAKI 172
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1038-1260 |
3.04e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.10 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1038 RLKKEEKTRQDVEKAKRKVEAELVD-LQEQQADLQAQLAELRAQ-LAAKEEELQTTQACLDEESRQRGAALKRVRDLEA- 1114
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEeLQQKQAAEQERLKQLEKErLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAa 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1115 ---------LLAELQEDLEAEKVARGKAEAarrdlgeelnslrseledsldttAAQQELRVKREQEMAMLKKAMEDEGRs 1185
Cdd:PRK09510 146 kakaeaeakRAAAAAKKAAAEAKKKAEAEA-----------------------AKKAAAEAKKKAEAEAAAKAAAEAKK- 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1343958102 1186 hetqiqelrqkhgQAVEELREHLEQAKKVRAALEkAKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDL 1260
Cdd:PRK09510 202 -------------KAEAEAKKKAAAEAKKKAAAE-AKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDL 262
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1073-1269 |
3.28e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1073 QLAELRAQLAAKEEEL----QTTQACLDEESRQRGAALKRVRDL------------EALLAELQEDLEAEKVARGKAEAA 1136
Cdd:PRK11448 40 QFGEALAKHIAALLGIyeppCENQHDLLRRLGKEGFLPDEILDVfhklrkignkavHEFHGDHREALMGLKLAFRLAVWF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1137 RRDLG-------------EELNSLRSELEDSLDTTAAQQELRVKREQEMAMLKKAMEDEGRSHETQIQELRQKhgqaVEE 1203
Cdd:PRK11448 120 HRTYGkdwdfkpgpfvppEDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEK----QQE 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1343958102 1204 LREHLEQAKKVRAALEKAKQALEKEAADlsadlRALSSTKQDVEQKKKKVEAQLND-------LQLRFSESER 1269
Cdd:PRK11448 196 LEAQLEQLQEKAAETSQERKQKRKEITD-----QAAKRLELSEEETRILIDQQLRKagweadsKTLRFSKGAR 263
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1199-1463 |
3.29e-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: 42.51 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1199 QAVEELREHLEQAKKVRAALEkakqalEKEAADlsADLRALSSTKQDVEQKKKKVEAQL--NDLQLRFSESERQRNELSE 1276
Cdd:NF012221 1542 QQADAVSKHAKQDDAAQNALA------DKERAE--ADRQRLEQEKQQQLAAISGSQSQLesTDQNALETNGQAQRDAILE 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1277 RVSKMTVELDSVTGLLNeaegrniklskeasSISSQLQDAQElLSEETRQKLN---LSGRLRQLEEDKgclmeqleeeME 1353
Cdd:NF012221 1614 ESRAVTKELTTLAQGLD--------------ALDSQATYAGE-SGDQWRNPFAgglLDRVQEQLDDAK----------KI 1668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1354 AKQAVERQASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAayDKLEKsRGRLQQEledvlmdlD 1433
Cdd:NF012221 1669 SGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKD--DALAK-QNEAQQA--------E 1737
|
250 260 270
....*....|....*....|....*....|
gi 1343958102 1434 SQRQLVSNLEKKQKKFDQMLAEERAVSAKS 1463
Cdd:NF012221 1738 SDANAAANDAQSRGEQDASAAENKANQAQA 1767
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1539-1923 |
3.65e-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: 42.42 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1539 EMKTQMEELEDELQVAE----DAKLRLEVNSQALRAQHERE-------------LQAREEQGEEKRRQLLKQVREleael 1601
Cdd:pfam05557 6 ESKARLSQLQNEKKQMElehkRARIELEKKASALKRQLDREsdrnqelqkrirlLEKREAEAEEALREQAELNRL----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1602 eeerKQRTLASAARKKLEGEVKNTE-EQLEAASRGRDEALK-QLRKNQGQLKELHRELEEGRAAHKEILASAREAERRCK 1679
Cdd:pfam05557 81 ----KKKYLEALNKKLNEKESQLADaREVISCLKNELSELRrQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1680 NLEAEI----------------LQMQEMLAAAERARKQA-------ETERDELSEEVAGGSSGR---SLLSDEKRRLEAK 1733
Cdd:pfam05557 157 NLEKQQsslaeaeqrikelefeIQSQEQDSEIVKNSKSElaripelEKELERLREHNKHLNENIenkLLLKEEVEDLKRK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1734 ISQLEEELEEEqANVETLNERLRKSQQLVDQLGAELTAERASSQNREGSRLQLEKQTRDLKAKLQDVESQARSkLKSSVA 1813
Cdd:pfam05557 237 LEREEKYREEA-ATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQ-LEKARR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1814 ALEAKLREAEEQLEVESRERQASAKNLRQKEKKLKDLTAQMEDERKQAQDYKDQM------EKSSARMKQLKHQLEEAEE 1887
Cdd:pfam05557 315 ELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKELtmsnysPQLLERIEEAEDMTQKMQA 394
|
410 420 430
....*....|....*....|....*....|....*.
