|
Name |
Accession |
Description |
Interval |
E-value |
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
842-1921 |
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: 1417.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 842 RHEDELLAKEAELTKVREKHLAAENRLTEMETMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLE 921
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 922 ARVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRV 1001
Cdd:pfam01576 82 SRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1002 AEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKK 1081
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1082 EEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERACRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQEL 1161
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1162 RSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQTLENERGELANEVKALLQGKG 1241
Cdd:pfam01576 322 RSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1242 DSEHKRKKVEAQLQELQVKFSEGERVRTELADKVSKLQVELDSVTGLLNQSDSKSSKLTKDFSALESQLQDTQELLQEEN 1321
Cdd:pfam01576 402 DSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEET 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1322 RQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRL 1401
Cdd:pfam01576 482 RQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQL 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1402 EEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSL 1481
Cdd:pfam01576 562 EEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSL 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1482 ARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVN 1561
Cdd:pfam01576 642 ARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVN 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1562 LQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLR 1641
Cdd:pfam01576 722 MQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLK 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1642 KLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALAL 1721
Cdd:pfam01576 802 KLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQ 881
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1722 EEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAV 1801
Cdd:pfam01576 882 DEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTV 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1802 KSKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRAEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEE 1881
Cdd:pfam01576 962 KSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEE 1041
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|
gi 806638593 1882 AEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKL 1921
Cdd:pfam01576 1042 AEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
95-764 |
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: 1359.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 175 ESGAGKTENTKKVIQYLAHVASSHKSKKD---QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDhniPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 332 PEDEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 411
Cdd:cd14920 241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 412 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 491
Cdd:cd14920 321 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 492 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCII 571
Cdd:cd14920 401 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 572 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYK 651
Cdd:cd14920 481 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 652 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 731
Cdd:cd14920 561 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 806638593 732 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14920 641 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
95-764 |
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: 1344.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 175 ESGAGKTENTKKVIQYLAHVASSHKSKKD----QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 250
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKEsgkkKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 251 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYR-FLSNGHVTIPGQQDKDMFQETMEAMRIM 329
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 330 GIPEDEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQ 409
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 410 ADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQ 489
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 490 EEYQREGIEWNFIDFGLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPK-FQKPKQLKDKADF 568
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKPKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 569 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRiigldqvagmsETALPGAFKTRKGMFRTVGQ 648
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE-----------SGGGGGKKKKKGGSFRTVSQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 649 LYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNS 728
Cdd:cd01377 547 LHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNA 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 806638593 729 IPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01377 627 IPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
95-764 |
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: 1336.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 175 ESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPED 334
Cdd:cd14919 161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 335 EQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAI 414
Cdd:cd14919 241 EQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 415 EALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 494
Cdd:cd14919 321 EALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 495 EGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCIIHYA 574
Cdd:cd14919 401 EGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCIIHYA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 575 GKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYKEQL 654
Cdd:cd14919 481 GKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYKEQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 655 AKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFM 734
Cdd:cd14919 561 AKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFM 640
|
650 660 670
....*....|....*....|....*....|
gi 806638593 735 DGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14919 641 DGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
95-764 |
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: 1306.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 175 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ-------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 247
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQssialshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 248 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMR 327
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 328 IMGIPEDEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 407
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 408 EQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 487
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 488 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKAD 567
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 568 FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSEtALPGAFKTRKGMFRTVG 647
Cdd:cd14932 481 FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGE-SLHGAFKTRKGMFRTVG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 648 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 727
Cdd:cd14932 560 QLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 639
|
650 660 670
....*....|....*....|....*....|....*..
gi 806638593 728 SIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14932 640 AIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
95-764 |
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: 1252.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 175 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ-------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 247
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQnslalshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 248 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMR 327
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 328 IMGIPEDEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 407
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 408 EQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 487
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 488 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKAD 567
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 568 FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSEtaLPGAFKTRKGMFRTVG 647
Cdd:cd15896 481 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSE--MPGAFKTRKGMFRTVG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 648 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 727
Cdd:cd15896 559 QLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 638
|
650 660 670
....*....|....*....|....*....|....*..
gi 806638593 728 SIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd15896 639 AIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
95-764 |
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: 1203.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 175 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ---GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTsitGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 332 PEDEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 411
Cdd:cd14921 241 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 412 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 491
Cdd:cd14921 321 FAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 492 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCII 571
Cdd:cd14921 401 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 572 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYK 651
Cdd:cd14921 481 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 652 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 731
Cdd:cd14921 561 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 806638593 732 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14921 641 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
95-764 |
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: 1145.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 175 ESGAGKTENTKKVIQYLAHVASShKSKKD-------------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 241
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAAS-KPKGSgavphpavnpavlIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 242 NFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQE 321
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 322 TMEAMRIMGIPEDEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYV 401
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 402 QKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFN 481
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 482 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKpKQ 561
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 562 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDrIIGLDQVAgMSETALpGAfKTRKG 641
Cdd:cd14911 476 FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQF-GA-RTRKG 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 642 MFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 721
Cdd:cd14911 552 MFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 806638593 722 EILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14911 632 ELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
95-764 |
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: 1128.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 175 ESGAGKTENTKKVIQYLAHVASSHKSKKDQG---ELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQdKDMFQETMEAMRIMGI 331
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETLESLRVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 332 PEDEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 411
Cdd:cd14930 240 SHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 412 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 491
Cdd:cd14930 320 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 492 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCII 571
Cdd:cd14930 400 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 572 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETalPGAFKTRKGMFRTVGQLYK 651
Cdd:cd14930 480 HYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDG--PPGGRPRRGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 652 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 731
Cdd:cd14930 558 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 806638593 732 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14930 638 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
83-764 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1118.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 83 VEDMAELTCLNEASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMM 162
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 163 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKSKKdQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 242
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN-VGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 243 FDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSN-GHVTIPGQQDKDMFQE 321
Cdd:pfam00063 160 FDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQsGCYTIDGIDDSEEFKI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 322 TMEAMRIMGIPEDEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYV 401
Cdd:pfam00063 240 TDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 402 QKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFN 481
Cdd:pfam00063 320 SKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 482 HTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQ 561
Cdd:pfam00063 400 HHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQKPRL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 562 lKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVagmsETALPGAFKTRKG 641
Cdd:pfam00063 477 -QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAAN----ESGKSTPKRTKKK 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 642 MFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 721
Cdd:pfam00063 552 RFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRY 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 806638593 722 EILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:pfam00063 632 RILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
76-776 |
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: 1024.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 76 NPPKFSKVEDMAELTCLNEASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITD 155
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 156 TAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKSKkdqGELERQLLQANPILEAFGNAKTVKNDNSSRF 235
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV---GSVEDQILESNPILEAFGNAKTLRNNNSSRF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 236 GKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH-VTIPGQQ 314
Cdd:smart00242 158 GKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGcLTVDGID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 315 DKDMFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNT-AAQKVSHLLGINVTDFTRGILTPR 393
Cdd:smart00242 238 DAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEELEKALTKRK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 394 IKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTN 473
Cdd:smart00242 318 IKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGS-TYFIGVLDIYGFEIFEVNSFEQLCINYAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 474 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTH 553
Cdd:smart00242 397 EKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEKK--PPGILSLLDEECRFPKGTDQTFLEKLNQHHKKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 554 PKFQKPKQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldqvagmsetalp 633
Cdd:smart00242 474 PHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSG------------------ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 634 GAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVV 713
Cdd:smart00242 535 VSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLP 614
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 806638593 714 FQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFRAGVLAHLEEERD 776
Cdd:smart00242 615 FDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
32-1151 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 907.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 32 VWVPSTKNGFEPASLKEEVGEEAIVEL---VENGKKVKVNKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLKERYY 106
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEegkKEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 107 SGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKK 186
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 187 VIQYLAHVASSHKSkkDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIR 266
Cdd:COG5022 172 IMQYLASVTSSSTV--EISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVH 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 267 QAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVT-IPGQQDKDMFQETMEAMRIMGIPEDEQMGLLRVISG 345
Cdd:COG5022 250 QNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKILAA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 346 VLQLGNIVFKKERNtDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERM 425
Cdd:COG5022 330 ILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 426 FRWLVLRINKALDKTKRQGaSFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFg 505
Cdd:COG5022 409 FDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY- 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 506 LDLQPCIDLIEKpAGPPGILALLDEECWFPKATDKSFVEKVVQ--EQGTHPKFQKPKQLKDKadFCIIHYAGKVDYKADE 583
Cdd:COG5022 487 FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDNK--FVVKHYAGDVEYDVEG 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 584 WLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIigldqvagmsetalpgafkTRKGMFRTVGQLYKEQLAKLMATLRN 663
Cdd:COG5022 564 FLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENI-------------------ESKGRFPTLGSRFKESLNSLMSTLNS 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 664 TNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNS----IPKGFMDGKQA 739
Cdd:COG5022 625 TQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtgEYTWKEDTKNA 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 740 CVLMIKALELDSNLYRIGQSKVFFRAGVLAHLEEERDLKITDVIIGFQACCRGYLARKAFAKRQQQLTAMKVLQRNCAAY 819
Cdd:COG5022 705 VKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLR 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 820 LRLRNWQWWRLFTKVKPLLNSIRHEDELLAKEAELTKVrekhlaaenrltemetmqsQLMAEK-LQLQEQLQAETELCAE 898
Cdd:COG5022 785 RLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKL-------------------QKTIKReKKLRETEEVEFSLKAE 845
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 899 AEELRARLTAKKQELEEICHDLEARVeeeeercQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKlKKLEE 978
Cdd:COG5022 846 VLIQKFGRSLKAKKRFSLLKKETIYL-------QSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELK-KSLSS 917
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 979 DQII-MEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKS--------KSLAKLKNKHEAMITDLEERLRREEKQRQELEKT 1049
Cdd:COG5022 918 DLIEnLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPElnklheveSKLKETSEEYEDLLKKSTILVREGNKANSELKNF 997
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1050 RRKLegdsTDLSDQIAELQAQIAELKmQLAKKEEELQAALARVEEEAA---QKNMALKKIRELETQISELQEDLeserac 1126
Cdd:COG5022 998 KKEL----AELSKQYGALQESTKQLK-ELPVEVAELQSASKIISSESTelsILKPLQKLKGLLLLENNQLQARY------ 1066
|
1130 1140
....*....|....*....|....*
gi 806638593 1127 rnKAEKQKRDLGEELEALKTELEDT 1151
Cdd:COG5022 1067 --KALKLRRENSLLDDKQLYQLEST 1089
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
95-764 |
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: 881.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRH-EMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 174 GESGAGKTENTKKVIQYLAHVASSHKSKKD--QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSssASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFL-----SNGHVTIPGQQDKDMFQETMEAM 326
Cdd:cd00124 161 ASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDDAEEFQELLDAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 327 RIMGIPEDEQMGLLRVISGVLQLGNIVFKKERNT--DQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKA 404
Cdd:cd00124 241 DVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITKP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 405 QTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQ-GASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 483
Cdd:cd00124 321 LTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 484 MFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLK 563
Cdd:cd00124 401 VFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 564 DKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDkfvselwkdvdriigldqvagmsetalpgafktrkgmf 643
Cdd:cd00124 478 KLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ-------------------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 644 rtvgqlYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 723
Cdd:cd00124 519 ------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRI 592
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 806638593 724 LTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd00124 593 LAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
95-764 |
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: 786.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 175 ESGAGKTENTKKVIQYLAHVAS---------SHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 245
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAAlgdgpgkkaQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 246 NGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETM 323
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVsmNPYD-YHFCSQGVTTVDNMDDGEELMATD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 324 EAMRIMGIPEDEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQK 403
Cdd:cd14927 240 HAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 404 AQTKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 483
Cdd:cd14927 320 GQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 484 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKP--- 559
Cdd:cd14927 399 MFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKPrpd 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 560 KQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldqVAGMSETALPGAFKTR 639
Cdd:cd14927 476 KKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENY--------VGSDSTEDPKSGVKEK 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 640 K---GMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQE 716
Cdd:cd14927 548 RkkaASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAD 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 806638593 717 FRQRYEILTPNSIPK-GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14927 628 FKQRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
96-764 |
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: 761.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 176 SGAGKTENTKKVIQYLAHVASS-----HKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 250
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATgdlakKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 251 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRI 328
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLIttNPYD-YPFISQGEILVASIDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 329 MGIPEDEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 407
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 408 EQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 487
Cdd:cd14913 320 DQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 488 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVV-QEQGTHPKFQKPKQLKDKA 566
Cdd:cd14913 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKVVKGRA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 567 D--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriigldqVAGMSETALPGAFKTRKG-MF 643
Cdd:cd14913 476 EahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYAT---------FATADADSGKKKVAKKKGsSF 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 644 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 723
Cdd:cd14913 547 QTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRV 626
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 806638593 724 LTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14913 627 LNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
95-764 |
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: 756.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 175 ESGAGKTENTKKVIQYLAHVASSHKSKKD-QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDgKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNK-YRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd14934 161 IESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKeYHWVSQGVTVVDNMDDGEELQITDVAFDVLGFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 333 EDEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADF 412
Cdd:cd14934 241 AEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQCNN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 413 AIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 492
Cdd:cd14934 321 SIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 493 QREGIEWNFIDFGLDLQPCIDLIEKPAGppgILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKDK---ADF 568
Cdd:cd14934 400 KREGIEWVFIDFGLDLQACIDLLEKPMG---IFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKGGKGKgpeAHF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 569 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSdkfvselwkdvdriIGLDQVAGMSETALPGAFKTRKGM-FRTVG 647
Cdd:cd14934 477 ELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSS--------------LGLLALLFKEEEAPAGSKKQKRGSsFMTVS 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 648 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 727
Cdd:cd14934 543 NFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPN 622
|
650 660 670
....*....|....*....|....*....|....*..
gi 806638593 728 SIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14934 623 VIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
95-764 |
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: 752.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 175 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ---GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAkskGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL-EPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMG 330
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 331 IPEDEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQA 410
Cdd:cd14909 241 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 411 DFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQE 490
Cdd:cd14909 321 TNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 491 EYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLK---DKA 566
Cdd:cd14909 400 EYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKPPKpgqQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 567 DFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriiGLDQVAGMSETAlpGAFKTRKGMFRTV 646
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAD-----HAGQSGGGEQAK--GGRGKKGGGFATV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 647 GQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 726
Cdd:cd14909 550 SSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNP 629
|
650 660 670
....*....|....*....|....*....|....*...
gi 806638593 727 NSIpKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14909 630 AGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
95-764 |
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: 731.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 175 ESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEhlKTDLLLEPYN--KYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd14929 161 DIYLLEKSRVIFQQPGERNYHIFYQILSGKKE--LRDLLLVSANpsDFHFCSCGAVAVESLDDAEELLATEQAMDILGFL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 333 EDEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADF 412
Cdd:cd14929 239 PDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVTY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 413 AIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 492
Cdd:cd14929 319 AVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEEY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 493 QREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKDK--ADFC 569
Cdd:cd14929 398 RKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKPDKKKfeAHFE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 570 IIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriiglDQVAGmseTALPGAFKTRK--GMFRTVG 647
Cdd:cd14929 475 LVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEN-------YISTD---SAIQFGEKKRKkgASFQTVA 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 648 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 727
Cdd:cd14929 545 SLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPR 624
|
650 660 670
....*....|....*....|....*....|....*...
gi 806638593 728 SIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14929 625 TFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
96-764 |
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: 716.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 96 SVLHNLKERYYSG-LIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 175 ESGAGKTENTKKVIQYLAHVASSHKSKKdqgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSGET---QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNG-HVTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd01380 159 RTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGgSPVIDGVDDAAEFEETRKALTLLGISE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 334 DEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFA 413
Cdd:cd01380 239 EEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 414 IEALAKATYERMFRWLVLRINKALDKTKRQGA-SFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 492
Cdd:cd01380 319 RDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 493 QREGIEWNFIDFgLDLQPCIDLIEkpaGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPK--FQKPKQLKDKadFCI 570
Cdd:cd01380 399 VKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPRFSNTA--FIV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 571 IHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSsdkfvselwkdvdriigldqvagmsetalpgafKTRKgmfRTVGQLY 650
Cdd:cd01380 473 KHFADDVEYQVEGFLEKNRDTVSEEHLNVLKAS---------------------------------KNRK---KTVGSQF 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 651 KEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIP 730
Cdd:cd01380 517 RDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEW 596
|
650 660 670
....*....|....*....|....*....|....
gi 806638593 731 KGfMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01380 597 LR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
96-764 |
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: 712.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 176 SGAGKTENTKKVIQYLAHVAS-SHKSKKDQ----GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 250
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAiGDRSKKDQtpgkGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 251 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRI 328
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItnNPYD-YAFISQGETTVASIDDAEELMATDNAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 329 MGIPEDEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 407
Cdd:cd14917 241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 408 EQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 487
Cdd:cd14917 320 QQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 488 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKDK- 565
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPRNIKGKp 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 566 -ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriigldqVAGMSETALPGAFKTRKG-MF 643
Cdd:cd14917 476 eAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN---------YAGADAPIEKGKGKAKKGsSF 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 644 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 723
Cdd:cd14917 547 QTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 626
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 806638593 724 LTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14917 627 LNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
96-764 |
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: 694.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 176 SGAGKTENTKKVIQYLAHVAS-SHKSKKD-----QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 249
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKEnpnanKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 250 VGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMR 327
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtnNPYD-YAFVSQGEVSVASIDDSEELLATDSAFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 328 IMGIPEDEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNTA-AQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:cd14916 241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 407 KEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 486
Cdd:cd14916 320 VQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 487 LEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKDK 565
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRNVKGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 566 --ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldQVAGMSETALPGAFKTRKGMF 643
Cdd:cd14916 476 qeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY-------ASADTGDSGKGKGGKKKGSSF 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 644 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 723
Cdd:cd14916 549 QTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 628
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 806638593 724 LTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14916 629 LNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
96-764 |
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: 691.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 176 SGAGKTENTKKVIQYLAHVASSHKSKKD------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 249
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEqqpgkmQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 250 VGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLkTDLLLEPYNKYR--FLSNGHVTIPGQQDKDMFQETMEAMR 327
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDfpFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 328 IMGIPEDEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 407 KEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 486
Cdd:cd14923 320 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 487 LEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVV-QEQGTHPKFQKPKQLKDK 565
Cdd:cd14923 399 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKPAKGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 566 AD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigLDQVAGMSETALPGAfKTRKGMF 643
Cdd:cd14923 476 AEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNY-----AGAEAGDSGGSKKGG-KKKGSSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 644 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 723
Cdd:cd14923 550 QTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 806638593 724 LTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14923 630 LNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
97-764 |
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: 690.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 97 VLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGES 176
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 177 GAGKTENTKKVIQYLAHVASSHKSKKD-----QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRIM 329
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLIttNPYD-YAFVSQGEITVPSIDDQEELMATDSAIDIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 330 GIPEDEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKE 408
Cdd:cd14918 242 GFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 409 QADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILE 488
Cdd:cd14918 321 QVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 489 QEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVV-QEQGTHPKFQKPKQLKDKAD 567
Cdd:cd14918 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKVVKGKAE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 568 --FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldQVAGMSETALPGAfKTRKGMFRT 645
Cdd:cd14918 477 ahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY-------ASAEADSGAKKGA-KKKGSSFQT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 646 VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILT 725
Cdd:cd14918 549 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLN 628
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 806638593 726 PNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14918 629 ASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
96-764 |
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: 683.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 176 SGAGKTENTKKVIQYLAHVASSHKSKKD-------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 248
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 249 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAM 326
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLIttNPYD-YPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 327 RIMGIPEDEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQ 405
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 406 TKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 485
Cdd:cd14912 320 TVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 486 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVV-QEQGTHPKFQKPKQLKD 564
Cdd:cd14912 399 VLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQKPKVVKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 565 KAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETAlpgafKTRKGM 642
Cdd:cd14912 476 KAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAGGGAKKGG-----KKKGSS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 643 FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14912 551 FQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 630
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 806638593 723 ILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14912 631 VLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
96-764 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 683.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 176 SGAGKTENTKKVIQYLAHVASSHKSKKD-------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 248
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 249 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAM 326
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLIttNPYD-YAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 327 RIMGIPEDEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQ 405
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 406 TKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 485
Cdd:cd14910 320 TVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 486 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKD 564
Cdd:cd14910 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 565 K--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriigldqvAGMSETALPGAFK--TRK 640
Cdd:cd14910 476 KveAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSG----------AAAAEAEEGGGKKggKKK 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 641 G-MFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQ 719
Cdd:cd14910 546 GsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQ 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 806638593 720 RYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14910 626 RYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
96-764 |
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: 675.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 176 SGAGKTENTKKVIQYLAHVASSHKskkdqgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 255
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 256 TYLLEKSRAIRQAKEERTFHIFYYLLSGAGE--HLKTDLLLEPYNKYRFLS-NGHVTIPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd14883 156 DYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDFDHLRLAMNVLGIP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 333 EDEQMGLLRVISGVLQLGNIVFKK-ERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 411
Cdd:cd14883 236 EEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEAR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 412 FAIEALAKATYERMFRWLVLRINKALDKTKRQGaSFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 491
Cdd:cd14883 316 DNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 492 YQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCII 571
Cdd:cd14883 395 YEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTEFGVK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 572 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDrIIGLDQVAGMSETALPGAfKTRKGMfRTVGQLYK 651
Cdd:cd14883 472 HYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPD-LLALTGLSISLGGDTTSR-GTSKGK-PTVGDTFK 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 652 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 731
Cdd:cd14883 549 HQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARSA 628
|
650 660 670
....*....|....*....|....*....|...
gi 806638593 732 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14883 629 DHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
96-764 |
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: 675.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 176 SGAGKTENTKKVIQYLAHVASSHKSKKD-------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 248
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEeaasgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 249 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAM 326
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLIttNPYD-FAFVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 327 RIMGIPEDEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQ 405
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 406 TKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 485
Cdd:cd14915 320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 486 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKD 564
Cdd:cd14915 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 565 KAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriiglDQVAGMSETALPGAFKTRKGM 642
Cdd:cd14915 476 KAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSG-------GQTAEAEGGGGKKGGKKKGSS 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 643 FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14915 549 FQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 628
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 806638593 723 ILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14915 629 VLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
96-764 |
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: 653.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 176 SGAGKTENTKKVIQYLAHVasshkSKKDQGELER---QLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGA 252
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAV-----SGGSESEVERvkdMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 253 NIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLE-PYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:cd01378 157 HITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQrPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 332 PEDEQMGLLRVISGVLQLGNIVFKKERNtDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVG---RDYVQKAQTKE 408
Cdd:cd01378 237 TEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSVYEVPLNVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 409 QADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILE 488
Cdd:cd01378 316 QAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 489 QEEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFP-KATDKSFVEKVVQEQGTHPKFQKPKQLKD--K 565
Cdd:cd01378 396 QEEYVREGIEWTPIKY-FNNKIICDLIEEK--PPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSGHFElrR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 566 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRiigldqvagmsetalpgafKTRKGMFRT 645
Cdd:cd01378 473 GEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD-------------------LDSKKRPPT 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 646 VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILT 725
Cdd:cd01378 534 AGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLS 613
|
650 660 670
....*....|....*....|....*....|....*....
gi 806638593 726 PNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01378 614 PKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
96-764 |
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: 650.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKgkKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 176 SGAGKTENTKKVIQYLAHVASshkskkDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 255
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGG------GSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 256 TYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLS-NGHVTIPGQQDKDMFQETMEAMRIMGIPED 334
Cdd:cd01383 154 TYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNqSNCLTIDGVDDAKKFHELKEALDTVGISKE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 335 EQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAI 414
Cdd:cd01383 234 DQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 415 EALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 494
Cdd:cd01383 314 DALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYEL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 495 EGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPkqlKDKAdFCIIHYA 574
Cdd:cd01383 394 DGIDWTKVDF-EDNQECLDLIEKK--PLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGE---RGGA-FTIRHYA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 575 GKVDYKADEWLMKNMDPLNDNIATLL----HQSSDKFVSELWKDVDRIigldqvagmsetALPGAFKTRKGMFRTVGQLY 650
Cdd:cd01383 467 GEVTYDTSGFLEKNRDLLHSDLIQLLsscsCQLPQLFASKMLDASRKA------------LPLTKASGSDSQKQSVATKF 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 651 KEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIp 730
Cdd:cd01383 535 KGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDV- 613
|
650 660 670
....*....|....*....|....*....|....
gi 806638593 731 KGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01383 614 SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
95-764 |
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: 632.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 174 GESGAGKTENTKKVIQYLAHVASshKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGG--RAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH-VTIPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd01384 159 IRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKcFELDGVDDAEEYRATRRAMDVVGIS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 333 EDEQMGLLRVISGVLQLGNIVFKKERNTDQASMPD---NTAAQKVSHLLGINVTDFTRGiLTPRIKVGRD-YVQKAQTKE 408
Cdd:cd01384 239 EEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDeksEFHLKAAAELLMCDEKALEDA-LCKRVIVTPDgIITKPLDPD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 409 QADFAIEALAKATYERMFRWLVLRINKAL--DKTKRqgaSFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 486
Cdd:cd01384 318 AATLSRDALAKTIYSRLFDWLVDKINRSIgqDPNSK---RLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 487 LEQEEYQREGIEWNFIDFgLDLQPCIDLIEKpaGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKqlKDKA 566
Cdd:cd01384 395 MEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPK--LSRT 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 567 DFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRiigldqvagmsetalPGAFKTRKgmFRTV 646
Cdd:cd01384 470 DFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR---------------EGTSSSSK--FSSI 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 647 GQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 726
Cdd:cd01384 533 GSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAP 612
|
650 660 670
....*....|....*....|....*....|....*...
gi 806638593 727 NsIPKGFMDGKQACVLMIKALELDSnlYRIGQSKVFFR 764
Cdd:cd01384 613 E-VLKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
95-764 |
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: 615.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 175 ESGAGKTENTKKVIQYLAHVASSHKSkkdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHSW------IEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH-VTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd01381 155 EQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNcLTCEGRDDAAEFADIRSAMKVLMFTD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 334 DEQMGLLRVISGVLQLGNIVFKK--ERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 411
Cdd:cd01381 235 EEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 412 FAIEALAKATYERMFRWLVLRINKALDKTKRQGAS--FIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQ 489
Cdd:cd01381 315 DVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 490 EEYQREGIEWNFIDFgLDLQPCIDLI-EKPAgppGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKAdF 568
Cdd:cd01381 395 EEYDKEGINWQHIEF-VDNQDVLDLIaLKPM---NIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNTS-F 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 569 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFvselwkdVDRIIGLDQVAGMSetalpgafkTRKGMfRTVGQ 648
Cdd:cd01381 470 GINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKF-------LKQLFNEDISMGSE---------TRKKS-PTLSS 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 649 LYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNS 728
Cdd:cd01381 533 QFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGI 612
|
650 660 670
....*....|....*....|....*....|....*.
gi 806638593 729 IPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01381 613 PPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
95-764 |
0e+00 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 594.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 174 GESGAGKTENTKKVIQYLAHVASSHkskkdQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSG-----AGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLlepynkyrflsnghvTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd01382 156 VSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL---------------KDPLLDDVGDFIRMDKAMKKIGLSD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 334 DEQMGLLRVISGVLQLGNIVFKKERNT-------DQASMPDNTAAqkvSHLLGINVTDF-----TRGILTPRIKVGRDYV 401
Cdd:cd01382 221 EEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYA---AELLGLDQDELrvsltTRVMQTTRGGAKGTVI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 402 QKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKrqGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFN 481
Cdd:cd01382 298 KVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 482 HTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPAGppGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKP-- 559
Cdd:cd01382 376 ERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSIPrk 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 560 ------KQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRiigldqvagMSETALP 633
Cdd:cd01382 453 sklkihRNLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTN---------NNKDSKQ 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 634 gafKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVV 713
Cdd:cd01382 524 ---KAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTS 600
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 806638593 714 FQEFRQRYEILTPNSIPKgfMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01382 601 FHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
95-764 |
0e+00 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 570.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 175 ESGAGKTENTKKVIQYLAHVASShkskkdQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGS------TNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGAST 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAgeHLKTDLLLEPYNKYRFLSNGH-VTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd14872 155 ENYLLEKSRVVYQIKGERNFHIFYQLLASP--DPASRGGWGSSAAYGYLSLSGcIEVEGVDDVADFEEVVLAMEQLGFDD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 334 DEQMGLLRVISGVLQLGNIVFKKERNTDQAS---MPDNTAAQKVSHLLGINVTDFTRGILTPRIKV-GRDYVQKAQTKEQ 409
Cdd:cd14872 233 ADINNVMSLIAAILKLGNIEFASGGGKSLVSgstVANRDVLKEVATLLGVDAATLEEALTSRLMEIkGCDPTRIPLTPAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 410 ADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQ 489
Cdd:cd14872 313 ATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 490 EEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFC 569
Cdd:cd14872 393 ALYQSEGVKFEHIDF-IDNQPVLDLIEKK--QPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVRTSRTEFI 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 570 IIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDriigldqvagmsetalpGAFKTRKGmfrTVGQL 649
Cdd:cd14872 470 VKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSE-----------------GDQKTSKV---TLGGQ 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 650 YKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILtPNSI 729
Cdd:cd14872 530 FRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFL-VKTI 608
|
650 660 670
....*....|....*....|....*....|....*.
gi 806638593 730 PKGFM-DGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14872 609 AKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
95-764 |
1.15e-179 |
|
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: 560.14 E-value: 1.15e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 175 ESGAGKTENTKKVIQYLAHVAsshksKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvNGYIVGANI 254
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN-----QRRNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVGAIT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNG-HVTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd01387 155 SQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFRRLLAAMQVLGFSS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 334 DEQMGLLRVISGVLQLGNIVFKKERNTDQ---ASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQA 410
Cdd:cd01387 235 EEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 411 DFAIEALAKATYERMFRWLVLRINKALDKTKRQGASfIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQE 490
Cdd:cd01387 315 LDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLS-IAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 491 EYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQlkDKADFCI 570
Cdd:cd01387 394 EYIREQIDWTEIAF-ADNQPVINLISKK--PVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRM--PLPEFTI 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 571 IHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKdvdriigldQVAGMSETALP----GAFKTRKGMFRTV 646
Cdd:cd01387 469 KHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFS---------SHRAQTDKAPPrlgkGRFVTMKPRTPTV 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 647 GQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 726
Cdd:cd01387 540 AARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVA 619
|
650 660 670
....*....|....*....|....*....|....*....
gi 806638593 727 NSIPKGfMDGKQACVLMIKALELD-SNLYRIGQSKVFFR 764
Cdd:cd01387 620 LKLPRP-APGDMCVSLLSRLCTVTpKDMYRLGATKVFLR 657
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
95-764 |
1.27e-178 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 557.47 E-value: 1.27e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQ----DREDQS 169
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 170 ILCTGESGAGKTENTKKVIQYLAHVASSHKSKKDQ-------------GELERQLLQANPILEAFGNAKTVKNDNSSRFG 236
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGegeaaseaieqtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 237 KFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDK 316
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 317 DMFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIVFKKERNTDQASmpDNTAAQKVSH---LLGINVTDFTRGILTPR 393
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQSLKLaaeLLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 394 IKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTN 473
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 474 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIE-KPAGPPGILALLDeECWFPKAT--DKSFVEKVVQEQ 550
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLHASF 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 551 GT-------------HPKFQKPKQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSdkfvselwkdvdr 617
Cdd:cd14890 476 GRksgsggtrrgssqHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR------------- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 618 iigldqvagmsetalpgafKTRKGMfrTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGV 697
Cdd:cd14890 542 -------------------RSIREV--SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGM 600
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 806638593 698 LEGIRICRQGFPNRVVFQEFRQRYEILTPNSipkgfMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14890 601 MEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
95-762 |
5.58e-174 |
|
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: 544.77 E-value: 5.58e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMY------KGKKRHEMPPHIYAITDTAYRSMMQDRE-- 166
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 167 --DQSILCTGESGAGKTENTKKVIQYLAHVASshKSKKDQGELER-----QLLQANPILEAFGNAKTVKNDNSSRFGKFI 239
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSS--ATTHGQNATERenvrdRVLESNPILEAFGNARTNRNNNSSRFGKFI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 240 RINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFL--SNGHVTIPGQQDKD 317
Cdd:cd14901 159 RLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQCYDRRDGVDDSV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 318 MFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIVF-KKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKV 396
Cdd:cd14901 239 QYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 397 GRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGAS-FIGILDIAGFEIFDLNSFEQLCINYTNEK 475
Cdd:cd14901 319 GGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCINFANEK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 476 LQQLFNHTMFILEQEEYQREGIEWNFIDFgldlqP----CIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKVVQEQG 551
Cdd:cd14901 399 LQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 552 THPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSElwkdvdriigldqvagmseta 631
Cdd:cd14901 472 KHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS--------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 632 lpgafktrkgmfrTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNR 711
Cdd:cd14901 531 -------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVR 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 806638593 712 VVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNL-----YRIGQSKVF 762
Cdd:cd14901 598 FPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIehlppFQVGKTKVF 653
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
95-764 |
6.65e-173 |
|
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: 543.12 E-value: 6.65e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 175 ESGAGKTENTKKVIQYLAHVasshkSKKDQGE-LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd01385 81 ESGSGKTESTNFLLHHLTAL-----SQKGYGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFL--SNGHvTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:cd01385 156 VEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLnqSDCY-TLEGEDEKYEFERLKQAMEMVGF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 332 PEDEQMGLLRVISGVLQLGNIVFKKER-NTDQASMPDNTAAQK-VSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQ 409
Cdd:cd01385 235 LPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDiISELLRVKEETLLEALTTKKTVTVGETLILPYKLPE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 410 ADFAIEALAKATYERMFRWLVLRINKAL----DKTKRQGASfIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 485
Cdd:cd01385 315 AIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 486 ILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPkQLKDK 565
Cdd:cd01385 394 KLEQEEYKKEGISWHNIEY-TDNTGCLQLISKK--PTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKP-QVMEP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 566 AdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELwkdvdriIGLDQVAGMSETALPGAFKT-----RK 640
Cdd:cd01385 470 A-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDPVAVFRWAVLRAFFRAmaafrEA 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 641 GMFR-----------------------------TVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQ 691
Cdd:cd01385 542 GRRRaqrtaghsltlhdrttksllhlhkkkkppSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQ 621
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 806638593 692 LRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILtpnsIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01385 622 LRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
95-764 |
7.87e-172 |
|
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: 538.98 E-value: 7.87e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 174 GESGAGKTENTKKVIQYLAHVAsshkskkdqGELE----RQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 249
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA---------GGLNdstiKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 250 VGANIETYLLEKSRAIRQAKEERTFHIFYYLLsgAGEHLKTDLLLEPYNKYRFL-SNGHVTIPGQQDKDMFQETMEAMRI 328
Cdd:cd14903 152 VGAKCRTYLLEKTRVISHERPERNYHIFYQLL--ASPDVEERLFLDSANECAYTgANKTIKIEGMSDRKHFARTKEALSL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 329 MGIPEDEQMGLLRVISGVLQLGNIVFKKERNTDQASM--PDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:cd14903 230 IGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 407 KEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 486
Cdd:cd14903 310 KDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 487 LEQEEYQREGIEWNFIDFgLDLQPCIDLIEkpaGPPGILALLDEECWFPKATDKSFVEKVVqeqGTHPKFQK----PKql 562
Cdd:cd14903 389 TVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQDviefPR-- 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdrIIGLDQVAGMSETALPGAFKTRKGM 642
Cdd:cd14903 460 TSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKE---KVESPAAASTSLARGARRRRGGALT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 643 FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14903 537 TTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFW 616
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 806638593 723 ILTPNSiPKGFMDGKQACVLMIKALELDS-NLYRIGQSKVFFR 764
Cdd:cd14903 617 LFLPEG-RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
96-764 |
3.46e-169 |
|
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: 530.70 E-value: 3.46e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 176 SGAGKTENTKKVIQYLAHVasshkSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 255
Cdd:cd01379 82 SGAGKTESANLLVQQLTVL-----GKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARIS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 256 TYLLEKSRAIRQAKEERTFHIFYYLLSG-AGEHLKTDLLLEPYNKYRFLSNGHVTIPG----QQDKDMFQETMEAMRIMG 330
Cdd:cd01379 157 EYLLEKSRVVHQAIGERNFHIFYYIYAGlAEDKKLAKYKLPENKPPRYLQNDGLTVQDivnnSGNREKFEEIEQCFKVIG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 331 IPEDEQMGLLRVISGVLQLGNIVFK---KERNTDQASM-PDNTAAQKVSHLLGINVTDFtRGILTPRIKVGR-DYVQKAQ 405
Cdd:cd01379 237 FTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRiSNPEALNNVAKLLGIEADEL-QEALTSHSVVTRgETIIRNN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 406 TKEQADFAIEALAKATYERMFRWLVLRINKAL--DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 483
Cdd:cd01379 316 TVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 484 MFILEQEEYQREGIEWNFIDFGlDLQPCID-LIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQGTHPkFQKPKql 562
Cdd:cd01379 396 IFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKFHNNIKSKY-YWRPK-- 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSElwkdvdriigldqvagmsetalpgafktrkgm 642
Cdd:cd01379 469 SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ-------------------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 643 frTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd01379 517 --TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYY 594
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 806638593 723 ILTPNSIPKGFMDgKQACVLMIKALELDSnlYRIGQSKVFFR 764
Cdd:cd01379 595 FLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
95-764 |
1.45e-168 |
|
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: 529.26 E-value: 1.45e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKK-RHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 174 GESGAGKTENTKKVIQYLahvasSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd14897 81 GESGAGKTESTKYMIKHL-----MKLSPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQD-------KDMFQETMEAM 326
Cdd:cd14897 156 IDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDseeleyyRQMFHDLTNIM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 327 RIMGIPEDEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:cd14897 236 KLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 407 KEQADFAIEALAKATYERMFRWLVLRINKAL----DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNH 482
Cdd:cd14897 316 LRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFND 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 483 TMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKql 562
Cdd:cd14897 396 YVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFKK--PLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVASP-- 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKdvdriigldqvagmsetalpgafktrkgm 642
Cdd:cd14897 471 GNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT----------------------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 643 frtvgQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14897 522 -----SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYK 596
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 806638593 723 ILTPNSiPKGFMDGKQACVLMIKALELDSnlYRIGQSKVFFR 764
Cdd:cd14897 597 EICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
95-726 |
1.27e-167 |
|
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: 527.72 E-value: 1.27e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVDMYKgKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 174 GESGAGKTENTKKVIQYLAHVASSHKSKKDQgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD--------- 244
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRSL--VEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSklkskrmsg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 245 VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSN------------------- 305
Cdd:cd14888 158 DRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGAdakpisidmssfephlkfr 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 306 -----GHVTIPGQQDKDMFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQ---KVSHL 377
Cdd:cd14888 238 yltksSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDdleKVASL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 378 LGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFE 457
Cdd:cd14888 318 LGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGVLDIFGFE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 458 IFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPPGILALLDEECWFPKA 537
Cdd:cd14888 398 CFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFCMLDEECFVPGG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 538 TDKSFVEKVVQEQGTHPKFQKPKqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKD-VD 616
Cdd:cd14888 475 KDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSAyLR 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 617 RIIGLdqvagmsetalpgafKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNG 696
Cdd:cd14888 553 RGTDG---------------NTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGG 617
|
650 660 670
....*....|....*....|....*....|
gi 806638593 697 VLEGIRICRQGFPNRVVFQEFRQRYEILTP 726
Cdd:cd14888 618 VLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
95-764 |
1.89e-167 |
|
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: 526.67 E-value: 1.89e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 174 GESGAGKTENTKKVIQYLAHVASSH---KSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 250
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSlelSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 251 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLS-NGHVTIPGQQDKDMFQETMEAMRIM 329
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 330 GIPEDEQMGLLRVISGVLQLGNIVFKkerNTDQASMPDNTAAQKVSHLLGINVTDFTRgILTPRIKVGR-DYVQKAQTKE 408
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTD-ALTQRSMFLRgEEILTPLNVQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 409 QADFAIEALAKATYERMFRWLVLRINKALdkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILE 488
Cdd:cd14873 317 QAVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 489 QEEYQREGIEWNFIDFgLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDkaDF 568
Cdd:cd14873 395 QLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVN--NF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 569 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWkdvdriiglDQVAGMSETALPGAFKTRKGmfRTVGQ 648
Cdd:cd14873 469 GVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLF---------EHVSSRNNQDTLKCGSKHRR--PTVSS 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 649 LYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNS 728
Cdd:cd14873 538 QFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNL 617
|
650 660 670
....*....|....*....|....*....|....*.