gi 1343958102 1888 EAQRVAAARRKLQRELDEALEANDALSREVSSLRSK 1923
Cdd:pfam05557 395 HNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQ 430
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1114-1500 |
3.69e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.25 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1114 ALLAELQEDLEAEKVARGKAEAARRDLGEELNS-----LRSELEDSLDTTAAQQELRVKREQEMAMlkKAMEDEGRSHET 1188
Cdd:COG5185 183 GLTLGLLKGISELKKAEPSGTVNSIKESETGNLgsestLLEKAKEIINIEEALKGFQDPESELEDL--AQTSDKLEKLVE 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1189 QIQELRQ-KHGQAVEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQD--------VEQKKKKVEAQLND 1259
Cdd:COG5185 261 QNTDLRLeKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLaaaeaeqeLEESKRETETGIQN 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1260 LQlrfSESERQRNELSERVSKMTVELDSVTGLLNEAegrniKLSKEASSISSQLqdaqellsEETRQKLNlsgrlrqlee 1339
Cdd:COG5185 341 LT---AEIEQGQESLTENLEAIKEEIENIVGEVELS-----KSSEELDSFKDTI--------ESTKESLD---------- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1340 dkgclmeqleeemEAKQAVERQASSLSVQLSDLKKRLEELSaavelleegkKRLQRELEAASGDYEEKAAAYDKLEKSRG 1419
Cdd:COG5185 395 -------------EIPQNQRGYAQEILATLEDTLKAADRQI----------EELQRQIEQATSSNEEVSKLLNELISELN 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1420 RLQQELEDVLMDLDSQRQLVSNLEKKQKKFD------QMLAEERAVSAKSAEERDRAEAEL---REKETKVLALMKMLED 1490
Cdd:COG5185 452 KVMREADEESQSRLEEAYDEINRSVRSKKEDlneeltQIESRVSTLKATLEKLRAKLERQLegvRSKLDQVAESLKDFMR 531
|
410
....*....|
gi 1343958102 1491 KQEALQEAER 1500
Cdd:COG5185 532 ARGYAHILAL 541
|
|
| IFT57 |
pfam10498 |
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ... |
1205-1294 |
3.81e-03 |
|
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles found at the periphery of cells of diverse organizms. Intra-flagellar transport (IFT) is required for the assembly and maintenance of eukaryotic cilia and flagella, and consists of the bidirectional movement of large protein particles between the base and the distal tip of the organelle. IFT particles contain multiple copies of two distinct protein complexes, A and B, which contain at least 6 and 11 protein subunits. IFT57 is part of complex B but is not, however, required for the core subunits to stay associated. This protein is known as Huntington-interacting protein-1 in humans.
Pssm-ID: 463118 [Multi-domain] Cd Length: 360 Bit Score: 41.86 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1205 REHLEQAKK----VRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSK 1280
Cdd:pfam10498 221 RAHLEQMKQhkksIEESLPDTKSQLDKLHTDISKTLEKIESREKYINSQLEPLIQEYREAQDELSEVQEKYKQLSEGVTE 300
|
90
....*....|....
gi 1343958102 1281 MTVELDSVTGLLNE 1294
Cdd:pfam10498 301 RTRELAEITEELEK 314
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1111-1568 |
3.83e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.15 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1111 DLEALLAELQEDLEAEKVArgKAEAARRDLGEELNSLRSELEDSLDttaAQQELRVKREQEMAMLKKAMEDEGRSHETqI 1190
Cdd:pfam06160 64 DIEELLFEAEELNDKYRFK--KAKKALDEIEELLDDIEEDIKQILE---ELDELLESEEKNREEVEELKDKYRELRKT-L 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1191 QELRQKHGQAVEELREHLEQAKKVRAALE---------KAK---QALEKEAADLSADLRALsstKQDVEQKKKKVEAQLN 1258
Cdd:pfam06160 138 LANRFSYGPAIDELEKQLAEIEEEFSQFEeltesgdylEARevlEKLEEETDALEELMEDI---PPLYEELKTELPDQLE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1259 DLQ------------LRFSESERQRNELSERVSKMTVELDSVTglLNEAEGRNiklskeaSSISSQLQDAQELLSEEtrq 1326
Cdd:pfam06160 215 ELKegyremeeegyaLEHLNVDKEIQQLEEQLEENLALLENLE--LDEAEEAL-------EEIEERIDQLYDLLEKE--- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1327 klnlsgrlrqleedkgclmeqleeeMEAKQAVErqasslsvqlsdlkKRLEELSAAVELLEEGKKRLQRELEAASGDY-- 1404
Cdd:pfam06160 283 -------------------------VDAKKYVE--------------KNLPEIEDYLEHAEEQNKELKEELERVQQSYtl 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1405 -EEKAAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEeraVSAKSAEERDRAEAeLREKETKVLa 1483
Cdd:pfam06160 324 nENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEE---IEEEQEEFKESLQS-LRKDELEAR- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1484 lmKMLEDKQEALQEAERTVKALRVEM--EDLISSKDDVGKSVHDLERakrgleaFVEEMKTQMEELEDELQVAEDAKLRL 1561
Cdd:pfam06160 399 --EKLDEFKLELREIKRLVEKSNLPGlpESYLDYFFDVSDEIEDLAD-------ELNEVPLNMDEVNRLLDEAQDDVDTL 469
|
....*..
gi 1343958102 1562 EVNSQAL 1568
Cdd:pfam06160 470 YEKTEEL 476
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
963-1394 |
3.89e-03 |
|
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: 42.35 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 963 QKLQLEKAAVEGRVKKLE---ENLLLSEDQNNKLQKERKLLEERLADMSS-NLAEEEEKSKNL-SKLKSKHESMISELEV 1037
Cdd:TIGR01612 1229 EKIDEEKKKSEHMIKAMEayiEDLDEIKEKSPEIENEMGIEMDIKAEMETfNISHDDDKDHHIiSKKHDENISDIREKSL 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1038 RLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELrAQL--AAKEEELQTTQACLDEESRQRGAALKRVRD---- 1111
Cdd:TIGR01612 1309 KIIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEI-ANIynILKLNKIKKIIDEVKEYTKEIEENNKNIKDeldk 1387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1112 LEALLAELQEDLEAEKvARGKAEAA--RRDLGEELNSLRsELEDSLDTTAAQQELRVKREQE----MAMLKKAME--DEG 1183