gi 806638593 729 IPKGFMDGKqaCVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14873 618 ALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
95-764 |
2.15e-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: 521.24 E-value: 2.15e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEM---PPHIYAITDTAYRSMMQDR----ED 167
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 168 QSILCTGESGAGKTENTKKVIQYLA----HVASSHKSKKDQG---ELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 240
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLAtaskLAKGASTSKGAANaheSIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 241 INFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH-VTIPGQQDKDMF 319
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNcVEVDGVDDATEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 320 QETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIVFkkERNTDQ----ASMPDNTAAQKVSHLLGINVTDFTRGILTPRIK 395
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 396 VGRDYV-QKAQTKEQADFAIEALAKATYERMFRWLVLRINKAldkTKRQG------------ASFIGILDIAGFEIFDLN 462
Cdd:cd14892 319 TARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINAC---HKQQTsgvtggaasptfSPFIGILDIFGFEIMPTN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 463 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFP-KATDKS 541
Cdd:cd14892 396 SFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDKQ 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 542 FVEKVVQEQ-GTHPKFQKPKQLKDkaDFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDkfvselwkdvdriig 620
Cdd:cd14892 473 LLTIYHQTHlDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK--------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 621 ldqvagmsetalpgafktrkgmFRTvgqlykeQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEG 700
Cdd:cd14892 536 ----------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEV 586
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 701 IRICRQGFPNRVVFQEFRQRYEILTPNS-IPKGFMDGKQACVLMIKALE-----LDSNLYRIGQSKVFFR 764
Cdd:cd14892 587 VRIRREGFPIRRQFEEFYEKFWPLARNKaGVAASPDACDATTARKKCEEivaraLERENFQLGRTKVFLR 656
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
97-764 |
1.21e-152 |
|
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: 486.72 E-value: 1.21e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 97 VLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMM----QDREDQSILC 172
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 173 TGESGAGKTENTKKVIQYLAHVAsshkskKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvNGYIVGA 252
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC------RGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHVKGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 253 NIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHvtipGQQD-----KDMFQETMEAMR 327
Cdd:cd14889 156 KINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGA----GCKRevqywKKKYDEVCNAMD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 328 IMGIPEDEQMGLLRVISGVLQLGNIVFKkerntdqasmPDNTAAQKVSH-------------------LLG--INVTDFT 386
Cdd:cd14889 232 MVGFTEQEEVDMFTILAGILSLGNITFE----------MDDDEALKVENdsngwlkaaagqfgvseedLLKtlTCTVTFT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 387 RGiltprikvgrDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQG--ASFIGILDIAGFEIFDLNSF 464
Cdd:cd14889 302 RG----------EQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRF 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 465 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFVE 544
Cdd:cd14889 372 EQACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLFL--NKPIGILSLLDEQSHFPQATDESFVD 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 545 KVVQEQGTHPKFQKPKQLKDKadFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWK-DVDRIIGLDQ 623
Cdd:cd14889 449 KLNIHFKGNSYYGKSRSKSPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTaTRSRTGTLMP 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 624 VAGMSETALPGAFKTRKgmfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRI 703
Cdd:cd14889 527 RAKLPQAGSDNFNSTRK---QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRI 603
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 806638593 704 CRQGFPNRVVFQEFRQRYEIL--TPNsIPKgfmdGKQACVLMIKALELDSnlYRIGQSKVFFR 764
Cdd:cd14889 604 RREGFSWRPSFAEFAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
95-727 |
9.77e-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: 476.06 E-value: 9.77e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVDMYKGKKRH--------EMPPHIYAITDTAYRSMMQDR 165
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 166 EDQSILCTGESGAGKTENTKKVIQYLAHVASSHKSK--------------KDQGELERQLLQANPILEAFGNAKTVKNDN 231
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSeevltltssiratsKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 232 SSRFGKFIRINFD-VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDL-LLEPYNKYRFLS---NG 306
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLgLKNQLSGDRYDYlkkSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 307 HVTIPGQQDKDMFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIVFKKERNTDQA--SMPDNTAAQKVSHLLGINVTD 384
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSpcCVKNKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 385 FTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKAL-------DKTKRQGASFIGILDIAGFE 457
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 458 IFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFP 535
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 536 KATDKSFVEKVVQEQGTHPKFQKPKQLKdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDV 615
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKIN-KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 616 DRiigldqvagmSETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCN 695
Cdd:cd14907 557 DG----------SQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYL 626
|
650 660 670
....*....|....*....|....*....|..
gi 806638593 696 GVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 727
Cdd:cd14907 627 GVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
96-730 |
1.26e-145 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 465.94 E-value: 1.26e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVDMY-----------KGKKRHEMPPHIYAITDTAYRSMMQ 163
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 164 ----DREDQSILCTGESGAGKTENTKKVIQYLAHV-----ASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSR 234
Cdd:cd14900 82 glngVMSDQSILVSGESGSGKTESTKFLMEYLAQAgdnnlAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 235 FGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEhlktdlllepynkyrflsnghvtipGQQ 314
Cdd:cd14900 162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE-------------------------AAR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 315 DKDMFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIVFKKERNTD-QASMPDNTAAQKV------SHLLGINVTDFTR 387
Cdd:cd14900 217 KRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLSVDATKLEK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 388 GILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKAL---DKTKRQGAS-FIGILDIAGFEIFDLNS 463
Cdd:cd14900 297 ALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFGFEVFPKNS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 464 FEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFV 543
Cdd:cd14900 377 FEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMPKGSDTTLA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 544 EKVVQEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDplndniatLLHQSSdkfvselwkdVDriigldq 623
Cdd:cd14900 454 SKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQEA----------VD------- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 624 vagmsetalpgafktrkgMFRTVGQlYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRI 703
Cdd:cd14900 509 ------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRV 569
|
650 660
....*....|....*....|....*..
gi 806638593 704 CRQGFPNRVVFQEFRQRYEILTPNSIP 730
Cdd:cd14900 570 ARAGFPIRLLHDEFVARYFSLARAKNR 596
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
95-764 |
1.55e-144 |
|
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: 463.75 E-value: 1.55e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERyySGLI----YTYSGLFCVVINPYKNLPiysEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDRE---D 167
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 168 QSILCTGESGAGKTENTKKVIQYLAH--VASSHKSKKDQG-----------ELERQLLQANPILEAFGNAKTVKNDNSSR 234
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTraVGGKKASGQDIEqsskkrklsvtSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 235 FGKFIRINFDVNGY-IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLS-NGHVTIPG 312
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 313 QQDKDMFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIVFKK----ERNTDQASMPDNTAAQKVSHLLGINVTDFTRG 388
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEedtsEGEAEIASESDKEALATAAELLGVDEEALEKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 389 ILTPRIkVGRDYVQKAQ-TKEQADFAIEALAKATYERMFRWLVLRINKALDKtKRQGASFIGILDIAGFEIFDL-NSFEQ 466
Cdd:cd14891 316 ITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFETkNDFEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 467 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKV 546
Cdd:cd14891 394 LLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIA--SKPNGILPLLDNEARNPNPSDAKLNETL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 547 VQEQGTHPKFQKPKQlKDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHqSSDKFVselwkdvdriigldqva 625
Cdd:cd14891 471 HKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLA-SSAKFS----------------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 626 gmsetalpgafktrkgmfrtvgqlykEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICR 705
Cdd:cd14891 532 --------------------------DQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLK 585
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 706 QGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIK-ALELDSNLYRIGQSKVFFR 764
Cdd:cd14891 586 VGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTLTQAILwAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
95-764 |
3.80e-142 |
|
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: 457.48 E-value: 3.80e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 174 GESGAGKTENTKKVIQYLAHVASSHKSKKDQgelerQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKDKTIA-----KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFL--SNGHVTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:cd14904 156 CETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKLFASTQKSLSLIGL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 332 PEDEQMGLLRVISGVLQLGNIVFkKERNTDQASMPDNTAAQKVSHLLGINVTDFtRGILTPRIKVGR-DYVQKAQTKEQA 410
Cdd:cd14904 236 DNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVAKMLGLPTTRI-EEALCNRSVVTRnESVTVPLAPVEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 411 DFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQE 490
Cdd:cd14904 314 EENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 491 EYQREGIEWNFIDFGlDLQPCIDLIEkpaGPPGILALLDEECWFPKATDKSFVEKV---VQEQGTHPKFQKPKQlkDKAD 567
Cdd:cd14904 394 EYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESIDFPKV--KRTQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 568 FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDriigldqvaGMSETALPGAFKTRKGMfRTVG 647
Cdd:cd14904 468 FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE---------APSETKEGKSGKGTKAP-KSLG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 648 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 727
Cdd:cd14904 538 SQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPP 617
|
650 660 670
....*....|....*....|....*....|....*...
gi 806638593 728 SIPKGfmDGKQACVLMIKALELDSNL-YRIGQSKVFFR 764
Cdd:cd14904 618 SMHSK--DVRRTCSVFMTAIGRKSPLeYQIGKSLIYFK 653
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
95-764 |
2.97e-140 |
|
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: 451.54 E-value: 2.97e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 175 ESGAGKTENTKKVIQYLahvaSSHKSKKDQGELeRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvNGYIVGANI 254
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL----SSLYQDQTEDRL-RQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVGASV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHV-TIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd14896 155 SHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFEGLLKALQGLGLCA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 334 DEQMGLLRVISGVLQLGNIVFKKERNTDQ--ASMPDNTAAQKVSHLLGINvTDFTRGILTPRIKV-GRDYVQKAQTKEQA 410
Cdd:cd14896 235 EELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVP-PERLEGAVTHRVTEtPYGRVSRPLPVEGA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 411 DFAIEALAKATYERMFRWLVLRINKALDKTKRQGA-SFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQ 489
Cdd:cd14896 314 IDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 490 EEYQREGIEWNFIDfGLDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQlkDKADFC 569
Cdd:cd14896 394 EECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQL--PLPVFT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 570 IIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGmsetalpgafktrkgmfrTVGQL 649
Cdd:cd14896 469 VRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP------------------TLASR 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 650 YKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSI 729
Cdd:cd14896 531 FQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQ 610
|
650 660 670
....*....|....*....|....*....|....*
gi 806638593 730 PkGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14896 611 E-ALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
95-747 |
5.64e-139 |
|
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: 450.88 E-value: 5.64e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVDMYK--------GKKRHEMPPHIYAITDTAYRSMMQ-D 164
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 165 REDQSILCTGESGAGKTENTKKVIQYLAHV----ASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 240
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVgrdqSSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 241 INFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVT---IPGQQDKD 317
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSYGPSfarKRAVADKY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 318 --MFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIVFKKE-RNTDQASMPDNTAAQ--KVSHLLGINVTDFTRGILTP 392
Cdd:cd14902 241 aqLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAEnGQEDATAVTAASRFHlaKCAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 393 RIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALD--------KTKRQGASFIGILDIAGFEIFDLNSF 464
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFESLNRNGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 465 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVE 544
Cdd:cd14902 401 EQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDK--SNGLFSLLDQECLMPKGSNQALST 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 545 KVVQEQGThpkfqkpkqlkdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSelwkdvdrIIGLDQV 624
Cdd:cd14902 478 KFYRYHGG------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVV--------AIGADEN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 625 AGMSETALPGAFKTRKGMFRT--VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIR 702
Cdd:cd14902 538 RDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVR 617
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 806638593 703 ICRQGFPNRVVFQEFRQRYEIL-----TPNSIPK-GFMDGKQA--CVLMIKAL 747
Cdd:cd14902 618 IARHGYSVRLAHASFIELFSGFkcflsTRDRAAKmNNHDLAQAlvTVLMDRVL 670
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
95-764 |
3.22e-134 |
|
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: 436.26 E-value: 3.22e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYK--GKKRHE-------MPPHIYAITDTAYRSMMQD- 164
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 165 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHK-SKKDQGELER-----QLLQANPILEAFGNAKTVKNDNSSRFGKF 238
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEgAPNEGEELGKlsimdRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 239 IRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGE--------HLKTDLLLEPYNKYRFLSNGHVTI 310
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEeehekyefHDGITGGLQLPNEFHYTGQGGAPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 311 PGQ-QDKDMFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIVFKKERNtDQASMPDNTAAQK----VSHLLGINVTDF 385
Cdd:cd14908 241 LREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEE-DGAAEIAEEGNEKclarVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 386 TRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGA-SFIGILDIAGFEIFDLNSF 464
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 465 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFP-KATDKSFV 543
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQAK--KKGILTMLDDECRLGiRGSDANYA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 544 EKVV--------QEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLM-KNMDPLNdniatllhqssdkfvselwkd 614
Cdd:cd14908 477 SRLYetylpeknQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP--------------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 615 vdriigldqvagmsetalpgafKTRKGMFRTvGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRC 694
Cdd:cd14908 536 ----------------------LTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRY 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 695 NGVLEGIRICRQGFPNRVVFQEFRQRYEILTPnSIPK----GFMDGKQACVLMIKALELDSNLYR--------------- 755
Cdd:cd14908 593 GGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlsWSMERLDPQKLCVKKMCKDLVKGVlspamvsmknipedt 671
|
730
....*....|.
gi 806638593 756 --IGQSKVFFR 764
Cdd:cd14908 672 mqLGKSKVFMR 682
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
93-821 |
6.77e-133 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 437.15 E-value: 6.77e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 93 NEASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHE-MPPHIYAITDTAYRSMMQDREDQSIL 171
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 172 CTGESGAGKTENTKKVIQYLAhvasSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA----SSKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRY 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:PTZ00014 264 GSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDSMGL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 332 PEDEQMGLLRVISGVLQLGNIVF--KKERNTDQASM--PDNTAA-QKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:PTZ00014 344 SESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESLEVfNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWS 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 407 KEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGAsFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 486
Cdd:PTZ00014 424 KDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFE 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 487 LEQEEYQREGIEWNFIDFgLDLQPCIDLI-EKPAgppGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDK 565
Cdd:PTZ00014 503 RESKLYKDEGISTEELEY-TSNESVIDLLcGKGK---SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKVDSNK 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 566 aDFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGldqvagmsetalpgafKTRKGMFrt 645
Cdd:PTZ00014 579 -NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKG----------------KLAKGQL-- 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 646 VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILT 725
Cdd:PTZ00014 640 IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLD 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 726 PNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR---AGVLAHLEEERDLKITDVIIGFQACCRGYLARKAFAKR 802
Cdd:PTZ00014 720 LAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKKKRKVRKN 799
|
730
....*....|....*....
gi 806638593 803 qqqltaMKVLQRNCaAYLR 821
Cdd:PTZ00014 800 ------IKSLVRIQ-AHLR 811
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
96-764 |
6.25e-131 |
|
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: 427.83 E-value: 6.25e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPiyseeivDMYKGKKRHE-------MPPHIYAITDTAYRSMMQ----- 163
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 164 --DREDQSILCTGESGAGKTENTKKVIQYLA----HVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGK 237
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAesskHTTATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 238 FIRINF-----DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYN--KYRFLSNG--HV 308
Cdd:cd14895 155 FVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQYISGGqcYQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 309 TIPGQQDKDMFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIVFKKERNTD---------------QASMPDNTAAQK 373
Cdd:cd14895 235 RNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSSLTVQQH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 374 ---VSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTK--------- 441
Cdd:cd14895 315 ldiVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQfalnpnkaa 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 442 -RQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPCIDLIEkpAG 520
Cdd:cd14895 395 nKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLE--QR 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 521 PPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKqlKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIAT 598
Cdd:cd14895 472 PSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEGFCEKNKDQPNAELFS 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 599 LLHQSSDKFVSELWKDVDRIIGLDQVAGMSETalpgafKTRKGMFRTV--GQLYKEQLAKLMATLRNTNPNFVRCIIPNH 676
Cdd:cd14895 550 VLGKTSDAHLRELFEFFKASESAELSLGQPKL------RRRSSVLSSVgiGSQFKQQLASLLDVVQQTQTHYIRCIKPND 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 677 EKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELdsnlyri 756
Cdd:cd14895 624 ESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASALIETLKVDHAEL------- 696
|
....*...
gi 806638593 757 GQSKVFFR 764
Cdd:cd14895 697 GKTRVFLR 704
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
95-764 |
1.11e-125 |
|
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: 412.47 E-value: 1.11e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 175 ESGAGKTENTKKVIQYLAHVASSHKSKkdqgeLERQLLQA-NPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV-----LSVEKLNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKyrflSNGHVTIPGQQDKDM------FQETMEAMR 327
Cdd:cd01386 156 IQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAE----SNSFGIVPLQKPEDKqkaaaaFSKLQAAMK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 328 IMGIPEDEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGI------------LTPRIK 395
Cdd:cd01386 232 TLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpqqsTTSSGQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 396 VGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALdKTKRQGASFIGILDIAGFEifdlN----------SFE 465
Cdd:cd01386 312 ESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSL-SSSHHSTSSITIVDTPGFQ----NpahsgsqrgaTFE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 466 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAG------------PPGILALLDEECW 533
Cdd:cd01386 387 DLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPQqalvrsdlrdedRRGLLWLLDEEAL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 534 FPKATDKSFVEKVVQEQG--THPKFQKPKQLKDKA-DFCIIHYAGK--VDYKADEWLMK-NMDPLNDNIATLLHQSSDKF 607
Cdd:cd01386 467 YPGSSDDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQESQKET 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 608 vselwkdvdriigldqvagmsetalpgAFKTRKGMFRTVgqlyKEQLAKLMATLRNTNPNFVRCIIPNHE------KKAG 681
Cdd:cd01386 547 ---------------------------AAVKRKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQHNagkderSTSS 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 682 KLDPHLVLD------QLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGF-----MDGKQACVLMIKALELD 750
Cdd:cd01386 596 PAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEELLEELDLE 675
|
730
....*....|....