Cdd:TIGR01612 1388 SEKLIKKIKDDINLEE-CKSKIESTldDKDIDECIKKIK-ELKNHILSEESNIDTYFKNADEnnenVLLLFKNIEmaDNK 1465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1184 RSHETQIQE--LRQKHGQAVEELREHLEQAKKVRAALEKAKQALEK----------EAADLSADLRALS------STKQD 1245
Cdd:TIGR01612 1466 SQHILKIKKdnATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKnkelfeqykkDVTELLNKYSALAiknkfaKTKKD 1545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1246 VEQKKKKVEAQLNDLQLRFSESERQRNELSERvsKMTVELDSvtgllneaeGRNIKLSKEASSISSQLQDAQELLSEETR 1325
Cdd:TIGR01612 1546 SEIIIKEIKDAHKKFILEAEKSEQKIKEIKKE--KFRIEDDA---------AKNDKSNKAAIDIQLSLENFENKFLKISD 1614
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1343958102 1326 QKLNLSGRLRQLEedkgclmeqleeemeakqAVERQASSLSV-----QLSDLKKRLEELSAAVELLEEGKKRLQ 1394
Cdd:TIGR01612 1615 IKKKINDCLKETE------------------SIEKKISSFSIdsqdtELKENGDNLNSLQEFLESLKDQKKNIE 1670
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
936-1199 |
4.16e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 42.24 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 936 SLQQEKKEMEQELQLmeaHIVQEEDARQKL-QLEK--AAVEGR---VK----KLEENLLLSEDQNNKLQKERKLLEERLA 1005
Cdd:pfam15818 110 SLQKKVSEMEQKLQL---HLLAKEDHHKQLnEIEKyyATITGQfglVKenhgKLEQNVQEAIQLNKRLSALNKKQESEIC 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1006 DMSSNL---AEEEEKSKNLSKLKSKHESM--------ISELEVRLKKE----EKTRQDVEKAKRKVEAELVDLQEQQADL 1070
Cdd:pfam15818 187 SLKKELkkvTSDLIKSKVTCQYKMGEENInltikeqkFQELQERLNMElelnKKINEEITHIQEEKQDIIISFQHMQQLL 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1071 QAQL---AELRAQLAAKEEELQTTQAclDEEsRQRgaalKRVRDLEALLAELQEdlEAEKvARGKAEAARRDLGEELNSL 1147
Cdd:pfam15818 267 QQQTqanTEMEAELKALKENNQTLER--DNE-LQR----EKVKENEEKFLNLQN--EHEK-ALGTWKKHVEELNGEINEI 336
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1343958102 1148 RSELEDSLDTTAAQQELRVKREQEmamlKKAMEDEgrsHETQIQELRQKHGQ 1199
Cdd:pfam15818 337 KNELSSLKETHIKLQEHYNKLCNQ----KKFEEDK---KFQNVPEVNNENSE 381
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1681-1827 |
4.37e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 41.64 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1681 LEAEILQMQEMLAAAERARKQAETERDELSEEVAGGSSGRSL-------LSDEKRRLEAKISQLEEELEEEQANVETLNE 1753
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDydgataqLRAAQAAVKAAQAQLAQAQIDLARRRVLAPI 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1343958102 1754 RLRKSQQLVDQlGAELTAERASSQNREGSRLQLEKQTRDLKAKLQDVESQARSKLKSSVAALEAKLREAEEQLE 1827
Cdd:pfam00529 136 GGISRESLVTA-GALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1468-1926 |
4.51e-03 |
|
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: 42.13 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1468 DRAEAELREKETKVLALMKMLEDKQEALQEAERTVKALRVE---MEDL----ISSKDDVGkSVHDLERAKRG-------- 1532
Cdd:pfam12128 151 DRTLLGRERVELRSLARQFALCDSESPLRHIDKIAKAMHSKegkFRDVksmiVAILEDDG-VVPPKSRLNRQqvehwird 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1533 --LEAFVEEMKTQMEELEDELQVAEDAKLRLEVNSQALRA---QHERELQAREEQGEEKRRQLLKQVRELEAELEEERKQ 1607
Cdd:pfam12128 230 iqAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSdetLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1608 RTLASAARKKLEGEVKNTEEQLEAAsrgRDEALKQLRKNQGQLKELHRELEEGRAAHKEILASAREAERRCKNLEAEILQ 1687
Cdd:pfam12128 310 LSAADAAVAKDRSELEALEDQHGAF---LDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1688 ------------------MQEMLAAAERA---------RKQAETERDELSEEVAGGSSGRSLL----------SDEKRRL 1730
Cdd:pfam12128 387 qnnrdiagikdklakireARDRQLAVAEDdlqaleselREQLEAGKLEFNEEEYRLKSRLGELklrlnqatatPELLLQL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1731 EAK---ISQLEEELEEEQANVETLNERLRKSQQLVDQLGAELTAERASSQNREGSRLQLEKQT----------------- 1790
Cdd:pfam12128 467 ENFderIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLfpqagtllhflrkeapd 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1791 -RDLKAKLQDVESQARSKLKSSV------------------------------AALEAKLREAEEQLEVESRERQASAKN 1839
Cdd:pfam12128 547 wEQSIGKVISPELLHRTDLDPEVwdgsvggelnlygvkldlkridvpewaaseEELRERLDKAEEALQSAREKQAAAEEQ 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1840 LRQKEKKLKDLTAQMEDERKQAQDYKDQMEKSSARMKQLKHQLEEAEEEAQRVAAARRK--------LQRELDEALEAND 1911
Cdd:pfam12128 627 LVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNsleaqlkqLDKKHQAWLEEQK 706
|
570
....*....|....*
gi 1343958102 1912 ALSREVSSLRSKLRR 1926
Cdd:pfam12128 707 EQKREARTEKQAYWQ 721
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
990-1250 |
4.81e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 990 NNKLQKERKLLEERLADMSSNLAEEEEKSKNLSKLKSKHESMISELEVRLKKEEKTRQDVEKAkrkveaeLVDLQEQQAD 1069
Cdd:PHA02562 194 QQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAA-------LNKLNTAAAK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1070 LQAQLAELrAQLAAKEEELQTTQACLDEESRQRGaalkRVRDLEALLAELQEDLEAEKVARgkaeaarrdlgEELNSLRS 1149
Cdd:PHA02562 267 IKSKIEQF-QKVIKMYEKGGVCPTCTQQISEGPD----RITKIKDKLKELQHSLEKLDTAI-----------DELEEIMD 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1150 ELedsLDTTAAQQELRVKreqemamlkkamedegrshetqiqeLRQKHGQAVEELRehleQAKKVRAALEKAKQAL---E 1226
Cdd:PHA02562 331 EF---NEQSKKLLELKNK-------------------------ISTNKQSLITLVD----KAKKVKAAIEELQAEFvdnA 378
|
250 260
....*....|....*....|....