gi 806638593 751 SNLYRIGQSKVFFR 764
Cdd:cd01386 676 KSSYRIGLSQVFFR 689
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
95-762 |
2.49e-124 |
|
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: 407.07 E-value: 2.49e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRH-EMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 174 GESGAGKTENTKKVIQYLAhvasSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA----SAKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLsNGHVT-IPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd14876 157 VVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFL-NPKCLdVPGIDDVADFEEVLESLKSMGLT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 333 EDEQMGLLRVISGVLQLGNIVFKKErntDQASMPDntAA----------QKVSHLLGINVTDFTRGILTPRIKVGRDYVQ 402
Cdd:cd14876 236 EEQIDTVFSIVSGVLLLGNVKITGK---TEQGVDD--AAaisneslevfKEACSLLFLDPEALKRELTVKVTKAGGQEIE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 403 KAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGAsFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNH 482
Cdd:cd14876 311 GRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKN-FMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFID 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 483 TMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPAGppGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFqKPKQL 562
Cdd:cd14876 390 IVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKF-KPAKV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGldqvagmsetalpgafKTRKGM 642
Cdd:cd14876 466 DSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKG----------------KIAKGS 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 643 FrtVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14876 530 L--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFK 607
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 806638593 723 ILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVF 762
Cdd:cd14876 608 FLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
95-762 |
4.40e-123 |
|
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: 403.85 E-value: 4.40e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVDMYKGKKR-HEMPPHIYAITDTAYRSMMQDRE--DQSI 170
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 171 LCTGESGAGKTENTKKVIQYLAHVASSHKSKKDQGELER---QLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 247
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAERieqRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 248 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIpgqqDKDMFQETMEAMR 327
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNL----EEDCFEVTREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 328 IMGIPEDEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVS---HLLGINVTDFTRGILTPRIKVGRDYV--Q 402
Cdd:cd14880 237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTKESVRtsaLLLKLPEDHLLETLQIRTIRAGKQQQvfK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 403 KAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNH 482
Cdd:cd14880 317 KPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 483 TMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQL 562
Cdd:cd14880 397 HYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALpgafktrkgm 642
Cdd:cd14880 474 SREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQSRAPV---------- 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 643 fRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14880 544 -LTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYK 622
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 806638593 723 ILTPN--SIPKGFMDGKQAcvlmikalELDSNLYRIGQSKVF 762
Cdd:cd14880 623 LLRRLrpHTSSGPHSPYPA--------KGLSEPVHCGRTKVF 656
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
95-760 |
3.73e-121 |
|
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: 400.51 E-value: 3.73e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVDMYKGKKR-HEMPPHIYAITDTAYRSMMQDREDQSILC 172
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 173 TGESGAGKTENTKKVIQYLAHVASSHKSKK-----DQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-VN 246
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQNnnnnnNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRsSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 247 GYIVGANIETYLLEKSR-AIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEP-YNKYRFL--------------SNGHVTI 310
Cdd:cd14906 161 GKIDGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvissfksqsSNKNSNH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 311 PGQQDKD-MFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIVFKKERNTDQAS--MPDNTAA-QKVSHLLGINVTDFT 386
Cdd:cd14906 241 NNKTESIeSFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 387 RGILTPRIKV-GRDYVQ-KAQTKEQADFAIEALAKATYERMFRWLVLRINKALDK----------TKRQGASFIGILDIA 454
Cdd:cd14906 321 QALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 455 GFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPAGppGILALLDEECWF 534
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSLLDDECIM 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 535 PKATDKSFVEKVVQEQGTHPKFQkpKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKd 614
Cdd:cd14906 478 PKGSEQSLLEKYNKQYHNTNQYY--QRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQ- 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 615 vdriigldqvagMSETALPGAFKTRKGMFRTVGQlYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRC 694
Cdd:cd14906 555 ------------QQITSTTNTTKKQTQSNTVSGQ-FLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRN 621
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 806638593 695 NGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSK 760
Cdd:cd14906 622 VGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIQSKLKTMGISNNK 687
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
95-764 |
1.49e-112 |
|
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: 374.15 E-value: 1.49e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYS-GLIYTYSGLFCVVINPYKNLPIYSEEIVDMY-KGKKRHEMPPHIYAITDTAYRSM-MQDREDQSIL 171
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 172 CTGESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQ----LLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-VN 246
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSNTSQRSIADKidenLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDpTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 247 GYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDL-LLEPYNKYRFLSNGHVTI----PGQ--QDKDMF 319
Cdd:cd14875 161 GVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTFVrrgvDGKtlDDAHEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 320 QETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIVFKKERNtDQASMPDNTAAQKVSHLLGINVTDFTRGILtprIKVGRD 399
Cdd:cd14875 241 QNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL---VKSKTS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 400 YVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALD-KTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQ 478
Cdd:cd14875 317 LVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 479 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKVVQE-QGTHPKFQ 557
Cdd:cd14875 397 HYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLWDQwANKSPYFV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 558 KPKQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELwkdvdriigLDQVAGMSEtalpgafk 637
Cdd:cd14875 474 LPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTL---------LSTEKGLAR-------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 638 tRKgmfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEF 717
Cdd:cd14875 536 -RK---QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQF 611
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 806638593 718 RQRYEILTPNSIPKGFMDGK--QACVLMI----KALELDSNLYRIGQSKVFFR 764
Cdd:cd14875 612 CRYFYLIMPRSTASLFKQEKysEAAKDFLayyqRLYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
95-764 |
7.06e-110 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 365.75 E-value: 7.06e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVDMYKGKKRH-----EMPPHIYAITDTAYRSMMQDREDQ 168
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 169 SILCTGESGAGKTENTKKVIQYLAHVASSHKSKkdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 248
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSSTD-----VQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 249 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHV-TIPGQQDKDMFQETMEAMR 327
Cdd:cd14886 156 LKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGIDDQKEFAPVRSQLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 328 IMgIPEDEQMGLLRVISGVLQLGNIVFKKERN--TDQASMPDNTAA-QKVSHLLGINVTDFTRGILTPRIKVGRDYVQKA 404
Cdd:cd14886 236 KL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIITKVVVINNETIISP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 405 QTKEQADFAIEALAKATYERMFRWLVLRINKALdKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTM 484
Cdd:cd14886 315 VTQAQAEVNIRAVAKDLYGALFELCVDTLNEII-QFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 485 FILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPAgpPGILALLDEECWFPKATDKSFVE---KVVQEQGTHPKfqKPKQ 561
Cdd:cd14886 394 FKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPN--LSIFSFLEEQCLIQTGSSEKFTSsckSKIKNNSFIPG--KGSQ 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 562 LKdkadFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLdqvagmsetalpgafktRKG 641
Cdd:cd14886 469 CN----FTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGN-----------------MKG 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 642 MFrtVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 721
Cdd:cd14886 528 KF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRN 605
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 806638593 722 EILT--PNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14886 606 KILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
95-721 |
1.91e-106 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 358.25 E-value: 1.91e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVDMY----------KGKKRHEMPPHIYAITDTAYRSMMQ 163
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 164 DREDQSILCTGESGAGKTENTKKVIQYLA------------HVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDN 231
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAvhcgtgnnnltnSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 232 SSRFGKFIRINF-DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSG-----AGEHLKTDLLLEPYNKYRFLSN 305
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 306 GHVTI--PGQQDKDMFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIVF-----KKERNT--DQASMPDNTAA----- 371
Cdd:cd14899 241 SLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVMSSTTGafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 372 QKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKAL-------------- 437
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 438 DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEK 517
Cdd:cd14899 401 VDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 518 PagPPGILALLDEECWFPKATDKSFVEKV---VQEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLND 594
Cdd:cd14899 480 R--PIGIFSLTDQECVFPQGTDRALVAKYyleFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 595 NIATLLHQSSDKFVSELWKDVDRiiglDQVAGMSETALPGAFKTRKGMFRT----VGQLYKEQLAKLMATLRNTNPNFVR 670
Cdd:cd14899 558 SAAQLLAGSSNPLIQALAAGSND----EDANGDSELDGFGGRTRRRAKSAIaavsVGTQFKIQLNELLSTVRATTPRYVR 633
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 806638593 671 CIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 721
Cdd:cd14899 634 CIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
95-764 |
3.82e-100 |
|
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: 340.09 E-value: 3.82e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYS--------GLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDRE 166
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 167 DQSILCTGESGAGKTENTKKVIQYLAHVASSHKSKKDQGeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVN 246
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG-LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 247 GYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLlepynkyrflsnghvtiPGQQDKDMF--QETME 324
Cdd:cd14887 160 GKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSS-----------------AGEGDPESTdlRRITA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 325 AMRIMGIPEDEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTA--------AQKVSHLL-------GINVTDFTRGI 389
Cdd:cd14887 223 AMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSevkclssGLKVTEASRKH 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 390 LT--------PRIKVGRDYV------------QKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKR------- 442
Cdd:cd14887 303 LKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesdsd 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 443 ------QGASFIGILDIAGFEIF---DLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI--DFGLDLQPC 511
Cdd:cd14887 383 edtpstTGTQTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsAFPFSFPLA 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 512 IDLIEKPA---------------------GPPGILALLDE------ECWFPKATDKSFVEKVVQEQGTHPKFQK--PKQL 562
Cdd:cd14887 463 STLTSSPSstspfsptpsfrsssafatspSLPSSLSSLSSslssspPVWEGRDNSDLFYEKLNKNIINSAKYKNitPALS 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLhQSSDKFVSElwkdvdriIGLDQVAGMSetalpgAFKTRKgm 642
Cdd:cd14887 543 RENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYTRL--------VGSKKNSGVR------AISSRR-- 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 643 fRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14887 606 -STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYE 684
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 806638593 723 ILTPNSIpKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14887 685 TKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
92-763 |
1.23e-97 |
|
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: 330.28 E-value: 1.23e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 92 LNEASVLHNLKERYYSGLIYTY---SGLfcVVINPYKNLPI--------YSEEIVDMYKGKKRHEMPpHIYAITDTAYRS 160
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSnsdaslgeYGSEYYDTTSGSKEPLPP-HAYDLAARAYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 161 MMQDREDQSILCTGESGAGKTENTKKVIQYLAHVaSSHKSKKDQgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 240
Cdd:cd14879 78 MRRRSEDQAVVFLGETGSGKSESRRLLLRQLLRL-SSHSKKGTK--LSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 241 INFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFL--SNGHVT--IPGQQDK 316
Cdd:cd14879 155 LQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasYGCHPLplGPGSDDA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 317 DMFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIVF--KKERNTDQASMpDNTAA-QKVSHLLGINVTDFtRGILTPR 393
Cdd:cd14879 235 EGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVV-KNTDVlDIVAAFLGVSPEDL-ETSLTYK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 394 IK-VGRD----YVQKAQTKEQADfaieALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFD---LNSFE 465
Cdd:cd14879 313 TKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQNRSstgGNSLD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 466 QLCINYTNEKLQ-----QLFNHTMFILEQEEYQREGIEWNfidfglDLQPCIDLIEKPAGppGILALLDEEC-WFPKATD 539
Cdd:cd14879 389 QFCVNFANERLHnyvlrSFFERKAEELEAEGVSVPATSYF------DNSDCVRLLRGKPG--GLLGILDDQTrRMPKKTD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 540 KSFVEKVVQEQGTHPKF---QKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLndniatllhqSSDkFVSelwkdvd 616
Cdd:cd14879 461 EQMLEALRKRFGNHSSFiavGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVL----------SPD-FVN------- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 617 riigldqvagmsetalpgafktrkgMFRTVGQLyKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNG 696
Cdd:cd14879 523 -------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLG 576
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 806638593 697 VLEGIRICRQGFPNRVVFQEFRQRYEILTPnsipkgFMDGKQACVLMIKALELDSNLYRIGQSKVFF 763
Cdd:cd14879 577 LPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
95-764 |
8.93e-97 |
|
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: 327.36 E-value: 8.93e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEivdmYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 175 ESGAGKTENTKKVIQ-YLAHVasshkskKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd14937 77 ESGSGKTEASKLVIKyYLSGV-------KEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIpE 333
Cdd:cd14937 150 IEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMNM-H 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 334 DEQMGLLRVISGVLQLGNIVFK---KERNTDQASMPDNT--AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKE 408
Cdd:cd14937 229 DMKDDLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 409 QADFAIEALAKATYERMFRWLVLRINKALDKTKrQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILE 488
Cdd:cd14937 309 ESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 489 QEEYQREGIEWNFIDFGLDlQPCIDLIEkpaGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKaDF 568
Cdd:cd14937 388 TELYKAEDILIESVKYTTN-ESIIDLLR---GKTSIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINK-NF 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 569 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDriigldqvagMSETAlpgafkTRKGMfrtVGQ 648
Cdd:cd14937 463 VIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVE----------VSESL------GRKNL---ITF 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 649 LYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRIcRQGFPNRVVFQEFRQRYEILTPNS 728
Cdd:cd14937 524 KYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYST 602
|
650 660 670
....*....|....*....|....*....|....*.
gi 806638593 729 IPKGFMDGKQACVLMIKAlELDSNLYRIGQSKVFFR 764
Cdd:cd14937 603 SKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
96-726 |
2.37e-96 |
|
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: 324.16 E-value: 2.37e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNlpIYSEEIVDMYKGKKRHeMPPHIYAITDTAYRSMMQdREDQSILCTGE 175
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 176 SGAGKTENTKKVIQYLAHVASSHKSkkdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvnGYIVGANIE 255
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTTS------IEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 256 TYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDlllepYNKYRF-LSNGHVTIPGQQDKDMFQETMEAMRIMGIPED 334
Cdd:cd14898 150 TYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKND-----FIDTSStAGNKESIVQLSEKYKMTCSAMKSLGIANFKSI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 335 EQMGLlrvisGVLQLGNIVFKKERNTDQASmpdNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAI 414
Cdd:cd14898 225 EDCLL-----GILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 415 EALAKATYERMFRWLVLRINKALDKTkrqGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 494
Cdd:cd14898 297 NSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 495 EGIEWNFIDFgLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVvqeqgthpKFQKPKQLKDKADFCII--H 572
Cdd:cd14898 374 EGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKI--------KKYLNGFINTKARDKIKvsH 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 573 YAGKVDYKADEWLMKNMDplndniatllhqssdkfvselwKDVDRIIGLDQVAgmsetalpgafktRKGMFRTVGQLYKE 652
Cdd:cd14898 442 YAGDVEYDLRDFLDKNRE----------------------KGQLLIFKNLLIN-------------DEGSKEDLVKYFKD 486
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 806638593 653 QLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 726
Cdd:cd14898 487 SMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGI 560
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
95-764 |
1.52e-92 |
|
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: 315.60 E-value: 1.52e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMY---KGKKRHEMPPHIYAITDTAYRSMMQDREDQSIL 171
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 172 CTGESGAGKTENTKKVIQYLAHVASSHKSKkdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVNGYIV 250
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTT-----FDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 251 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH----VTIPGQQDKDMFQETMEAM 326
Cdd:cd14878 156 GARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMredvSTAERSLNREKLAVLKQAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 327 RIMGIPEDEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:cd14878 236 NVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 407 KEQADFAIEALAKATYERMFRWLVLRINKAL---DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 483
Cdd:cd14878 316 IQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 484 MFILEQEEYQREGIEWNFIDFGLDLQPCID-LIEKPAgppGILALLDEECWFPKATDKSFVEKV---VQEQGTHPKFQKP 559
Cdd:cd14878 396 LFLQEQTECVQEGVTMETAYSPGNQTGVLDfFFQKPS---GFLSLLDEESQMIWSVEPNLPKKLqslLESSNTNAVYSPM 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 560 KQ------LKDK-ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELwkdvdriigldqvagmsetal 632
Cdd:cd14878 473 KDgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHL--------------------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 633 pgaFKTRkgmFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRV 712
Cdd:cd14878 532 ---FQSK---LVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRL 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 806638593 713 VFQEFRQRYEILTPNSI-PKGFMDGKQACVLMIKALELDSnlYRIGQSKVFFR 764
Cdd:cd14878 606 SFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
96-750 |
8.48e-82 |
|
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: 283.54 E-value: 8.48e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYknlpiyseeivdMYKGKKRH-------EMPPHIYAITDTAYRSMMQDREDQ 168
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTltstrssPLAPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 169 SILCTGESGAGKTENTKKVIQYLAHVASshkskkdqGELE----RQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFd 244
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAG--------GGPEtdafKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 245 VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYN--KYRFLSNGHVTIPGQQDKDMFQET 322
Cdd:cd14881 141 TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAEDAARFQAW 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 323 MEAMRIMGIPedeQMGLLRVISGVLQLGNIVFKkERNTDQASMPDNTAAQKVSHLLGINVTDFTRGiLTPRIK-VGRDYV 401
Cdd:cd14881 221 KACLGILGIP---FLDVVRVLAAVLLLGNVQFI-DGGGLEVDVKGETELKSVAALLGVSGAALFRG-LTTRTHnARGQLV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 402 QKAQTKEQADFAIEALAKATYERMFRWLVLRINKaldkTKRQGAS--------FIGILDIAGFEIFDLNSFEQLCINYTN 473
Cdd:cd14881 296 KSVCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMFGFEDPKPSQLEHLCINLCA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 474 EKLQQLFNHTMFILEQEEYQREGIEWNF-IDFgLDLQPCIDLIEkpAGPPGILALLDEECwFPKATDKSFVEKVVQEQGT 552
Cdd:cd14881 372 ETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKIKVQHRQ 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 553 HPKFQKPKQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFvselwkdvdriigldqvagmsetal 632
Cdd:cd14881 448 NPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNF------------------------- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 633 pgAFKTRKGMFRTvgqlykeQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRV 712
Cdd:cd14881 502 --GFATHTQDFHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRM 572
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 806638593 713 VFQEFRQRYEILTPNSIPKGFMDGKQAC--VLMIKALELD 750
Cdd:cd14881 573 RFKAFNARYRLLAPFRLLRRVEEKALEDcaLILQFLEAQP 612
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
95-716 |
8.87e-81 |
|
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: 282.18 E-value: 8.87e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVDMYKGKKRHE-------MPPHIYAITDTAYRSMMQDRE 166
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 167 DQSILCTGESGAGKTENTKKVIQYLAHVasshKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-- 244
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI----QTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEev 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 245 -------VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSG-AGEHLKTDLLLEPYNKYRFLSN----------G 306
Cdd:cd14884 157 entqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLNPdeshqkrsvkG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 307 HVTIPG----------QQDKDMFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNIVFKkerntdqasmpdntaaqKVSH 376
Cdd:cd14884 237 TLRLGSdsldpseeekAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK-----------------AAAE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 377 LLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGA----------- 445
Cdd:cd14884 300 CLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDEsdnediysine 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 446 SFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKpagppgIL 525
Cdd:cd14884 380 AIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFIAK------IF 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 526 ALLDE-----ECWFPKATDKSFV-----EKVVQEQGTH------PKFQK---PKQLKDKADFCIIHYAGKVDYKADEWLM 586
Cdd:cd14884 453 RRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVsygfvlNHDADgtaKKQNIKKNIFFIRHYAGLVTYRINNWID 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 587 KNMDPLNDNIATLLHQSSDKFVSElwkdvdriigldqvagmsetalpGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNP 666
Cdd:cd14884 533 KNSDKIETSIETLISCSSNRFLRE-----------------------ANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDM 589
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 806638593 667 NFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQE 716
Cdd:cd14884 590 YYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
95-729 |
1.05e-69 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 247.86 E-value: 1.05e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYkgkkrhemppHIYAITDTAYRSMMQDRED-QSILCT 173
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 174 GESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERqllqanpILEAFGNAKTVKNDNSSRFGKFIRINFDVNgYIVGAN 253
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHSSAIES-------VFKSFGCAKTLKNDEATRFGCSIDLLYKRN-VLTGLN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 254 IE-TYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd14874 143 LKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 333 EDEQMGLLRVISGVLQLGNIVFKKERNTD---QASMPDNTAAQK-VSHLLGINVTDFTRgILTPRIKVGrdyvqKAQTKE 408
Cdd:cd14874 223 DDHCISIYKIISTILHIGNIYFRTKRNPNveqDVVEIGNMSEVKwVAFLLEVDFDQLVN-FLLPKSEDG-----TTIDLN 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 409 QADFAIEALAKATYERMFRWLVLRINKALDKTKRQGAsfIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILE 488
Cdd:cd14874 297 AALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHDQ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 489 QEEYQREGIEWNF-IDFGLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQlKDKAD 567
Cdd:cd14874 375 LVDYAKDGISVDYkVPNSIENGKTVELLFKK--PYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARN-KERLE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 568 FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldqvagmsetalpgAFKTRKgMFRTVG 647
Cdd:cd14874 452 FGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESY-------------------SSNTSD-MIVSQA 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 648 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 727
Cdd:cd14874 512 QFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLPG 591
|
..
gi 806638593 728 SI 729
Cdd:cd14874 592 DI 593
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
96-717 |
2.20e-68 |
|
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: 245.39 E-value: 2.20e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVDMYKgkKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 175 ESGAGKTENTKKVIQYLAHVASShKSKKdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTDLS-RSKY----LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSN-GHVTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd14905 155 YSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVFDRLKMSFVFFDFPS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 334 DEQMGLLRVISGVLQLGNIVFKKERNtdQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAqtkeqadfa 413
Cdd:cd14905 235 EKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENR--------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 414 iEALAKATYERMFRWLVLRINKALDKTkrQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQ 493
Cdd:cd14905 304 -DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 494 REGIEW-NFIDFGlDLQPCIDLIEKpagppgILALLDEECWFPKATDKSFVEKVVQEQGTHPKF-QKPKQlkdkadFCII 571
Cdd:cd14905 381 TERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgKKPNK------FGIE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 572 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFV---SELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFR---- 644
Cdd:cd14905 448 HYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLfsrDGVFNINATVAELNQMFDAKNTAKKSPLSIVKVLLScgsn 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 645 --------------------------TVGQLYKeQLAKLMATLRNTNPN--FVRCIIPNHEKKAGKLDPHLVLDQLRCNG 696
Cdd:cd14905 528 npnnvnnpnnnsgggggggnsgggsgSGGSTYT-TYSSTNKAINNSNCDfhFIRCIKPNSKKTHLTFDVKSVNEQIKSLC 606
|
650 660
....*....|....*....|....*
gi 806638593 697 VLEGIRICRQGFP----NRVVFQEF 717
Cdd:cd14905 607 LLETTRIQRFGYTihynNKIFFDRF 631
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
98-722 |
1.98e-67 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 244.11 E-value: 1.98e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 98 LHNLKERYYSGLIYTYSGLFCVVINPYKNLPIY----------SEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDRED 167
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYtpdhmqaynkSREQTPLYEKDTVNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 168 QSILCTGESGAGKTENTKKVIQYLAHVASS----HKSKKDQGELE---RQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 240
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDEteprPDSEGASGVLHpigQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 241 INFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAgEH---LKTDLLL-EPYNKYRFLSN-----GHVTIP 311
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGV-QHdptLRDSLEMnKCVNEFVMLKQadplaTNFALD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 312 GQQDKDMfqetMEAMRIMGIPEDEQMGLLRVISGVLQLGNIVF-------KKERNTDQASMPDNTA------AQ--KVSH 376
Cdd:cd14893 243 ARDYRDL----MSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggKSVGGANSTTVSDAQScalkdpAQilLAAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 377 LLGIN--VTD---FTRGILTpriKVGRDYVQ--KAQTKEQADFAIEALAKATYERMFRWLVLRINKAL----DKTKR--- 442
Cdd:cd14893 319 LLEVEpvVLDnyfRTRQFFS---KDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKsni 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 443 ----QGasfIGILDIAGFEIFD--LNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWNFIDFGLDLQ 509
Cdd:cd14893 396 vinsQG---VHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 510 PCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKAD------------FCIIHYAGKV 577
Cdd:cd14893 473 KCLQLFEDK--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 578 DYKADEWLMKNMDPLNDNIATLLHQSSDKfvselwkdVDRIIGLDQVA------GMSETALPGAF--KTRKGMFR----- 644
Cdd:cd14893 551 TYNGKGLSSKNMLSISSTCAAIMQSSKNA--------VLHAVGAAQMAaassekAAKQTEERGSTssKFRKSASSaresk 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 645 -----TVGQLYKEQLAKLMAtLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQ 719
Cdd:cd14893 623 nitdsAATDVYNQADALLHA-LNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFR 701
|
...
gi 806638593 720 RYE 722
Cdd:cd14893 702 RYK 704
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
96-764 |
3.05e-67 |
|
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: 241.18 E-value: 3.05e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 176 SGAGKTENTKKVIQYLAHVAsshksKKDQGELERqLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 255
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLG-----DGNRGATGR-VESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 256 TYLLEKSRAIRQAKEERTFHIFYYLLSG--AGEHLKtDLLLEPYNKYRFLSNGHVTIPG---------QQDKDMFQETME 324
Cdd:cd14882 156 MYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYLRIPPEVPPSklkyrrddpEGNVERYKEFEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 325 AMRIMGIPEDEQMGLLRVISGVLQLGNIVFKKerNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKA 404
Cdd:cd14882 235 ILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 405 QTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKrqgASF-----IGILDIAGFEIFDLNSFEQLCINYTNEKLQQL 479
Cdd:cd14882 313 HTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFGFECFHRNRLEQLMVNTLNEQMQYH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 480 FNHTMFI---LEQEEYQREGIEWNFIDFGLDLQpciDLIEKPAgppGILALLDEECwfPKATDKSFVEKVVQEQgtHPKF 556
Cdd:cd14882 390 YNQRIFIsemLEMEEEDIPTINLRFYDNKTAVD---QLMTKPD---GLFYIIDDAS--RSCQDQNYIMDRIKEK--HSQF 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 557 QKPKQlkdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriiglDQVAGMsetalpgaf 636
Cdd:cd14882 460 VKKHS---AHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVRNM--------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 637 KTRKGMFRTVGQlykEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQE 716
Cdd:cd14882 521 RTLAATFRATSL---ELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQE 597
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 806638593 717 FRQRYEILTPNSIPKGFMDgKQACVLMIKALELDSnlYRIGQSKVFFR 764
Cdd:cd14882 598 FLRRYQFLAFDFDETVEMT-KDNCRLLLIRLKMEG--WAIGKTKVFLK 642
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
117-248 |
5.96e-60 |
|
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: 203.73 E-value: 5.96e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 117 FCVVINPYKNLPIYSEEIVD-MYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 195
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIIvFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 806638593 196 SSHKSKKD----------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 248
Cdd:cd01363 81 FNGINKGEtegwvylteiTVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
96-762 |
1.13e-57 |
|
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: 214.31 E-value: 1.13e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVDMYK-GKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 175 ESGAGKTENTKKVIQYLAHVASSHKS------------------KKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFG 236
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKGSRRlptnlndqeednihneenTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 237 KFIRINFDvNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDK 316
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 317 DMFQETMEAMRIMGIPEDEQMGLLRVISGVLQLGNI-----VFKKE---------------------RNTDQASMPDNTA 370
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkaFRKKSllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 371 AQKV-SHLLGINVTDFTRGILTPRIkVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKR--QGASF 447
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 448 IGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgpPGILAL 527
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPT--EGSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 528 LDEECWFPKATDKS-FVEKVVQEQGTHPKFQKPKQLK-DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSD 605
Cdd:cd14938 478 LLENVSTKTIFDKSnLHSSIIRKFSRNSKYIKKDDITgNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 606 KFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQ----LYKEQLAKLMATLRNTNPNFVRCIIPNHEKKA- 680
Cdd:cd14938 558 EYMRQFCMFYNYDNSGNIVEEKRRYSIQSALKLFKRRYDTKNQmavsLLRNNLTELEKLQETTFCHFIVCMKPNESKREl 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 681 GKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPnsipkgfmDGKQACVLMIKALELDSNLYRIGQSK 760
Cdd:cd14938 638 CSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISNYEWMIGNNM 709
|
..
gi 806638593 761 VF 762
Cdd:cd14938 710 IF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1035-1863 |
6.26e-34 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 143.27 E-value: 6.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1035 RLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQIS 1114
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1115 ELQEDLESERACRNKAEKQKRDLGEELEALKTELEdtldSTAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKH 1194
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLE----ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1195 SQAVEELAEQLEQTKRVKATLEKAKQTLENERGELanevkallqgkgdSEHKRKKVEAQLQELQVKFSEGERVRTELADK 1274
Cdd:TIGR02168 389 AQLELQIASLNNEIERLEARLERLEDRRERLQQEI-------------EELLKKLEEAELKELQAELEELEEELEELQEE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1275 VSKLQVELDSVTGLLNQSDSKSSKLTKDFSALESQ---LQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEA 1351
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARldsLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGY 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1352 KRNLEKQI-ATLHAQVTDMKKKMEDGVGCLETAEEAKRRLqkdleglsqrLEEKVAAYDKLEKTKTRLQQELDDLlvdld 1430
Cdd:TIGR02168 536 EAAIEAALgGRLQAVVVENLNAAKKAIAFLKQNELGRVTF----------LPLDSIKGTEIQGNDREILKNIEGF----- 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1431 hqRQSVSNLEKKQKKFDQLLAeekTISAKYAEERDRAEAEAREKETKALSLARALEE-------AMEQKAELERLNKQFR 1503
Cdd:TIGR02168 601 --LGVAKDLVKFDPKLRKALS---YLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGdlvrpggVITGGSAKTNSSILER 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1504 -TEMEDLmsskddvGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERdLQGRDEQSEE 1582
Cdd:TIGR02168 676 rREIEEL-------EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEE 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1583 KKKQLVRQVREMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASRE 1662
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1663 EILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIanssgkgALALEEKRRLEARIAQLEEELEEEQ 1742
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-------EALLNERASLEEALALLRSELEELS 900
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1743 GNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSKYKASIAALEAKIAQLEEQ 1822
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 806638593 1823 LDN-------------ETKERQ----AASKQVRRAEKKLKDVLLQVEDERRnaEQFKD 1863
Cdd:TIGR02168 981 IKElgpvnlaaieeyeELKERYdfltAQKEDLTEAKETLEEAIEEIDREAR--ERFKD 1036
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
933-1830 |
2.56e-32 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 137.88 E-value: 2.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 933 YLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKvtteaKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEE 1012
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELALLVLRLEELRE-----ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1013 EKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEgdstdlsDQIAELQAQIAELKMQLAKKEEELQAALARV 1092
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE-------AQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1093 EEEAAQKNMALKKIRELETQISELQEDLESERACRNKAEKQKRDLGEELEALKTELEdtlDSTAAQQELRSKREQEVSIL 1172
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE---RLEDRRERLQQEIEELLKKL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1173 KKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQTLENERGELANEVKALlqgkgdsehkrkkveA 1252
Cdd:TIGR02168 431 EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL---------------E 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1253 QLQELQVKFSEGERvrteladKVSKLQVELDSVTGLLNQSDSKSSKLTKdfsALESQLQDT-QELLQEENRQKLSLSTKL 1331
Cdd:TIGR02168 496 RLQENLEGFSEGVK-------ALLKNQSGLSGILGVLSELISVDEGYEA---AIEAALGGRlQAVVVENLNAAKKAIAFL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1332 KQMEDEKNSFREQLEEEEEAKRNLEkqiatlhaqvTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRL---EEKVAAY 1408
Cdd:TIGR02168 566 KQNELGRVTFLPLDSIKGTEIQGND----------REILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvDDLDNAL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1409 DKLEKTKTR----------------LQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAR 1472
Cdd:TIGR02168 636 ELAKKLRPGyrivtldgdlvrpggvITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1473 EKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATE 1552
Cdd:TIGR02168 716 QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1553 DAKLRLEVNLQAMKAQFeRDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQrsiamaaRKKLEMDLKDLEAHIDTANKN 1632
Cdd:TIGR02168 796 EELKALREALDELRAEL-TLLNEEAANLRERLESLERRIAATERRLEDLEEQ-------IEELSEDIESLAAEIEELEEL 867
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1633 REEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIAN 1712
Cdd:TIGR02168 868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE 947
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1713 ssgKGALALEEKRRLEARIAqleeeleeeqGNTELINDRLKKANLQIDQINTdlnlershaqKNENARQQLERQNKELKA 1792
Cdd:TIGR02168 948 ---EYSLTLEEAEALENKIE----------DDEEEARRRLKRLENKIKELGP----------VNLAAIEEYEELKERYDF 1004
|
890 900 910
....*....|....*....|....*....|....*...
gi 806638593 1793 KLQEMESAVKSKYKasiaaLEAKIaqleEQLDNETKER 1830
Cdd:TIGR02168 1005 LTAQKEDLTEAKET-----LEEAI----EEIDREARER 1033
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1035-1879 |
3.19e-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: 134.41 E-value: 3.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1035 RLRREEKQRQeLEKTRRKLEgdstDLSDQIAELQAQIAELKMQlAKKEEELQAAlaRVEEEAAQKNMALKKIRELETQIS 1114
Cdd:TIGR02168 171 KERRKETERK-LERTRENLD----RLEDILNELERQLKSLERQ-AEKAERYKEL--KAELRELELALLVLRLEELREELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1115 ELQEDLESERACRNKAEKQKRDLGEELEALKTEL-EDTLDSTAAQQELrskreQEVSILKKTLEDEAKTHEAQIQEMRQK 1193
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVsELEEEIEELQKEL-----YALANEISRLEQQKQILRERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1194 hsqaVEELAEQLEQTKRVKATLEKAKQTLENERGELANEVKALLQgkgdsehKRKKVEAQLQELQVKFSEGERVRTELAD 1273
Cdd:TIGR02168 318 ----LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA-------ELEELEAELEELESRLEELEEQLETLRS 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1274 KVSKLQVELDSvtgllnqsdsksskLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKqmedeknsfreqleeeEEAKR 1353
Cdd:TIGR02168 387 KVAQLELQIAS--------------LNNEIERLEARLERLEDRRERLQQEIEELLKKLE----------------EAELK 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1354 NLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELddllvdldhqr 1433
Cdd:TIGR02168 437 ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFS----------- 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1434 QSVSNLEKKQKKF--------DQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKA---ELERLNKQF 1502
Cdd:TIGR02168 506 EGVKALLKNQSGLsgilgvlsELISVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVtflPLDSIKGTE 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1503 --RTEMEDLMSSKDDVGkSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAK-LRLEVNLQAMK------------- 1566
Cdd:TIGR02168 586 iqGNDREILKNIEGFLG-VAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKkLRPGYRIVTLDgdlvrpggvitgg 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1567 -AQFERDLQGRD---EQSEEKKKQLVRQVREMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRK 1642
Cdd:TIGR02168 665 sAKTNSSILERRreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1643 LQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALE 1722
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1723 EKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMEsavk 1802
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS---- 900
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1803 skykASIAALEAKIAQLEEQLDNETKERQAASKQVRRAEKKLKDVLLQV-EDERRNAEQFK-------DQADKASTRLKQ 1874
Cdd:TIGR02168 901 ----EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEalenkieDDEEEARRRLKR 976
|
....*
gi 806638593 1875 LKRQL 1879
Cdd:TIGR02168 977 LENKI 981
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
821-1631 |
5.45e-31 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 133.64 E-value: 5.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 821 RLRNWQWWRLFTKVKpllnsiRHEDELLAKEAELTKVREKHLAAENRLTEMETMQSQLMAEKLQLQEqlqaetelcaEAE 900
Cdd:TIGR02168 221 ELRELELALLVLRLE------ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE----------EIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 901 ELRARLTAKKQELEeichDLEARVeeeeercQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQ 980
Cdd:TIGR02168 285 ELQKELYALANEIS----RLEQQK-------QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 981 IIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDL 1060
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1061 sdQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERACRNKAEKQKRDLGEE 1140
Cdd:TIGR02168 434 --ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1141 LEAlKTELEDTLDSTAAQQELRSKREQEVSI-----LKKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATL 1215
Cdd:TIGR02168 512 LKN-QSGLSGILGVLSELISVDEGYEAAIEAalggrLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGND 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1216 EKAKQTLENERGELANEVKALLQGKGDSEHKRKKV-----EAQLQELQVKFSEGERVRTELADKVSK------------- 1277
Cdd:TIGR02168 591 REILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvddLDNALELAKKLRPGYRIVTLDGDLVRPggvitggsaktns 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1278 ----LQVELDSVTGLLNQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKR 1353
Cdd:TIGR02168 671 sileRRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1354 NLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDldhQR 1433
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER---LE 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1434 QSVSNLEKKQKKFDQLLAEEKTISakyaEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSK 1513
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELS----EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1514 DDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDaKLRLEVNLQAMKA-QFERDLQGRDEQSEEKKKQLVRQVR 1592
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE-RLSEEYSLTLEEAeALENKIEDDEEEARRRLKRLENKIK 982
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 806638593 1593 EM-------EAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANK 1631
Cdd:TIGR02168 983 ELgpvnlaaIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
991-1710 |
6.53e-30 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 130.19 E-value: 6.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 991 AKEKKLLEDR---VAEFttnlmeEEEKSKSLAKLK------NKHEAMITDLEERLRREEKQRQELEK----TRRKLEGDS 1057
Cdd:TIGR02169 152 PVERRKIIDEiagVAEF------DRKKEKALEELEeveeniERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1058 TDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQED-----------LESERAC 1126
Cdd:TIGR02169 226 YELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeqlrvkekigeLEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1127 RNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKhsqaVEELAEQLE 1206
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE----LEEVDKEFA 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1207 QTKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVSKLQVELdsvt 1286
Cdd:TIGR02169 382 ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL---- 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1287 gllnqsdsksSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQV 1366
Cdd:TIGR02169 458 ----------EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTV 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1367 TDMKKKMEDGVGCLETAeeAKRRLQK---DLEGLSQRL-----EEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVsN 1438