gi 1343958102 1227 KEAADLSADLRALSSTKQDVEQKK 1250
Cdd:PHA02562 379 EELAKLQDELDKIVKTKSELVKEK 402
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1650-1926 |
4.84e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1650 LKELHRELEEGRAAHKEILASAREAERRCKNLEAEilqmqemLAAAERARKQAETERDELSEEVAGgssgrslLSDEKRR 1729
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKE-------LEEVLREINEISSELPELREELEK-------LEKEVKE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1730 LEA---KISQLEEELEEEQANVETLNERLRksqqlvdqlgaeltaerassqnregsrlQLEKQTRDLKAKLQDVESQA-R 1805
Cdd:PRK03918 233 LEElkeEIEELEKELESLEGSKRKLEEKIR----------------------------ELEERIEELKKEIEELEEKVkE 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1806 SKLKSSVAALEAKLREAEEQLEVESRERQASAKNLRQKEKKLKDLTAQMEDERKQAQDYKDQMEKSSARMKQLKHQLEEA 1885
Cdd:PRK03918 285 LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELY 364
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1343958102 1886 EEEAQRVAAARR-----------KLQRELDEALEANDALSREVSSLRSKLRR 1926
Cdd:PRK03918 365 EEAKAKKEELERlkkrltgltpeKLEKELEELEKAKEEIEEEISKITARIGE 416
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1148-1658 |
5.00e-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: 41.65 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1148 RSELEDSLDTTAAQQELRVKREQEMamlkkamedegrshETQIQELRQKHGQAVEELREHLEQAKKVRAALEKAKQaLEK 1227
Cdd:pfam05557 29 RIELEKKASALKRQLDRESDRNQEL--------------QKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNK-KLN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1228 EAADLSADLRALSSTKQDvEQKKKKVEAQLNDLQLRFSESERQRnelservskmtveldsvtglLNEAEGRNIKLSKEAS 1307
Cdd:pfam05557 94 EKESQLADAREVISCLKN-ELSELRRQIQRAELELQSTNSELEE--------------------LQERLDLLKAKASEAE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1308 SISSQLQDAQELLSEETRQKLNLSGRLRQLEEDKgclmeQLEEEMEAKQAVERQASSLSVQLSDLKKRLEELSAAVELLE 1387
Cdd:pfam05557 153 QLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDS-----EIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1388 EGKKRLQRELEAASGDYEEKAAAYDKLEKsrgrLQQELED-VLMDLDSQRQLVSNlEKKQKKFDQMLAEERAVSAK--SA 1464
Cdd:pfam05557 228 EEVEDLKRKLEREEKYREEAATLELEKEK----LEQELQSwVKLAQDTGLNLRSP-EDLSRRIEQLQQREIVLKEEnsSL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1465 EERDRA-EAELREKETKVLALMKMLEDKQEALQEAERTVKAL----------RVEMEDLISSKDD---VGKSVHDLERAK 1530
Cdd:pfam05557 303 TSSARQlEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLqrrvllltkeRDGYRAILESYDKeltMSNYSPQLLERI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1531 RGLEAFVEEMKTQMEELEDELQVAEDaklrlEVNSQALRAQH-ERELQareeqgeekrrqllkqvreleaeleEERKQRT 1609
Cdd:pfam05557 383 EEAEDMTQKMQAHNEEMEAQLSVAEE-----ELGGYKQQAQTlERELQ-------------------------ALRQQES 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1343958102 1610 LAsaarkklegEVKNTEEQLEAASRGRDEALKQLRKNQGQLKELHRELE 1658
Cdd:pfam05557 433 LA---------DPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELE 472
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
935-1281 |
5.33e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 935 ISLQQEKKEMEQELQLMEAHIVQEEDARQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLLEERLADMSSNLAEE 1014
Cdd:COG4372 13 LSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1015 EEKSKNLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEEL----QT 1090
Cdd:COG4372 93 QAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELaaleQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1091 TQACLDEESRQRGAALKRVRDLEALLAELQEDLEAEKVARGKAEAARRDLGEELNSLRSELEDSLDTTAAQQELRVKREQ 1170
Cdd:COG4372 173 LQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1171 EMAMLKKAMEDEGRSHETQIQElRQKHGQAVEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKK 1250
Cdd:COG4372 253 EEVILKEIEELELAILVEKDTE-EEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELA 331
|
330 340 350
....*....|....*....|....*....|.
gi 1343958102 1251 KKVEAQLNDLQLRFSESERQRNELSERVSKM 1281
Cdd:COG4372 332 LAILLAELADLLQLLLVGLLDNDVLELLSKG 362
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1606-1861 |
5.33e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1606 KQRTLASAARKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQGQLKELHRELEEGRAAHKEILASAREAERRCKNLEAEI 1685
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1686 LQMQEMLAAAERARKQAETERDELSEEVAGGSSGRSLLSDEKRRLEAKISQLEEELEEEQANVETLNERLRKSQQLVDQL 1765
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1766 GAELTAERASSQNREGSRLQLE-KQTRDLKAKLQDVESQARSKLKSSVAALEAKLREAEEQLEVESRERQASAKNLRQKE 1844
Cdd:COG4372 170 EQELQALSEAEAEQALDELLKEaNRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
250
....*....|....*..
gi 1343958102 1845 KKLKDLTAQMEDERKQA 1861
Cdd:COG4372 250 ELLEEVILKEIEELELA 266
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1075-1316 |
5.33e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 41.86 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1075 AELRAQlaakEEELQttQAcldEESRQRgaalkrvrdLEALLAELQEDlEAEKVARGKAEAARRdlgeelnslRSELEDS 1154
Cdd:PRK05035 436 AEIRAI----EQEKK--KA---EEAKAR---------FEARQARLERE-KAAREARHKKAAEAR---------AAKDKDA 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1155 LDTTAAqqelRVKREQEMAMLKKAMEDEGRSHETQIQELRQKHGQAVEELREHLEQA-------KKVRAALEKAKQaleK 1227
Cdd:PRK05035 488 VAAALA----RVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAaaadpkkAAVAAAIARAKA---K 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1228 EAADLSADlralSSTKQDVEQKKKKVEAQLNDLQLRFSESERQRNELSERVSKMTVELDSVTGLLNEAEGRniKLSKEAS 1307
Cdd:PRK05035 561 KAAQQAAN----AEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAK--KAEQQAN 634
|
....*....