Cdd:TIGR02169 528 AQLGSVGERYATAIEVA--AGNRLNNvvvEDDAVAKEAiellkRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAV-D 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1439 LEKKQKKF---------DQLLAE----------------------------------EKTISAKYAEERDRAEAEAREKE 1475
Cdd:TIGR02169 605 LVEFDPKYepafkyvfgDTLVVEdieaarrlmgkyrmvtlegelfeksgamtggsraPRGGILFSRSEPAELQRLRERLE 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1476 tkalSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAK 1555
Cdd:TIGR02169 685 ----GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1556 LRLEVNLQAMKAQFErdlQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREE 1635
Cdd:TIGR02169 761 KELEARIEELEEDLH---KLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 806638593 1636 AIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEI 1710
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI 912
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
970-1554 |
1.56e-27 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 121.97 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 970 EAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKT 1049
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1050 RRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERACRNK 1129
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1130 AEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEvsilkktlEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTK 1209
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE--------EEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1210 RVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEA--QLQELQVKFSEGERVRTELADKVSKLQVELDSVTG 1287
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAalLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1288 LLNQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVT 1367
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1368 DmkkKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRqsvsnlEKKQKKFD 1447
Cdd:COG1196 630 A---RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE------LELEEALL 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1448 QLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLmsskDDVGKSVHELEKSK 1527
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL----EELERELERLEREI 776
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 806638593 1528 RAL--------------EQQVEEMKTQLEELEDELQATEDA 1554
Cdd:COG1196 777 EALgpvnllaieeyeelEERYDFLSEQREDLEEARETLEEA 817
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1011-1733 |
4.41e-27 |
|
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: 120.94 E-value: 4.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1011 EEEKSKSLAKLKNKHEAMI--TDLEERLRREE-----KQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEE 1083
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAEryQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1084 ELQAALARVEEEAAQKNMALK-KIRELETQISELQEDLESERACRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELR 1162
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEQLRVKeKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1163 SKREQEVSILKKTLED---EAKTHEAQIQEMRQKHSQAVEEL---AEQLEQTKRVKATLEKAKQTLENERGELANEVKAL 1236
Cdd:TIGR02169 353 DKLTEEYAELKEELEDlraELEEVDKEFAETRDELKDYREKLeklKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1237 LQGKgdsehkrKKVEAQLQELQVKFSEGERVRTELADKVSKLQVELDSVTGLLNQSDSKSSKLTKDFSALESQLQ----- 1311
Cdd:TIGR02169 433 EAKI-------NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARaseer 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1312 -----DTQELLQEEN------------------------------------------------RQKLSLST-----KLKQ 1333
Cdd:TIGR02169 506 vrggrAVEEVLKASIqgvhgtvaqlgsvgeryataievaagnrlnnvvveddavakeaiellkRRKAGRATflplnKMRD 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1334 MEDEKNSFREQ-----------------------------LEEEEEAKRNLEK-QIATLHAQVTDMKKKMEDGVGCLETA 1383
Cdd:TIGR02169 586 ERRDLSILSEDgvigfavdlvefdpkyepafkyvfgdtlvVEDIEAARRLMGKyRMVTLEGELFEKSGAMTGGSRAPRGG 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1384 EEAKRRLQKDLEGLSQRLEEkvaaydkLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKK----QKKFDQLLAEEKTISAK 1459
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKigeiEKEIEQLEQEEEKLKER 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1460 YAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQF--------RTEMEDLMSSKDDVGKSVHELEKSKRALE 1531
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALndlearlsHSRIPEIQAELSKLEEEVSRIEARLREIE 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1532 QQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFErDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSIAMAA 1611
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE-NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1612 RKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKdcmrELDDTRASREEIlaqaKENEKKLKSMEAEMIQLQEELAA 1691
Cdd:TIGR02169 898 LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS----EIEDPKGEDEEI----PEEELSLEDVQAELQRVEEEIRA 969
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 806638593 1692 AERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQ 1733
Cdd:TIGR02169 970 LEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
867-1699 |
8.83e-27 |
|
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: 119.79 E-value: 8.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 867 RLTEMETMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQY----LQAEKKKMQ 942
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEkigeLEAEIASLE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 943 QNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQiimEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLK 1022
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREI---EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1023 NKHEamitDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALArveeeaaqknma 1102
Cdd:TIGR02169 385 DELK----DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL------------ 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1103 lkKIRELETQISELQEDLESERACRNKAEKQKRDLGEELEALKTELeDTLDSTAAQQELRSKREQEVSILKKTLEDEAKT 1182
Cdd:TIGR02169 449 --EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL-AEAEAQARASEERVRGGRAVEEVLKASIQGVHG 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1183 HEAQIQEMRQKHSQAVEELAEQLEQTKRVK--ATLEKAKQTLENERGELA-----NEVKA------LLQGKGDSEHKRKK 1249
Cdd:TIGR02169 526 TVAQLGSVGERYATAIEVAAGNRLNNVVVEddAVAKEAIELLKRRKAGRAtflplNKMRDerrdlsILSEDGVIGFAVDL 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1250 VEAQLQ-ELQVKFSEGERVRTELADKVSKLQVELDSVTgLLNQSDSKSSKLTKDFSALESQLQDTQELLQEEnrqkLSLS 1328
Cdd:TIGR02169 606 VEFDPKyEPAFKYVFGDTLVVEDIEAARRLMGKYRMVT-LEGELFEKSGAMTGGSRAPRGGILFSRSEPAEL----QRLR 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1329 TKLKQMEDEKNSFREQLeeeeeakRNLEKQIATLHAQVTDMKKKmedgvgcLETAEEAKRRLQKDLEGLSQRLEEKVAAY 1408
Cdd:TIGR02169 681 ERLEGLKRELSSLQSEL-------RRIENRLDELSQELSDASRK-------IGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1409 DKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTisAKYAEERDRAEAEAREKETKALSLARALEEA 1488
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI--PEIQAELSKLEEEVSRIEARLREIEQKLNRL 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1489 MEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQatedaklrlevnlqamkaq 1568
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG------------------- 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1569 ferDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIdTANKNREEAIKQLRKLQAQMK 1648
Cdd:TIGR02169 886 ---DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK-GEDEEIPEEELSLEDVQAELQ 961
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 806638593 1649 DCMRELDD-----TRASR--EEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQA 1699
Cdd:TIGR02169 962 RVEEEIRAlepvnMLAIQeyEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1202-1923 |
1.05e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 119.78 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1202 AEQLEQTKRVKATLEKAKQTLE-NERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVSKLQV 1280
Cdd:TIGR02168 209 AEKAERYKELKAELRELELALLvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1281 ELDSVTGLLNQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEeeeeakrNLEKQIA 1360
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE-------SLEAELE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1361 TLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEkvaaydkLEKTKTRLQQELDDLLVDLDHQRQSVSNLE 1440
Cdd:TIGR02168 362 ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER-------LEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1441 KKqkKFDQLLAEEKTISAKYAEERDRAEAEareKETKALSLARALEEAMEQKAELERLNKQFRTeMEDLMSSKDDVGKSV 1520
Cdd:TIGR02168 435 LK--ELQAELEELEEELEELQEELERLEEA---LEELREELEEAEQALDAAERELAQLQARLDS-LERLQENLEGFSEGV 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1521 HELEKSKRALEQQVEEMKTQLE-----ELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRD------EQSEEKKKQLVR 1589
Cdd:TIGR02168 509 KALLKNQSGLSGILGVLSELISvdegyEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELgrvtflPLDSIKGTEIQG 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1590 QVREMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANkNREEAIKQLRKLQAQMKdcMRELDDTRASREEILAQA- 1668
Cdd:TIGR02168 589 NDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVD-DLDNALELAKKLRPGYR--IVTLDGDLVRPGGVITGGs 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1669 --------------KENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQL 1734
Cdd:TIGR02168 666 aktnssilerrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1735 EEELeeeqgntELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSKyKASIAALEA 1814
Cdd:TIGR02168 746 EERI-------AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL-RAELTLLNE 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1815 KIAQLEEQLDNETKERQAASKQVRRAEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRR 1894
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
730 740
....*....|....*....|....*....
gi 806638593 1895 KLQRELedatetadamnREVSSLKNKLRR 1923
Cdd:TIGR02168 898 ELSEEL-----------RELESKRSELRR 915
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1082-1910 |
1.09e-26 |
|
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: 119.40 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1082 EEELQAALARVEEeaaqknmALKKIRELETQISELQEDLESERACRNKAEKQKrdlgeeleALKTELEDTlDSTAAQQEL 1161
Cdd:TIGR02169 169 DRKKEKALEELEE-------VEENIERLDLIIDEKRQQLERLRREREKAERYQ--------ALLKEKREY-EGYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1162 RSKREQEVSILKKTleDEAKTHEAQIQEMRQKHSQAVEELAEQLEQ-TKRVKATLEKAKQTLENERGELANEVKALLQGK 1240
Cdd:TIGR02169 233 EALERQKEAIERQL--ASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1241 GDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVSKLQVELDSVTgllnqsdSKSSKLTKDFSALESQLQDTQELLQEE 1320
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT-------EEYAELKEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1321 NRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKK-------MEDGVGCLETAEEAKRRLQKD 1393
Cdd:TIGR02169 384 RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKineleeeKEDKALEIKKQEWKLEQLAAD 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1394 LEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQ-------LLAEEKTISAKYAEERD- 1465
Cdd:TIGR02169 464 LSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLGSVGERYATAIEv 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1466 ----RAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKD---DVGKSVHELEKSKRALEQQV---- 1534
Cdd:TIGR02169 544 aagnRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDgviGFAVDLVEFDPKYEPAFKYVfgdt 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1535 ---EEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSIAMAA 1611
Cdd:TIGR02169 624 lvvEDIEAARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENR 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1612 RKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAA 1691
Cdd:TIGR02169 704 LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALND 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1692 AERAKRQAQ-QERDELADEIAnssgkgalalEEKRRLEARIAQLEEELEEEQGNTELINDrlKKANLQIDQINTDlnler 1770
Cdd:TIGR02169 784 LEARLSHSRiPEIQAELSKLE----------EEVSRIEARLREIEQKLNRLTLEKEYLEK--EIQELQEQRIDLK----- 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1771 shAQKNENARQQlerqnKELKAKLQEMESAVKSKykasiaalEAKIAQLEEQLDNETKERQAASKQVRRAEKKLKDVLLQ 1850
Cdd:TIGR02169 847 --EQIKSIEKEI-----ENLNGKKEELEEELEEL--------EAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1851 VEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQrANASRRKLQRELEDATETADAM 1910
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE-EELSLEDVQAELQRVEEEIRAL 970
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1302-1925 |
1.16e-25 |
|
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: 116.04 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1302 DFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQ-------VTDMKKKME 1374
Cdd:pfam01576 6 EMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARkqeleeiLHELESRLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1375 DGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEek 1454
Cdd:pfam01576 86 EEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1455 tISAKYAEErdraeaearEKETKALSLARALEEAMEQKAElERLNKQfrtemedlmsskddvGKSVHELEKSKRALEQQV 1534
Cdd:pfam01576 164 -FTSNLAEE---------EEKAKSLSKLKNKHEAMISDLE-ERLKKE---------------EKGRQELEKAKRKLEGES 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1535 EEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFErDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSIAMAARKK 1614
Cdd:pfam01576 218 TDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE-EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1615 LEMDLK----DLEAHIDTANKNREEAIKQLRKLqAQMKDCMREldDTRASREEILAQAKENEKKLKSMEAEMIQLQEELA 1690
Cdd:pfam01576 297 LGEELEalktELEDTLDTTAAQQELRSKREQEV-TELKKALEE--ETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1691 AAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLER 1770
Cdd:pfam01576 374 NLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAE 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1771 SHAQKNENARQQLERQNKELKAKLQEmESAVKSKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRAEKKLKDVLLQ 1850
Cdd:pfam01576 454 GKNIKLSKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKK 532
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 806638593 1851 VEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKLRRGD 1925
Cdd:pfam01576 533 LEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFD 607
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
101-705 |
2.95e-25 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 114.45 E-value: 2.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 101 LKERYYSGLIYTYSGLFCV-VINPYKNL------PIYSEEIVDMYKGKKRHE--MPPHIYAI------------------ 153
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIakqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 154 --TDTAYRSMMQDReDQSILCTGESGAGKTENTKKVIQYLAHVA---------------------------SSHKS---- 200
Cdd:cd14894 87 psTISSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAqpalskgseetckvsgstrqpkiklftSSTKStiqm 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 201 ---------------------------------------------------------KKDQGELERQL------------ 211
Cdd:cd14894 166 rteeartialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyeKLEHLEDEEQLrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 212 ----LQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDVNGY---IVGANIETYLLEKSRAIRQA------KEERTFHI 276
Cdd:cd14894 246 lsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 277 FYYLLSGAGEH-----LKTDLLLEPYN--KYRFLSNGHVTIPG--------QQDKDMFQETMEAMRIMGIPEDEQMGLLR 341
Cdd:cd14894 326 LYAMVAGVNAFpfmrlLAKELHLDGIDcsALTYLGRSDHKLAGfvskedtwKKDVERWQQVIDGLDELNVSPDEQKTIFK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 342 VISGVLQLGNIVFKKERNTDQASMPDN---TAAQKVSHLLGI-NVTDFTRGILTPRIKV--GRDYVQKAQTKEQADFAIE 415
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELgSVEKLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 416 ALAKATYERMFRWLVLRINKAL-------DKTKRQ---------GASFIGILDIAGFEIFDLNSFEQLCINYTNEKLqql 479
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL--- 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 480 fnhtmfileqeeYQREGiewNFIDFGLDLQPCI-------DLIEKPAGPPGILALLDEECWFPKAT----------DKSF 542
Cdd:cd14894 563 ------------YAREE---QVIAVAYSSRPHLtardsekDVLFIYEHPLGVFASLEELTILHQSEnmnaqqeekrNKLF 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 543 VEKVVQEQGThpKFQKPKQLKDKAD-----------FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSEL 611
Cdd:cd14894 628 VRNIYDRNSS--RLPEPPRVLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRM 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 612 WKDVDRiIGLD-----QVAGMSETALPGAfKTRKGMFRTVGQLYKEQLAKLMatlrntnPNFVRCIIPNHEKKAGKLDPH 686
Cdd:cd14894 706 LNESSQ-LGWSpntnrSMLGSAESRLSGT-KSFVGQFRSHVNVLTSQDDKNM-------PFYFHCIRPNAKKQPSLVNND 776
|
810
....*....|....*....
gi 806638593 687 LVLDQLRCNGVLEGIRICR 705
Cdd:cd14894 777 LVEQQCRSQRLIRQMEICR 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1351-1923 |
3.95e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 114.26 E-value: 3.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1351 AKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLD 1430
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1431 HQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLM 1510
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1511 SSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQgrDEQSEEKKKQLVRQ 1590
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE--EEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1591 VREMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAqmkdCMRELDDTRASREEILAQAKE 1670
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA----VAVLIGVEAAYEAALEAALAA 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1671 NEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELIND 1750
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1751 RLkkanlqidqintdlnlershAQKNENARQQLERQNKELKAKLQEMESAVKSKYKASIAALEAKIAQLEEQldnetKER 1830
Cdd:COG1196 627 LV--------------------AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE-----AEL 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1831 QAASKQVRRAEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATET---- 1906
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPeppd 761
|
570
....*....|....*..
gi 806638593 1907 ADAMNREVSSLKNKLRR 1923
Cdd:COG1196 762 LEELERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1198-1839 |
1.48e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 112.34 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1198 VEELAEQLEQTKRVKAtLEKAKQTLENErgELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVSK 1277
Cdd:COG1196 202 LEPLERQAEKAERYRE-LKEELKELEAE--LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1278 LQVELDSVTGLLNQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEK 1357
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1358 QIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVS 1437
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1438 NLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELErlnkqfrtEMEDLMSSKDDVG 1517
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL--------EAEADYEGFLEGV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1518 KSVHELEKSKRaLEQQVEEMKTQLEELEDELQATEDAKLRLEVNlqamkaqfERDLQGRDEQSEEKKKQLVRQVREMEAE 1597
Cdd:COG1196 511 KAALLLAGLRG-LAGAVAVLIGVEAAYEAALEAALAAALQNIVV--------EDDEVAAAAIEYLKAAKAGRATFLPLDK 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1598 LEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKS 1677
Cdd:COG1196 582 IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1678 MEAEmiQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANL 1757
Cdd:COG1196 662 LTGG--SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1758 QIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMES----------AVKSKY----------KASIAALEAKIa 1817
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPvnllaieeyeELEERYdflseqredlEEARETLEEAI- 818
|
650 660
....*....|....*....|...
gi 806638593 1818 qleEQLDNETKER-QAASKQVRR 1839
Cdd:COG1196 819 ---EEIDRETRERfLETFDAVNE 838
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1037-1608 |
3.66e-22 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 104.35 E-value: 3.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1037 RREEKQRQELEKTRRKLEG-DSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAqknmALKKIRELETQISE 1115
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADE----VLEEHEERREELET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1116 LQEDLESERACRNKAEKQKRDLGEELEALK---TELEDTLDSTAAQQELRSKREQEVSILKKTLEDEakthEAQIQEMRQ 1192
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRerlEELEEERDDLLAEAGLDDADAEAVEARREELEDR----DEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1193 KHSQAVEELAEQLEQTKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELA 1272
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1273 DKVSKLQVELDSVTGLLNQsdsksskLTKDFSALESQLQDTQELLQE----ENRQKLSLSTKLKQMEDEknsfREQLEEe 1348
Cdd:PRK02224 412 DFLEELREERDELREREAE-------LEATLRTARERVEEAEALLEAgkcpECGQPVEGSPHVETIEED----RERVEE- 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1349 eeakrnLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKdLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVD 1428
Cdd:PRK02224 480 ------LEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEER-REDLEELIAERRETIEEKRERAEELRERAAELEAE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1429 LDHQRQSVsnlEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKAL--SLARALEEAMEQKAELERLNKQFRTEM 1506
Cdd:PRK02224 553 AEEKREAA---AEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAiaDAEDEIERLREKREALAELNDERRERL 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1507 EDLMSSKDDVGKSVHEleKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFER--DLQGRDEQSEEKK 1584
Cdd:PRK02224 630 AEKRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEEleELRERREALENRV 707
|
570 580 590
....*....|....*....|....*....|
gi 806638593 1585 KQL------VRQVREMEAELEDERKQRSIA 1608
Cdd:PRK02224 708 EALealydeAEELESMYGDLRAELRQRNVE 737
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
865-1717 |
2.43e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 102.53 E-value: 2.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 865 ENRLTEMeTMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQEL---EEICHDLEARVEEEEERCQYLQAEKKKM 941
Cdd:PTZ00121 1086 DNRADEA-TEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEArkaEDARKAEEARKAEDAKRVEIARKAEDAR 1164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 942 QQNIQELEEQLEEEESARQKLQLEKVTteaKLKKLEEDQIIMEDQncKLAKEKKLLEDRVAEfttnlmeEEEKSKSLAKL 1021
Cdd:PTZ00121 1165 KAEEARKAEDAKKAEAARKAEEVRKAE---ELRKAEDARKAEAAR--KAEEERKAEEARKAE-------DAKKAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1022 KnkheamitdlEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIaelKMQLAKKEEELQAALARVEEEAAQKNM 1101
Cdd:PTZ00121 1233 E----------EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAI---KAEEARKADELKKAEEKKKADEAKKAE 1299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1102 ALKKIRELETQISELQEDLESERACRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLEDEAK 1181
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK 1379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1182 THEAQIQEMRQKHSqavEELAEQLEQTKRVKATLEKAKQTLE--NERGELANEVKALLQGKGDSEHKRKKVEAQLQELQV 1259
Cdd:PTZ00121 1380 ADAAKKKAEEKKKA---DEAKKKAEEDKKKADELKKAAAAKKkaDEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1260 KFSEGERVRTELADKVSKL--QVELDSVTGLLNQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKlslSTKLKQMEDE 1337
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAkkKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK---ADEAKKAEEA 1533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1338 KNSFR----EQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEE----KVAAYD 1409
Cdd:PTZ00121 1534 KKADEakkaEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEekkmKAEEAK 1613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1410 KLEKTKTRlQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETkalslARALEEAM 1489
Cdd:PTZ00121 1614 KAEEAKIK-AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE-----AKKAEEDE 1687
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1490 EQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEEledELQATEDAKlrlevnlqamKAQF 1569
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE---DKKKAEEAK----------KDEE 1754
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1570 ERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSIAMAARKKLEmDLKDLEAHIDTANK--------NREEAIKQLR 1641
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK-DIFDNFANIIEGGKegnlvindSKEMEDSAIK 1833
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 806638593 1642 KLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKG 1717
Cdd:PTZ00121 1834 EVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAG 1909
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1010-1871 |
4.61e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 101.37 E-value: 4.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1010 EEEEKSKSLAKLKNKHEamiTDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEEL-QAA 1088
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTE---TGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDArKAE 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1089 LARVEEEAAQKNMALKKIreletQISELQEDLESERACRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQe 1168
Cdd:PTZ00121 1168 EARKAEDAKKAEAARKAE-----EVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEE- 1241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1169 vsilKKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQtKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRK 1248
Cdd:PTZ00121 1242 ----AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE-ARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKK 1316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1249 KVEAQLQELQVKfSEGERVRTELADKVSKLQVELDSVTGLLNQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLS 1328
Cdd:PTZ00121 1317 ADEAKKKAEEAK-KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE 1395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1329 TKLKQMEDEKNSfrEQLEEEEEAKRNLE--KQIATLHAQVTDMKKKMEDGvgclETAEEAKRRLQ--KDLEGLSQRLEEK 1404
Cdd:PTZ00121 1396 AKKKAEEDKKKA--DELKKAAAAKKKADeaKKKAEEKKKADEAKKKAEEA----KKADEAKKKAEeaKKAEEAKKKAEEA 1469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1405 VAAYDKLEKTK-TRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLL-AEE--KTISAKYAEERDRAEAEAREKETKALS 1480
Cdd:PTZ00121 1470 KKADEAKKKAEeAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKkAEEakKADEAKKAEEAKKADEAKKAEEKKKAD 1549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1481 LARALEEAmeQKAELERLNKQFRTEMEDlmssKDDVGKSVHELEKSKRALEQQVEEMKTQLEELE-DELQATEDAKLRLE 1559
Cdd:PTZ00121 1550 ELKKAEEL--KKAEEKKKAEEAKKAEED----KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKaEEAKKAEEAKIKAE 1623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1560 vnlQAMKAQFER-DLQGRDEQSEEKKKQ-----------LVRQVREMEAELEDERKqrsiAMAARKKLEMDLKDLEAHID 1627
Cdd:PTZ00121 1624 ---ELKKAEEEKkKVEQLKKKEAEEKKKaeelkkaeeenKIKAAEEAKKAEEDKKK----AEEAKKAEEDEKKAAEALKK 1696
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1628 TANKNREeaIKQLRKLQAQMKdcmRELDDTRASREEILAQAKENEKKlksmEAEMIQLQEELAAAERAKRQAQQERDELA 1707
Cdd:PTZ00121 1697 EAEEAKK--AEELKKKEAEEK---KKAEELKKAEEENKIKAEEAKKE----AEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1708 DEIANSSGKGALALEE--KRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLE------RSHAQKNENA 1779
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEelDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAikevadSKNMQLEEAD 1847
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1780 RQQLERQNKELKAKLQEMESAVKSKYKASIAALEAKI--AQLEEQLDNETKERQAASKQVRRAEKKLKDVLLQVED-ERR 1856
Cdd:PTZ00121 1848 AFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIeeADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEyIKR 1927
|
890
....*....|....*
gi 806638593 1857 NAEQFKDQADKASTR 1871
Cdd:PTZ00121 1928 DAEETREEIIKISKK 1942
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
838-1420 |
1.42e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 99.24 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 838 LNSIRHEDELLAKEAELTKVREKHLAAENRLTE--METMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEE 915
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEaeLEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 916 ichdLEARVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKK 995
Cdd:COG1196 314 ----LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 996 LLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELK 1075
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1076 MQLAKKEEELQAALARVEEEAAQKNMALKKIRELE---------TQISELQEDLESERACRNKAEKQKRDLGEELEALKT 1146
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEgflegvkaaLLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1147 EL--EDTLDSTAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQTLEN 1224
Cdd:COG1196 550 NIvvEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1225 ERGELANEVKALLqgkgdsEHKRKKVEAQLQELQVKFSEGERVRTELADKVSKLQVELDSVTGLLNQsdsKSSKLTKDFS 1304
Cdd:COG1196 630 ARLEAALRRAVTL------AGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE---EELELEEALL 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1305 ALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMedgvgcletaE 1384
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELEREL----------E 770
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 806638593 1385 EAKRRLQK----------DLEGLSQRLEEKVAAYDKLEKTKTRLQQ 1420
Cdd:COG1196 771 RLEREIEAlgpvnllaieEYEELEERYDFLSEQREDLEEARETLEE 816
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1591-1909 |
6.20e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 97.31 E-value: 6.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1591 VREMEAELEDERKQRSIAMAARKkLEMDLKDLEAhidtanknrEEAIKQLRKLQAQmkdcmreLDDTRASREEILAQAKE 1670
Cdd:COG1196 195 LGELERQLEPLERQAEKAERYRE-LKEELKELEA---------ELLLLKLRELEAE-------LEELEAELEELEAELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1671 NEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELIND 1750
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1751 RLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSKyKASIAALEAKIAQLEEQLDNETKER 1830
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA-LRAAAELAAQLEELEEAEEALLERL 416
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 806638593 1831 QAASKQVRRAEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADA 1909
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
846-1591 |
1.39e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 96.29 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 846 ELLAKEAELTKVREKHLAAENRLTEMETMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVE 925
Cdd:TIGR02169 295 KIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 926 EEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFT 1005
Cdd:TIGR02169 375 EVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1006 TNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIA---ELKMQLAKKE 1082
Cdd:TIGR02169 455 WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhGTVAQLGSVG 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1083 EELQAALarveeEAAQKNMALKKIRELETQISELQEDLESERACR------NKAEKQKRDLGEELE-------------- 1142
Cdd:TIGR02169 535 ERYATAI-----EVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRatflplNKMRDERRDLSILSEdgvigfavdlvefd 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1143 -----ALKTELEDTLdstaAQQELRSKREQEVSILKKTLEDEAKTHEAQI----QEMRQKHSQAVEELAEQLEQTKRVKA 1213
Cdd:TIGR02169 610 pkyepAFKYVFGDTL----VVEDIEAARRLMGKYRMVTLEGELFEKSGAMtggsRAPRGGILFSRSEPAELQRLRERLEG 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1214 tLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVSKLQVELDSVTGLLNQSD 1293
Cdd:TIGR02169 686 -LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1294 SKSSKLTKDFSALESQLQDTQELLQEEnrqklslstKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQvtdmkkkm 1373
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLEARLSHS---------RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE-------- 827
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1374 edgvgcLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEE 1453
Cdd:TIGR02169 828 ------KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1454 KtisakyaEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSkDDVGKSVHELEKSKRALE-- 1531
Cdd:TIGR02169 902 E-------RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL-EDVQAELQRVEEEIRALEpv 973
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 806638593 1532 -----QQVEEMKTQLEELEDELqatedAKLRLEvnlqamkaqfERDLQGRDEQSEEKKKQLVRQV 1591
Cdd:TIGR02169 974 nmlaiQEYEEVLKRLDELKEKR-----AKLEEE----------RKAILERIEEYEKKKREVFMEA 1023
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1080-1710 |
2.00e-19 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 95.52 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1080 KKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERACRNKAEKQKRDLGEELEALKTELEDtLDSTAaqQ 1159
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE-LEELK--E 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1160 ELRSKREQevsilKKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQ--TLENERGELANEVKALL 1237
Cdd:PRK03918 239 EIEELEKE-----LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1238 QGKGDSEHKRKKVEAQLQELQVKFSEGErvrtELADKVSKLQVELDSVtgllnqsdSKSSKLTKDFSALESQLQDTQELL 1317
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLE----ELKKKLKELEKRLEEL--------EERHELYEEAKAKKEELERLKKRL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1318 QEENRQKLSlsTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKK-KMEDGVGCLETAEEAKRRL----QK 1392
Cdd:PRK03918 382 TGLTPEKLE--KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKaKGKCPVCGRELTEEHRKELleeyTA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1393 DLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLlvdldhqrqsvSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAR 1472
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKE-----------SELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYE 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1473 EKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATE 1552
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELK 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1553 DAKLRLEVNLQAMKaqferDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSIAMAARK-----KLEMDLKDLEAHID 1627
Cdd:PRK03918 609 DAEKELEREEKELK-----KLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELreeylELSRELAGLRAELE 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1628 TANKNREEAIKQLRKLQaqmkdcmRELDDTRASREEIlaqakeneKKLKSMEAEMIQLQEELAAAE-RAKRQAQQERDEL 1706
Cdd:PRK03918 684 ELEKRREEIKKTLEKLK-------EELEEREKAKKEL--------EKLEKALERVEELREKVKKYKaLLKERALSKVGEI 748
|
....
gi 806638593 1707 ADEI 1710
Cdd:PRK03918 749 ASEI 752
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1141-1932 |
3.40e-19 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 95.19 E-value: 3.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1141 LEALKTELEDTLDSTAAQQELRSKreQEVSILKKTLEDEAKTHEAQIQ-----EMRQKHSQAVEELAEQLEQT-KRVKAT 1214
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEK--QKFYLRQSVIDLQTKLQEMQMErdamaDIRRRESQSQEDLRNQLQNTvHELEAA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1215 LEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRT----ELADKVSKLQVELDSVTGLL- 1289
Cdd:pfam15921 158 KCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTmhfrSLGSAISKILRELDTEISYLk 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1290 -------NQSDSKSSKLTKDFSALESQLQD-TQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLE----K 1357
Cdd:pfam15921 238 grifpveDQLEALKSESQNKIELLLQQHQDrIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNsmymR 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1358 QIATLHAQVTDMKKKMEdgvgcletaeEAKRRLQKDLEGLSQRLeekVAAYDKLEKTKTRLQQ---------ELDDLLVD 1428
Cdd:pfam15921 318 QLSDLESTVSQLRSELR----------EAKRMYEDKIEELEKQL---VLANSELTEARTERDQfsqesgnldDQLQKLLA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1429 LDHQRQSVSNLEKKQKK--FDQLLAEEKTISAKYAEERDRaEAEAREKETKALSLARALEEAMEQK-AELERLNKQFR-- 1503
Cdd:pfam15921 385 DLHKREKELSLEKEQNKrlWDRDTGNSITIDHLRRELDDR-NMEVQRLEALLKAMKSECQGQMERQmAAIQGKNESLEkv 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1504 -TEMEDLMSSKDDVGKSVHELEKSKRALE---QQVEEMKTQLEELEDELQAT--EDAKLRLEVNLQAMKAQFERDLQGRD 1577
Cdd:pfam15921 464 sSLTAQLESTKEMLRKVVEELTAKKMTLEsseRTVSDLTASLQEKERAIEATnaEITKLRSRVDLKLQELQHLKNEGDHL 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1578 EQSEEKKKQLVRQVREMEAELEDERKQrsiamaarkkLEMDLKDLEAHIDTANKNREEAIKqlrkLQAQMKDCMRELDDT 1657
Cdd:pfam15921 544 RNVQTECEALKLQMAEKDKVIEILRQQ----------IENMTQLVGQHGRTAGAMQVEKAQ----LEKEINDRRLELQEF 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1658 RASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIaqlEEE 1737
Cdd:pfam15921 610 KILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNF---RNK 686
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1738 LEEEQGNTELINDRLKKANLQIDQI-NTDLNLERS--HAQKNENARQqlerqnKELKAKlqemesavkskyKASIAALEA 1814
Cdd:pfam15921 687 SEEMETTTNKLKMQLKSAQSELEQTrNTLKSMEGSdgHAMKVAMGMQ------KQITAK------------RGQIDALQS 748
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1815 KIAQLEEQLDNETKERQAASKQVRRAEKKLKDVLL-------QVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQ 1887
Cdd:pfam15921 749 KIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATeknkmagELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQ 828
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 806638593 1888 R--ANASRRKLQRELeDATETADAMNREVSSLKNKLRRgdmPFVVTR 1932
Cdd:pfam15921 829 RqeQESVRLKLQHTL-DVKELQGPGYTSNSSMKPRLLQ---PASFTR 871
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
821-1611 |
6.29e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 94.36 E-value: 6.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 821 RLRNWQWWRLFTKVKPLLNSIRH-EDELLAKEAELTKVREKHLAAENRLTEMETMQSQLMAE--KLQLQEQLQAET---E 894
Cdd:TIGR02169 219 EKREYEGYELLKEKEALERQKEAiERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKikDLGEEEQLRVKEkigE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 895 LCAEAEELRARLTAKKQELEeichDLEARVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLK 974
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELE----DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 975 KLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERL-----RREEKQrQELEKT 1049
Cdd:TIGR02169 375 EVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKIneleeEKEDKA-LEIKKQ 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1050 RRKLEGDSTDLSD----------QIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISEL-QE 1118
Cdd:TIGR02169 454 EWKLEQLAADLSKyeqelydlkeEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLgSV 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1119 DLESERACRNKAekqkrdlGEELEALKteLEDTLDSTAAQQELRSKR------------EQEVSILKKTLEDEAKTHEAQ 1186
Cdd:TIGR02169 534 GERYATAIEVAA-------GNRLNNVV--VEDDAVAKEAIELLKRRKagratflplnkmRDERRDLSILSEDGVIGFAVD 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1187 IQEMRQKHSQAVeelaEQLEQTKRVKATLEKAKQTLENER-----GELANEVKALLQG----KGDSEHKRKKvEAQLQEL 1257
Cdd:TIGR02169 605 LVEFDPKYEPAF----KYVFGDTLVVEDIEAARRLMGKYRmvtleGELFEKSGAMTGGsrapRGGILFSRSE-PAELQRL 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1258 QVKFSEGERVRTELADKVSKLQVELDSVTGLLNQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDE 1337
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1338 KNSFREQLEEEEEAKRNLEKQIATLHAQVTDmkKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTR 1417
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1418 LQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELER 1497
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1498 LNKQFRTEMEDLMSSKDDVGKSVHELEKSKRAlEQQVEEMKTQLEELEDELQATEDaklrleVNLQAMKaQFERDLQGRD 1577
Cdd:TIGR02169 918 RLSELKAKLEALEEELSEIEDPKGEDEEIPEE-ELSLEDVQAELQRVEEEIRALEP------VNMLAIQ-EYEEVLKRLD 989
|
810 820 830
....*....|....*....|....*....|....*
gi 806638593 1578 EQsEEKKKQLVRQVREMEAELED-ERKQRSIAMAA 1611
Cdd:TIGR02169 990 EL-KEKRAKLEEERKAILERIEEyEKKKREVFMEA 1023
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
960-1569 |
6.59e-19 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 93.55 E-value: 6.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 960 QKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAK--------------LKNKH 1025
Cdd:TIGR04523 43 KTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSdlskinseikndkeQKNKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1026 EAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEEL---QAALARVEEEAAQKNMA 1102
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKlniQKNIDKIKNKLLKLELL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1103 L-------KKIRELETQISELQEDLESERACRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEV---SIL 1172
Cdd:TIGR04523 203 LsnlkkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELeqnNKK 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1173 KKTLEDEAKTHEAQIQEMRQKHSQaveelaeqlEQTKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKkvea 1252
Cdd:TIGR04523 283 IKELEKQLNQLKSEISDLNNQKEQ---------DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK---- 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1253 qlqELQVKFSEGERVRTELADKVSKLQVeldsvtgLLNQSDSKSS---KLTKDFSALESQLQDTQELLQEENRQKLSLST 1329
Cdd:TIGR04523 350 ---ELTNSESENSEKQRELEEKQNEIEK-------LKKENQSYKQeikNLESQINDLESKIQNQEKLNQQKDEQIKKLQQ 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1330 KLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYD 1409
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELK 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1410 KLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLA--EEKTISAKYAEERDRAEAEAREKETKalslaraLEE 1487
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISdlEDELNKDDFELKKENLEKEIDEKNKE-------IEE 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1488 AMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKA 1567
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKE 652
|
..