gi 1343958102 1308 SISSQLQDA 1316
Cdd:PRK05035 635 AEPEEPVDP 643
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1362-1499 |
5.67e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1362 ASSLSVQLSDLKKRLEELSAAVELLEEGKKRLQRELEAASgdyEEKAAaydKLEKSRGRLQQELEDVLMDLDSQRQLVSN 1441
Cdd:COG0542 399 AARVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEAS---FERLA---ELRDELAELEEELEALKARWEAEKELIEE 472
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1343958102 1442 LEKKQKKFDQMLAEERAVSAKSAEERDRAEAELREKETKVLA--------------LMKMLEDKQEALQEAE 1499
Cdd:COG0542 473 IQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTEediaevvsrwtgipVGKLLEGEREKLLNLE 544
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
987-1448 |
5.78e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.13 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 987 EDQNNKLQKERKLLEERLADMSSNLAEEEEKSKNLSKLK------SKHESMISELEVRLKKEEKTRQDVEKAKRKVEAEL 1060
Cdd:PTZ00440 1119 NKQTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDITLNevneieIEYERILIDHIVEQINNEAKKSKTIMEEIESYKKD 1198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1061 VDL------QEQQADLQ----AQLAELRAQLAAKEEELQTTQACLDEESRqrgaALKRVRDLEALLAELQEDLEAEKVAR 1130
Cdd:PTZ00440 1199 IDQvkknmsKERNDHLTtfeyNAYYDKATASYENIEELTTEAKGLKGEAN----RSTNVDELKEIKLQVFSYLQQVIKEN 1274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1131 GKAEAARRDLGE-----ELNSLRSELEDSLDTTAAQQEL----RVKREQEMAMLKKAMED--EGRSHETQIQElRQKHGQ 1199
Cdd:PTZ00440 1275 NKMENALHEIKNmyeflISIDSEKILKEILNSTKKAEEFsndaKKELEKTDNLIKQVEAKieQAKEHKNKIYG-SLEDKQ 1353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1200 AVEELR-------EHLEQAKKVRAALEKAKQALEKEAADLSADLRALSS----TKQDVEQKKKKVEAQLNDLQLRFSESE 1268
Cdd:PTZ00440 1354 IDDEIKkieqikeEISNKRKEINKYLSNIKSNKEKCDLHVRNASRGKDKidflNKHEAIEPSNSKEVNIIKITDNINKCK 1433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1269 RQRNELSERVSKMTVELDS-------VTGLLNEAE--GRNIKLSKEASSISSQLQDAQELLSEETRQKLNLSGRLRQLEE 1339
Cdd:PTZ00440 1434 QYSNEAMETENKADENNDSiikyekeITNILNNSSilGKKTKLEKKKKEATNIMDDINGEHSIIKTKLTKSSEKLNQLNE 1513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1340 DKGCLMEQLE----EEMEAKQAVERQASSLSVQLSD---LKKRLEE-LSAAVELLEEGKKRLQRELEAASGDYEEKAAAY 1411
Cdd:PTZ00440 1514 QPNIKREGDVlnndKSTIAYETIQYNLGRVKHNLLNilnIKDEIETiLNKAQDLMRDISKISKIVENKNLENLNDKEADY 1593
|
490 500 510
....*....|....*....|....*....|....*..
gi 1343958102 1412 DKLEKSRGRLQQELEDVLMDLDSQRQLVSNLEKKQKK 1448
Cdd:PTZ00440 1594 VKYLDNILKEKQLMEAEYKKLNEIYSDVDNIEKELKK 1630
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
934-1195 |
5.78e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 40.98 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 934 SISLQQEKKEMEQELQLMEAHIVQEEDARQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLLEERLADMSSNLAE 1013
Cdd:TIGR02794 21 GSLYHSVKPEPGGGAEIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1014 EEEKsknlsklKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQA-QLAELRAQLAAKEEElQTTQ 1092
Cdd:TIGR02794 101 EKAA-------KQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAeEEAKAKAAAEAKKKA-EEAK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1093 ACLDEESRQRGAALKRVRDLEALLAELQEDLEAEKVARGKAEAARRDLGEELNSLRSELEDSLDTTAAQQElrVKREQEM 1172
Cdd:TIGR02794 173 KKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASG--SNAEKQG 250
|
250 260
....*....|....*....|...
gi 1343958102 1173 AMLKKAMEDEGRSHETQIQELRQ 1195
Cdd:TIGR02794 251 GARGAAAGSEVDKYAAIIQQAIQ 273
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1541-1823 |
6.00e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 41.47 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1541 KTQMEELEDELQVAEDAKLRLEvnsqalraqhERelQAREEQGEEKRRQLLKQVRELEAELEEERKQRTLASAARKKLEG 1620
Cdd:PRK05035 435 KAEIRAIEQEKKKAEEAKARFE----------AR--QARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAA 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1621 EVKNTEEQLEAASRGRDEALKQLRKNQGQLKELHRELEEGRAAHKEILASAREaerRCKNLEAEILQMQEML-------- 1692
Cdd:PRK05035 503 TQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIA---RAKAKKAAQQAANAEAeeevdpkk 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1693 AAAERARKQAETERDELSEEVAGGSSGRSLLSDEKRRLEAKISQLEEELEEEQANVETLNErlrksqqlVDQLGAELTAE 1772
Cdd:PRK05035 580 AAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEP--------VDPRKAAVAAA 651
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1343958102 1773 RASSQNRegsrlqlekqtrdlKAKLQDVESQARSKLKSSVAALEAKLREAE 1823
Cdd:PRK05035 652 IARAKAR--------------KAAQQQANAEPEEAEDPKKAAVAAAIARAK 688
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1111-1286 |
6.32e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 39.55 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1111 DLEALLAELQEDLEAEkvargkAEAARRDLGEELNSLRSELEDslDTTAAQQELRVKREQEMAMLKKAMEDEGRSHETQI 1190
Cdd:pfam01442 8 ELSTYAEELQEQLGPV------AQELVDRLEKETEALRERLQK--DLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1191 QELRQKHGQAVEELREHLEQ-AKKVRAALEKAKQALEKEAADLSADLRAlsSTKQDVEQKKKKVEAQLNDLQLRFSESER 1269
Cdd:pfam01442 80 EELRKRLNADAEELQEKLAPyGEELRERLEQNVDALRARLAPYAEELRQ--KLAERLEELKESLAPYAEEVQAQLSQRLQ 157
|
170
....*....|....*...
gi 1343958102 1270 Q-RNELSERVSKMTVELD 1286
Cdd:pfam01442 158 ElREKLEPQAEDLREKLD 175
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1368-1512 |
6.49e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1368 QLSDLKKRLEELSAAVELLEEGKKRLQRELEAASgdyeekaAAYDKLEKSRGRLQQeledvlmDLDSQRQLVSNLEKKQK 1447
Cdd:PRK09039 54 ALDRLNSQIAELADLLSLERQGNQDLQDSVANLR-------ASLSAAEAERSRLQA-------LLAELAGAGAAAEGRAG 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1343958102 1448 KFDQMLAEERAVSAksaeeRDRAEAELREKEtkVLALMKMLEDKQEALQEAERTVKALRVEMEDL 1512
Cdd:PRK09039 120 ELAQELDSEKQVSA-----RALAQVELLNQQ--IAALRRQLAALEAALDASEKRDRESQAKIADL 177
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
937-1438 |
6.74e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 937 LQQEKKEMEQELQLMEA---HIVQEEDARQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLqkerKLLEERLADMSSNLA- 1012
Cdd:PRK01156 216 TLKEIERLSIEYNNAMDdynNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYY----KELEERHMKIINDPVy 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1013 --------------EEEEKSKNLSKLKS---KHESMISELEVRlkkeEKTRQDVEKAKRKVE---AELVDLQEQQADLQA 1072
Cdd:PRK01156 292 knrnyindyfkyknDIENKKQILSNIDAeinKYHAIIKKLSVL----QKDYNDYIKKKSRYDdlnNQILELEGYEMDYNS 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1073 QLAELRAQLAAKEEELQTTQACLDEESRQRGAALKRVRDLEALLAELQEDLEaekvargkaeaarrDLGEELNSLrsele 1152
Cdd:PRK01156 368 YLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQ--------------DISSKVSSL----- 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1153 dsldttaaQQELRVKREQEMAMLKKAMEDEGRS---------HETQIQELRQKHGQAVEELREHLEQAK-KVRAALEKAK 1222
Cdd:PRK01156 429 --------NQRIRALRENLDELSRNMEMLNGQSvcpvcgttlGEEKSNHIINHYNEKKSRLEEKIREIEiEVKDIDEKIV 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1223 QALEKEAADLSADLRALSSTKQDVEQKKKKVEAQLNDLQlRFSESERQRNELSERVSKMTVE-LDS-VTGLLNEAEGRNI 1300
Cdd:PRK01156 501 DLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKIN-ELKDKHDKYEEIKNRYKSLKLEdLDSkRTSWLNALAVISL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1301 ----KLSKEASSISSQLQDA----QELLSEETRQKLNLSGRLRQLEEDKGCLMEQLEEEMEAKQAVER------QASSLS 1366
Cdd:PRK01156 580 idieTNRSRSNEIKKQLNDLesrlQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKlrgkidNYKKQI 659
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1343958102 1367 VQLSDLKKRLEELSAAVELLEEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLMDLDSQRQL 1438
Cdd:PRK01156 660 AEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKI 731
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1785-1925 |
6.77e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1785 QLEKQTRDLKAKLQDVEsQARSKLKSSVAALEAKLREAEEQLEvESRERQASAKNLRQkekkLKDLTAQMEDERKQAQDY 1864
Cdd:COG1579 35 ELEDELAALEARLEAAK-TELEDLEKEIKRLELEIEEVEARIK-KYEEQLGNVRNNKE----YEALQKEIESLKRRISDL 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1343958102 1865 KDQMEKSSARMKQLKHQLEEAEEEAQRVAAARRKLQRELDEALEANDALSREVSSLRSKLR 1925
Cdd:COG1579 109 EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
880-1218 |
6.79e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.06 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 880 QLVEEQAMLEAKLQAEAELYAEAEDMRVRLEAKKQELEEVLHEMEARLEEEEERSISLQQEKKEMEQELQLMEAHIVQEE 959
Cdd:pfam13868 27 QIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 960 DarQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLLEERladmssnlAEEEEKSKNLSKLKSKHEsmiselevRL 1039
Cdd:pfam13868 107 V--ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKE--------EEREEDERILEYLKEKAE--------RE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1040 KKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQttqacldEESRQRGAALKRVRDLEALLAEL 1119
Cdd:pfam13868 169 EEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERK-------ERQKEREEAEKKARQRQELQQAR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1120 QEDLEAEKvaRGKAEAARRDLGEELNSLRSELEDSLDTTAAQQELRVKREQEMAMLKKAMEDEGRSHETQIQELRQKHGQ 1199
Cdd:pfam13868 242 EEQIELKE--RRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGER 319
|
330
....*....|....*....
gi 1343958102 1200 AVEELREHLEQAKKVRAAL 1218
Cdd:pfam13868 320 LREEEAERRERIEEERQKK 338
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1498-1769 |
6.88e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.90 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1498 AERTVKALRV--EMEDLISSKDDvGKSVHDLErAKRGLEAFVEEMKTQMEELEDELQvaedaKLRLEVnsQALRAqherE 1575
Cdd:pfam09787 10 ADYKQKAARIlqSKEKLIASLKE-GSGVEGLD-SSTALTLELEELRQERDLLREEIQ-----KLRGQI--QQLRT----E 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1576 LQAREEQGEEKRRQLLKQVReleaeleEERKQRTLASAARKKLEGEVKNTEEQLEAAsrgRDEALKQLRKNQGQLKELHR 1655
Cdd:pfam09787 77 LQELEAQQQEEAESSREQLQ-------ELEEQLATERSARREAEAELERLQEELRYL---EEELRRSKATLQSRIKDREA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1656 ELEEGRA--AHKEILASAR-EAERRCKNLEAEILQMQEMLAA--AERARKQAETERDELSEEVAGGSSGRS---LLSDEK 1727
Cdd:pfam09787 147 EIEKLRNqlTSKSQSSSSQsELENRLHQLTETLIQKQTMLEAlsTEKNSLVLQLERMEQQIKELQGEGSNGtsiNMEGIS 226
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1343958102 1728 RRLEAKISQLEEELEEEQANVETLNERLRKSQQLVDQLGAEL 1769
Cdd:pfam09787 227 DGEGTRLRNVPGLFSESDSDRAGMYGKVRKAASVIDKFSIRL 268
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1473-1643 |
6.89e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1473 ELREKETKVLALMKMLEDKQEALQEAERTVKALRVEMEDLIsskddvgKSVHDLERAKRGLEAFVEEMKTQMEELEDELQ 1552
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAK-------TELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1553 VAEDAK----LRLEVNSQALR-AQHERELQAREEQGEEKRRQLlkqvrelEAELEEERKQRTLASAARKKLEGEVKNTEE 1627
Cdd:COG1579 84 NVRNNKeyeaLQKEIESLKRRiSDLEDEILELMERIEELEEEL-------AELEAELAELEAELEEKKAELDEELAELEA 156
|
170
....*....|....*.
gi 1343958102 1628 QLEAASRGRDEALKQL 1643
Cdd:COG1579 157 ELEELEAEREELAAKI 172
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
936-1257 |
7.02e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 936 SLQQEKKEMEQELQLMEAHIVQEEDARQKLQLEKAAVEGRVKKLEENLLLSEDQNNKLQKERKLLEERLADMSSNLAEEE 1015
Cdd:COG4372 49 QLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1016 EKSKNLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQACL 1095
Cdd:COG4372 129 QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1096 DEESRQRGAALKRVRDLEALLAELQEDLEAEKVARGKAEAARRDLGEELNSLRSELEDSLDTTAAQQELRVKREQEMAML 1175
Cdd:COG4372 209 IESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1176 KKAMEDEGRSHETQIQELRQKHGQAVEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSSTKQDVEQKKKKVEA 1255
Cdd:COG4372 289 EEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
..
gi 1343958102 1256 QL 1257
Cdd:COG4372 369 DG 370
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
937-1130 |
7.40e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 937 LQQEKKEMEQELQLMEAHiVQEEDARQKLQLEKAavegrvkkleenlllSEDQNNKLQKerklLEERLADMSSNLaeeEE 1016
Cdd:PRK12704 44 LEEAKKEAEAIKKEALLE-AKEEIHKLRNEFEKE---------------LRERRNELQK----LEKRLLQKEENL---DR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1017 KSKNLSKLKSkhesmisELEVRLKKEEKTRQDVEKAKRKVEaELVdlQEQQADLQaQLAELRAQlAAKEEELQTTQacld 1096
Cdd:PRK12704 101 KLELLEKREE-------ELEKKEKELEQKQQELEKKEEELE-ELI--EEQLQELE-RISGLTAE-EAKEILLEKVE---- 164
|
170 180 190
....*....|....*....|....*....|....
gi 1343958102 1097 EESRQRGAALKRVRDLEAllaelqeDLEAEKVAR 1130
Cdd:PRK12704 165 EEARHEAAVLIKEIEEEA-------KEEADKKAK 191
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1180-1277 |
8.01e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.48 E-value: 8.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1180 EDEGRSHETQIQELRQK---HGQAVEELREHLEQAKKVRAALEKAKQALEKEAADLSADLRALSS--TKQDVEQKKKKVE 1254
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQlelQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEkaAETSQERKQKRKE 220
|
90 100
....*....|....*....|...
gi 1343958102 1255 AqlndlqlrfSESERQRNELSER 1277
Cdd:PRK11448 221 I---------TDQAAKRLELSEE 234
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1036-1696 |
8.23e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.35 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1036 EVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAqlaELRAQLAAKEEELQTTQA--------CLDEESRQRGAALK 1107
Cdd:NF041483 546 EVRAAAERAARELREETERAIAARQAEAAEELTRLHT---EAEERLTAAEEALADARAeaerirreAAEETERLRTEAAE 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1108 RVRDLEALLAELQEDLEAEKVA-----RGKAEAA----RRDLGEELNSLRSELEDSLDTTAAQQELRVKREQEMAM--LK 1176
Cdd:NF041483 623 RIRTLQAQAEQEAERLRTEAAAdasaaRAEGENVavrlRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEAAeaLA 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1177 KAMEDEGRSHETQIQELRQKHGQAVEELREHLEQAKKVRAALEKAKQALEKEAADL--SADLRA---LSSTKQDVEQKKK 1251
Cdd:NF041483 703 AAQEEAARRRREAEETLGSARAEADQERERAREQSEELLASARKRVEEAQAEAQRLveEADRRAtelVSAAEQTAQQVRD 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1252 KV-----EAQLNDLQLRFS---ESERQRNELSERVSKMTVELDSVTGLLNEAEGRNIKLSKEAS---------SISSQLQ 1314
Cdd:NF041483 783 SVaglqeQAEEEIAGLRSAaehAAERTRTEAQEEADRVRSDAYAERERASEDANRLRREAQEETeaakalaerTVSEAIA 862
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1315 DAQELLSEET----RQKLNLSGRLRQLEEDKGCLMEQLEE------EMEAKQA--------VERQASSLSVQLSDLKKRL 1376
Cdd:NF041483 863 EAERLRSDASeyaqRVRTEASDTLASAEQDAARTRADAREdanrirSDAAAQAdrligeatSEAERLTAEARAEAERLRD 942
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1377 EELSAAVELLEEGKKRLQRELEAASGDYE----EKAAAYDKLEKSRGRLQQELEDVLMDLDSQRQLVSNleKKQKKFDQM 1452
Cdd:NF041483 943 EARAEAERVRADAAAQAEQLIAEATGEAErlraEAAETVGSAQQHAERIRTEAERVKAEAAAEAERLRT--EAREEADRT 1020
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1453 LAEERAVSAK----SAEERDRAEAELREKETKVL--ALMKMLEDKQEALQEAERTVKALRVEMEDLISSKDDVGKSVhdl 1526
Cdd:NF041483 1021 LDEARKDANKrrseAAEQADTLITEAAAEADQLTakAQEEALRTTTEAEAQADTMVGAARKEAERIVAEATVEGNSL--- 1097
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1527 erakrgleafVEEMKTQMEELedeLQVAEDAKLRLEVNSQALRAQHERELqarEEQGEEKRRQLLKQVRELEAeleeeRK 1606
Cdd:NF041483 1098 ----------VEKARTDADEL---LVGARRDATAIRERAEELRDRITGEI---EELHERARRESAEQMKSAGE-----RC 1156
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1607 QRTLASAARKKLEGEVKNTEEQLEAASRGRDEALKQLRKNQGQLKE-------LHRELEEGRA-----AHKEILASAREA 1674
Cdd:NF041483 1157 DALVKAAEEQLAEAEAKAKELVSDANSEASKVRIAAVKKAEGLLKEaeqkkaeLVREAEKIKAeaeaeAKRTVEEGKREL 1236
|
730 740
....*....|....*....|....*
gi 1343958102 1675 E---RRCKNLEAEILQMQEMLAAAE 1696
Cdd:NF041483 1237 DvlvRRREDINAEISRVQDVLEALE 1261
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
857-1150 |
8.62e-03 |
|
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: 40.82 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 857 LKAVREAAAKAEADLKDITQKHSQLVEEQAMLEAKLQAEAELYAEAEDMRVRLEAKKQELEEVLHEMEarleeeeersis 936
Cdd:pfam19220 141 NKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATR------------ 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 937 lqqekkemeQELQLMEAHIVQEEDARQKLQLEkaavegrvkkleenlllSEDQNNKLQKERKLLEERLADMSSNLAEEEE 1016
Cdd:pfam19220 209 ---------ARLRALEGQLAAEQAERERAEAQ-----------------LEEAVEAHRAERASLRMKLEALTARAAATEQ 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1017 KSKNLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKRKVEAELVDLQEQQADLQAQLAELRAQLAAKEEELQTTQACLD 1096
Cdd:pfam19220 263 LLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALE 342
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1343958102 1097 EesrqrgaALKRVRDLEALLAELQEDLEAEKVArgkAEAARRDLGEELNSLRSE 1150
Cdd:pfam19220 343 R-------AEERIASLSDRIAELTKRFEVERAA---LEQANRRLKEELQRERAE 386
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1034-1135 |
8.91e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 40.63 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1034 ELEVRLKKEEKTRQ-DVEKAKRKVEAELVDLQEQQADLQAQLAELRAQ------------LAAKEEELQTTQACLDEESR 1100
Cdd:COG2268 209 ERETEIAIAQANREaEEAELEQEREIETARIAEAEAELAKKKAEERREaetaraeaeaayEIAEANAEREVQRQLEIAER 288
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1343958102 1101 QRGAALKRVR----------------DLEALLAELQEDLEAE-KVARGKAEA 1135
Cdd:COG2268 289 EREIELQEKEaereeaeleadvrkpaEAEKQAAEAEAEAEAEaIRAKGLAEA 340
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1666-1843 |
9.02e-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: 39.91 E-value: 9.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1666 EILASAREAERRCKNLEAEILQMQEMLAAAERARKQAETERDELseevaggssgrsllsdekrrlEAKISQLEEELEEEQ 1745
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL---------------------EKEIKRLELEIEEVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1746 ANVETLNERLR--KSQQLVDQLGAELTAERASSQNREGSRLQLEKQTRDLKAKLQDVESQaRSKLKSSVAALEAKLREAE 1823
Cdd:COG1579 73 ARIKKYEEQLGnvRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE-LAELEAELEEKKAELDEEL 151
|
170 180
....*....|....*....|
gi 1343958102 1824 EQLEVESRERQASAKNLRQK 1843
Cdd:COG1579 152 AELEAELEELEAEREELAAK 171
|
|
| PilO |
COG3167 |
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures]; |
1031-1086 |
9.26e-03 |
|
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
Pssm-ID: 442400 [Multi-domain] Cd Length: 202 Bit Score: 39.55 E-value: 9.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1343958102 1031 MISELEVRLKKEEKTRQDVEKAKRKVeAELVDLQEQQADLQAQLAELRAQLAAKEE 1086
Cdd:COG3167 44 QLEELEELEAEEAQLKQELEKKQAKA-ANLPALKAQLEELEQQLGELLKQLPSKAE 98
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
854-1076 |
9.68e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 9.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 854 EEELKAVREAAAKAEADLKDITQKHSQLVEEQAMLEAKLQAEAELYAEAEDMRVRLEAKKQELEEVLHEMEARLEEEEER 933
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNE 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 934 SISLQQEKKEMEQELQLMEAHIVQEEDARQKLQLEKAAVEGRVKKLEENlllsedQNNKLQKERKLLEERLADMSSNLAE 1013
Cdd:PRK03918 604 YLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL------EKKYSEEEYEELREEYLELSRELAG 677
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1343958102 1014 EEEKSKNLSKLKSKHESMISELEVRLKKEEKTRQDVEKAKrKVEAELVDLQEQQADLQAQLAE 1076
Cdd:PRK03918 678 LRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLE-KALERVEELREKVKKYKALLKE 739
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1387-1700 |
9.87e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 40.29 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1387 EEGKKRLQRELEAASGDYEEKAAAYDKLEKSRGRLQQELEDVLmdldsQRQLVSNLEKKQKKFDQMLAEERAVSAKSAEE 1466
Cdd:pfam13868 36 AEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQEL-----EEQIEEREQKRQEEYEEKLQEREQMDEIVERI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1467 RDRAEAELREKETKVLALMKMLeDKQEALQEAERTVKALRVEMEDLISSKDDVGKSVHDLERAKRGLEAFvEEMKTQMEE 1546
Cdd:pfam13868 111 QEEDQAEAEEKLEKQRQLREEI-DEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIE-EEKEREIAR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343958102 1547 LEDELQVAEDAKLRLE-VNSQALRAQHERELQAREEQGEEKRRQLLKQVRELEAELEEERKQRTLASAARKKLEgevknT 1625
Cdd:pfam13868 189 LRAQQEKAQDEKAERDeLRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEE-----F 263
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1343958102 1626 EEQLEAASRGRDEALKQLRKNQGQLKELHRELEEGRAAHKEILASAREAERRCKNLEAEILQMQEMLAAAERARK 1700
Cdd:pfam13868 264 ERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| |