gi 806638593 1568 QF 1569
Cdd:TIGR04523 653 TI 654
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
961-1795 |
1.05e-18 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 93.26 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 961 KLQLEKVTTEAKlKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEamitdleerlRREE 1040
Cdd:pfam15921 73 KEHIERVLEEYS-HQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRES----------QSQE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1041 KQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKE---EELQAALARVEEEAAQK-----NMALKKIRELETQ 1112
Cdd:pfam15921 142 DLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKiyehdSMSTMHFRSLGSA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1113 ISELQEDLESERAcrnKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRskreqevsilkktLEDEAKTHEAQIQEMRQ 1192
Cdd:pfam15921 222 ISKILRELDTEIS---YLKGRIFPVEDQLEALKSESQNKIELLLQQHQDR-------------IEQLISEHEVEITGLTE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1193 KHSQAveelaeqLEQTKRVKATLEKAKQTLENERGELANEVKALlqgkgdsehkrkkvEAQLQELQVKFSEGERVrteLA 1272
Cdd:pfam15921 286 KASSA-------RSQANSIQSQLEIIQEQARNQNSMYMRQLSDL--------------ESTVSQLRSELREAKRM---YE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1273 DKVSKLQVELDSVTGLLNQSDSKSSKLTKDFSALESQLqdtQELLQEENRQKLSLSTKLKQME-----DEKNSFREQLEE 1347
Cdd:pfam15921 342 DKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL---QKLLADLHKREKELSLEKEQNKrlwdrDTGNSITIDHLR 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1348 EEEAKRNLEKQiaTLHAQVTDMKKKMEdgvGCLEtaeeakrRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQ---QELDD 1424
Cdd:pfam15921 419 RELDDRNMEVQ--RLEALLKAMKSECQ---GQME-------RQMAAIQGKNESLEKVSSLTAQLESTKEMLRkvvEELTA 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1425 LLVDLDHQRQSVSNLEKkqkkfdQLLAEEKTISAKYAE---ERDRAEAEARE-----KETKALSLARALEEAME-QKAEL 1495
Cdd:pfam15921 487 KKMTLESSERTVSDLTA------SLQEKERAIEATNAEitkLRSRVDLKLQElqhlkNEGDHLRNVQTECEALKlQMAEK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1496 ERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEdELQATEDAKLrlevnlqamkaqfeRDLQG 1575
Cdd:pfam15921 561 DKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFK-ILKDKKDAKI--------------RELEA 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1576 RDEQSEEKKKQLVRQVREMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKN----REEAIKQLRKLQAQMKDCM 1651
Cdd:pfam15921 626 RVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNfrnkSEEMETTTNKLKMQLKSAQ 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1652 RELDDTRASreeilaqakenekkLKSMEAE-------MIQLQEELaAAERAKRQAQQERDELADE-IANSSGKGALALEE 1723
Cdd:pfam15921 706 SELEQTRNT--------------LKSMEGSdghamkvAMGMQKQI-TAKRGQIDALQSKIQFLEEaMTNANKEKHFLKEE 770
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 806638593 1724 KRRLEARIAQLEEELEEEQGNTELIndRLKKANLQIDQINTDLNLERSHAQKNEnARQQLERQNKE-LKAKLQ 1795
Cdd:pfam15921 771 KNKLSQELSTVATEKNKMAGELEVL--RSQERRLKEKVANMEVALDKASLQFAE-CQDIIQRQEQEsVRLKLQ 840
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
857-1548 |
2.30e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 92.05 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 857 VREKHLAAENRLTEMETMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHD---LEARVEEEEERCQY 933
Cdd:PRK03918 146 SREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREineISSELPELREELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 934 LQAEKKKMQQniqeleeqleeEESARQKLQLEKVTTEAKLKKLEEDqiimedqncklakeKKLLEDRVAEFTTNLMEEEE 1013
Cdd:PRK03918 226 LEKEVKELEE-----------LKEEIEELEKELESLEGSKRKLEEK--------------IRELEERIEELKKEIEELEE 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1014 KSKSLAKLKNKHEAMITdLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKmQLAKKEEELQAALARVE 1093
Cdd:PRK03918 281 KVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1094 EEAAQKNMALKKIRELEtqiselqedleseracrnkaEKQKRDLGEELEALKTELEdtldstaaqqelrskreqEVSILK 1173
Cdd:PRK03918 359 ERHELYEEAKAKKEELE--------------------RLKKRLTGLTPEKLEKELE------------------ELEKAK 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1174 KTLEDEAKTHEAQIQEMRQKhsqaVEELAEQLEQTKRVKATLEKAKQTL-ENERGELANEVKALLqgkgdsehkrKKVEA 1252
Cdd:PRK03918 401 EEIEEEISKITARIGELKKE----IKELKKAIEELKKAKGKCPVCGRELtEEHRKELLEEYTAEL----------KRIEK 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1253 QLQELQVKFSEGERVRTELaDKVSKLQVELDSVTGLLNQSDSKSSKLTK-DFSALESQLQDTQELLQEENRQKLSLSTKL 1331
Cdd:PRK03918 467 ELKEIEEKERKLRKELREL-EKVLKKESELIKLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1332 KQMEdEKNSFREQLEEEEEAKRNLEKQIATLHaqvtdmKKKMEDGVGCLEtaeeakrrlqkDLEGLSQRLEEKVAAYDKL 1411
Cdd:PRK03918 546 KELE-KLEELKKKLAELEKKLDELEEELAELL------KELEELGFESVE-----------ELEERLKELEPFYNEYLEL 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1412 EKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEErdraeaEAREKETKALSLARALEEAMEQ 1491
Cdd:PRK03918 608 KDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE------EYEELREEYLELSRELAGLRAE 681
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 806638593 1492 KAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEqQVEEMKTQLEELEDEL 1548
Cdd:PRK03918 682 LEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALL 737
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
983-1637 |
3.05e-18 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 91.62 E-value: 3.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 983 MEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSD 1062
Cdd:TIGR04523 38 LEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1063 QIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERACRNKAEKQKRDLGEELE 1142
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1143 ALKTELEDTLDSTAAQQELRSK---REQEVSILKKTLED----------EAKTHEAQIQEMRQKHSQAVEELAE---QLE 1206
Cdd:TIGR04523 198 KLELLLSNLKKKIQKNKSLESQiseLKKQNNQLKDNIEKkqqeinekttEISNTQTQLNQLKDEQNKIKKQLSEkqkELE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1207 QTKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEhkRKKVEAQLQELQVKFSEGERVRTELADKVSKLQVELdsvT 1286
Cdd:TIGR04523 278 QNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSE--LKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKEL---T 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1287 GLLNQSDSKSSKLTKDFSALESQLQDTQELLQEENR---QKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLH 1363
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNlesQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1364 AQVTDMKKKMEDgvgcLETAEEAKRRLQKDLEGLSQRLEEKVAA----YDKLEKTKTRLQQELDDLLVDLDHQRQSVSNL 1439
Cdd:TIGR04523 433 ETIIKNNSEIKD----LTNQDSVKELIIKNLDNTRESLETQLKVlsrsINKIKQNLEQKQKELKSKEKELKKLNEEKKEL 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1440 EKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARAL----------------EEAMEQKAELERLNKQFR 1503
Cdd:TIGR04523 509 EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkenlekeideknkeiEELKQTQKSLKKKQEEKQ 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1504 TEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQF-------------- 1569
Cdd:TIGR04523 589 ELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIkeirnkwpeiikki 668
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 806638593 1570 -----------ERDLQGRDEQSEEKKKQLVRQVREMEAELEDErKQRSIAMAARKKLEMDlKDLEAHIDTANKNREEAI 1637
Cdd:TIGR04523 669 kesktkiddiiELMKDWLKELSLHYKKYITRMIRIKDLPKLEE-KYKEIEKELKKLDEFS-KELENIIKNFNKKFDDAF 745
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1185-1922 |
4.29e-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: 91.28 E-value: 4.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1185 AQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQTLENERGEL--ANEVKALLQGKGDSE-----HKRKKVEAQLQEL 1257
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERekAERYQALLKEKREYEgyellKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1258 QVKFSEGERVRTELADKVSKLQVELDSVTGLLNQSDSKSSKLTKDFSA--------LESQLQDTQELLQEENRQKLSLST 1329
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLrvkekigeLEAEIASLERSIAEKERELEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1330 KLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYD 1409
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1410 KLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDqllaeektisakyaEERDRAEAEAREKETKalslaraLEEAM 1489
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE--------------EEKEDKALEIKKQEWK-------LEQLA 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1490 EQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQF 1569
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAI 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1570 ERDLQGR-------DEQSEEKKKQLVRQVREMEA------ELEDERKQRS-IAMAARKKLEMDLKDLEAHI--------- 1626
Cdd:TIGR02169 542 EVAAGNRlnnvvveDDAVAKEAIELLKRRKAGRAtflplnKMRDERRDLSiLSEDGVIGFAVDLVEFDPKYepafkyvfg 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1627 DTANKNREEAIKQLrKLQAQMKDCMRELDD--------TRASREEILAQAKENEKkLKSMEAEMIQLQEELAAAERAKRQ 1698
Cdd:TIGR02169 622 DTLVVEDIEAARRL-MGKYRMVTLEGELFEksgamtggSRAPRGGILFSRSEPAE-LQRLRERLEGLKRELSSLQSELRR 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1699 AQQERDELADEIANSSgkgalalEEKRRLEARIaqleeeleeeqgntELINDRLKKANLQIDQINTDLnlershaQKNEN 1778
Cdd:TIGR02169 700 IENRLDELSQELSDAS-------RKIGEIEKEI--------------EQLEQEEEKLKERLEELEEDL-------SSLEQ 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1779 ARQQLERQNKELKAKLQEMEsAVKSKYKASIAALEAKIA-----QLEEQLDNETKERQAASKQVRRAEKKLKDVLL---Q 1850
Cdd:TIGR02169 752 EIENVKSELKELEARIEELE-EDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLekeY 830
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 806638593 1851 VEDERRNAEQ----FKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKLR 1922
Cdd:TIGR02169 831 LEKEIQELQEqridLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
997-1576 |
4.42e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 91.25 E-value: 4.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 997 LEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDST---DLSDQIAELQAQIAE 1073
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETERereELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1074 LkmqlakkEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESER----ACRNKAEK----------QKRDLGE 1139
Cdd:PRK02224 291 L-------EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRvaaqAHNEEAESlredaddleeRAEELRE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1140 ELEALKTELEDTldstaaqQELRSKREQEVSILKKTLEDEAKTHEaQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAK 1219
Cdd:PRK02224 364 EAAELESELEEA-------REAVEDRREEIEELEEEIEELRERFG-DAPVDLGNAEDFLEELREERDELREREAELEATL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1220 QTLENERgelaNEVKALL---------QGKGDSEHkrkkVEAqLQELQVKFSEGERVRTELADKVSKLQVELDSVTGLln 1290
Cdd:PRK02224 436 RTARERV----EEAEALLeagkcpecgQPVEGSPH----VET-IEEDRERVEELEAELEDLEEEVEEVEERLERAEDL-- 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1291 qsdsksSKLTKDFSALESQLQDTQELLqeenrqklslstklkqmEDEKNSFREQleeeeeakrnlEKQIATLHAQVTDMK 1370
Cdd:PRK02224 505 ------VEAEDRIERLEERREDLEELI-----------------AERRETIEEK-----------RERAEELRERAAELE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1371 KKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLqqelddllVDLDHQRQSVSNLEKKQKKFDQLL 1450
Cdd:PRK02224 551 AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLL--------AAIADAEDEIERLREKREALAELN 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1451 AEEKTisaKYAEERDRAEAEAREKEtkalslARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDvgksvheLEKSKRAL 1530
Cdd:PRK02224 623 DERRE---RLAEKRERKRELEAEFD------EARIEEAREDKERAEEYLEQVEEKLDELREERDD-------LQAEIGAV 686
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 806638593 1531 EQQVEEmktqLEELEDELQATEDAKLRLEV------NLQAMKAQFERDLQGR 1576
Cdd:PRK02224 687 ENELEE----LEELRERREALENRVEALEAlydeaeELESMYGDLRAELRQR 734
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1520-1909 |
4.43e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.15 E-value: 4.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1520 VHELEKSKRALEQQVE------EMKTQLEELEDELQATEDAKLRLEvnlqamkaqfERDLQGRDEQSEEKKKQLVRQVRE 1593
Cdd:COG1196 195 LGELERQLEPLERQAEkaeryrELKEELKELEAELLLLKLRELEAE----------LEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1594 MEAELEDERKQrsiamaarkklemdLKDLEAHIDTANKNREEAIKQLRKLQaqmkdcmRELDDTRASREEILAQAKENEK 1673
Cdd:COG1196 265 LEAELEELRLE--------------LEELELELEEAQAEEYELLAELARLE-------QDIARLEERRRELEERLEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1674 KLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANssgkgalalEEKRRLEARIAQLEEELEEEQGNTELINDRLK 1753
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE---------AEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1754 KANLQiDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAvkskyKASIAALEAKIAQLEEQLDNETKERQAA 1833
Cdd:COG1196 395 AAELA-AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE-----EEALEEAAEEEAELEEEEEALLELLAEL 468
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 806638593 1834 SKQVRRAEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQ-LKRQLEEAEEEAQRANASRRKLQRELEDATETADA 1909
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA 545
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
992-1866 |
9.43e-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: 90.42 E-value: 9.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 992 KEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQE--------------LEKTRRKLEGDS 1057
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAkkaleyyqlkekleLEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1058 TDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERACRNKAEKQKRDL 1137
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1138 GEELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEK 1217
Cdd:pfam02463 313 EEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1218 AKQTLE--NERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTEladKVSKLQVELDSVTGLLNQSDSK 1295
Cdd:pfam02463 393 KEEELElkSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLT---EEKEELEKQELKLLKDELELKK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1296 SSKLTKDFSALESQLQDTQEL---LQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKK 1372
Cdd:pfam02463 470 SEDLLKETQLVKLQEQLELLLsrqKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1373 MEDGVGCLETAEEAKRRLQKDLEG-LSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLA 1451
Cdd:pfam02463 550 IVEVSATADEVEERQKLVRALTELpLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGIL 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1452 EEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALE 1531
Cdd:pfam02463 630 KDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREK 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1532 QQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSIAMAA 1611
Cdd:pfam02463 710 EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVE 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1612 RKKLEmdlkDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAA 1691
Cdd:pfam02463 790 EEKEE----KLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITK 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1692 -AERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLER 1770
Cdd:pfam02463 866 eELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEA 945
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1771 SHAQKNENARQQLERQNKELKAKLQEMESaVKSKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRAEKKLKDVLLQ 1850
Cdd:pfam02463 946 DEKEKEENNKEEEEERNKRLLLAKEELGK-VNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLE 1024
|
890
....*....|....*.
gi 806638593 1851 VEDERRNAEQFKDQAD 1866
Cdd:pfam02463 1025 LFVSINKGWNKVFFYL 1040
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
847-1238 |
3.34e-17 |
|
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: 88.58 E-value: 3.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 847 LLAKEAELTKVREKhlaaenrlteMETMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELeeicHDLEARVEE 926
Cdd:TIGR02168 672 ILERRREIEELEEK----------IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI----SALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 927 EEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTT 1006
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1007 NLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEgdstdlsDQIAELQAQIAELKMQLAKKEEELQ 1086
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE-------ELIEELESELEALLNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1087 AALARVEEEAAQKNMALKKIRELETQISELQEDLESERACRNKAEKQKRDLgeeLEALKTELEDTLDSTAAQQELRSKRE 1166
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL---QERLSEEYSLTLEEAEALENKIEDDE 967
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 806638593 1167 QEvsilkktLEDEAKTHEAQIQEMRQKHSQAVEELAEQ---LEQTKRVKATLEKAKQTLENERGELANEVKALLQ 1238
Cdd:TIGR02168 968 EE-------ARRRLKRLENKIKELGPVNLAAIEEYEELkerYDFLTAQKEDLTEAKETLEEAIEEIDREARERFK 1035
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
845-1682 |
5.97e-17 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 87.79 E-value: 5.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 845 DELLAKEAELTKVREKHLAAE-------NRLTEMETMQSQLMaeklQLQEQLQAETELCAEAEELRARLTAKK------- 910
Cdd:TIGR00606 224 DQITSKEAQLESSREIVKSYEneldplkNRLKEIEHNLSKIM----KLDNEIKALKSRKKQMEKDNSELELKMekvfqgt 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 911 -QELEEICHDLEARVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCK 989
Cdd:TIGR00606 300 dEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 990 LAKEKKLLEDRVAEFTTNLMEE--EEKSKSLAKLKNkheamitDLEERLRREEKQRQELEKTR----RKLEGDSTDLSDQ 1063
Cdd:TIGR00606 380 DGFERGPFSERQIKNFHTLVIErqEDEAKTAAQLCA-------DLQSKERLKQEQADEIRDEKkglgRTIELKKEILEKK 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1064 IAELQAQIAELKM------QLAKKEEELQAALARVEEEAAQKNMALKKIRELETQiselQEDLESERACRNKAEKQKrDL 1137
Cdd:TIGR00606 453 QEELKFVIKELQQlegssdRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQ----NEKADLDRKLRKLDQEME-QL 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1138 GEELEALKTELEDTLDSTAAQQELRSKREQEVSIL---------KKTLEDEAKTHEAQIQEMRQKHSQAVEELAeQLEQT 1208
Cdd:TIGR00606 528 NHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELtsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELA-SLEQN 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1209 KRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVE---AQLQELQVKFSEGERVRTELADKVSKLQVELDSV 1285
Cdd:TIGR00606 607 KNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEkssKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRV 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1286 TGLLNQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQ 1365
Cdd:TIGR00606 687 FQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKND 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1366 VTDMKKKMEDGVGCLETAEEAK------RRLQKDLEGLSQRLEEKVAAYD--KLEKTKTRLQQELDDLLVDLDHQRQSVS 1437
Cdd:TIGR00606 767 IEEQETLLGTIMPEEESAKVCLtdvtimERFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSKIE 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1438 NLEK----KQKKFDQL------LAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEME 1507
Cdd:TIGR00606 847 LNRKliqdQQEQIQHLksktneLKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKE 926
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1508 DLMSSKDDVGKSVH-ELEKSKRALEQQVEEMKTQLEELEDelqATEDAKLRLEVNLQAMKAQFerdlqgrdEQSEEKKKQ 1586
Cdd:TIGR00606 927 ELISSKETSNKKAQdKVNDIKEKVKNIHGYMKDIENKIQD---GKDDYLKQKETELNTVNAQL--------EECEKHQEK 995
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1587 LVRQVREMEAELEDERKQRSIAM--AARKKLEMDLKDLEAHIDTANKNREEaiKQLRKLQAQMKDCMRELDDTRASREEI 1664
Cdd:TIGR00606 996 INEDMRLMRQDIDTQKIQERWLQdnLTLRKRENELKEVEEELKQHLKEMGQ--MQVLQMKQEHQKLEENIDLIKRNHVLA 1073
|
890
....*....|....*...
gi 806638593 1665 LAQAKENEKKLKSMEAEM 1682
Cdd:TIGR00606 1074 LGRQKGYEKEIKHFKKEL 1091
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1015-1706 |
7.08e-17 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 87.28 E-value: 7.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1015 SKSLAKLKNKHEAMITDLE--ERLRREEKQRQELEKTRRKLEgdstDLSDQIAELQAQIAELKMQLAKKE-EELQAALAR 1091
Cdd:COG4913 231 VEHFDDLERAHEALEDAREqiELLEPIRELAERYAAARERLA----ELEYLRAALRLWFAQRRLELLEAElEELRAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1092 VEEEaaqknmalkkIRELETQISELQEDLESeracrnkAEKQKRDL-GEELEALKTELEDtldstaAQQELRsKREQEVS 1170
Cdd:COG4913 307 LEAE----------LERLEARLDALREELDE-------LEAQIRGNgGDRLEQLEREIER------LERELE-ERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1171 ILKKTLED---EAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQTLENERGELANEVKALlqgkgdsEHKR 1247
Cdd:COG4913 363 RLEALLAAlglPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL-------ERRK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1248 KKVEAQLQELqvkfsegervRTELADKVSKLQVELDSVTGLLnqsdsksskltkDFSALESQLQDTQELLQeeNRQKLSL 1327
Cdd:COG4913 436 SNIPARLLAL----------RDALAEALGLDEAELPFVGELI------------EVRPEEERWRGAIERVL--GGFALTL 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1328 ---STKLKQMED--EKNSFREQLEEEEEAKRNLEKQIATLHAQVTdmkkkmedgVGCLETAE-EAKRRLQKDLEGLSQRL 1401
Cdd:COG4913 492 lvpPEHYAAALRwvNRLHLRGRLVYERVRTGLPDPERPRLDPDSL---------AGKLDFKPhPFRAWLEAELGRRFDYV 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1402 eeKVAAYDKLEKTKTRLQQELDDLLVDLDHQ--------RQSV---SNLEKKQKKFDQLLAEEKTIsAKYAEERDRAEAE 1470
Cdd:COG4913 563 --CVDSPEELRRHPRAITRAGQVKGNGTRHEkddrrrirSRYVlgfDNRAKLAALEAELAELEEEL-AEAEERLEALEAE 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1471 AREKETKALSLARALEEAMEQK------AELERLNKQfrteMEDLMSSKDDVgksvhelekskRALEQQVEEMKTQLEEL 1544
Cdd:COG4913 640 LDALQERREALQRLAEYSWDEIdvasaeREIAELEAE----LERLDASSDDL-----------AALEEQLEELEAELEEL 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1545 EDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSIAmaarkklemdlKDLEA 1624
Cdd:COG4913 705 EEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR-----------ENLEE 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1625 HIDTANKNREEAIKQLRKLQAQMK----DCMRELDDTRASREEILA-------------QAKENEKKLKSMEAEMIQLQE 1687
Cdd:COG4913 774 RIDALRARLNRAEEELERAMRAFNrewpAETADLDADLESLPEYLAlldrleedglpeyEERFKELLNENSIEFVADLLS 853
|
730
....*....|....*....
gi 806638593 1688 ELaaaERAKRQAQQERDEL 1706
Cdd:COG4913 854 KL---RRAIREIKERIDPL 869
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1380-1879 |
1.16e-16 |
|
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: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1380 LETAEEAKRRLQkDLEGLSQRLEEKVAAYDKLEKTKTRL-----QQELDDLLVDLDHQRQSVSNLEKK----QKKFDQLL 1450
Cdd:COG4913 244 LEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAElerlEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1451 AEEKTISAKYAE-----------ERDRAEAEAREKETKALSLARALEeAMEQKAELERlnKQFRTEMEDLMSSKDDVGKS 1519
Cdd:COG4913 323 EELDELEAQIRGnggdrleqlerEIERLERELEERERRRARLEALLA-ALGLPLPASA--EEFAALRAEAAALLEALEEE 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1520 VHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDL--------------QGRDEQSE---- 1581
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALgldeaelpfvgeliEVRPEEERwrga 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1582 ----------------------------EKKKQLVR--QVREMEAELEDER-KQRSIAM-------AARKKLEMDLKDLE 1623
Cdd:COG4913 480 iervlggfaltllvppehyaaalrwvnrLHLRGRLVyeRVRTGLPDPERPRlDPDSLAGkldfkphPFRAWLEAELGRRF 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1624 AHIDTANknrEEAIKQLRK---LQAQMKD--CMRELDDTRASREE-ILAQakENEKKLKSMEAEMIQLQEELAAAERAKR 1697
Cdd:COG4913 560 DYVCVDS---PEELRRHPRaitRAGQVKGngTRHEKDDRRRIRSRyVLGF--DNRAKLAALEAELAELEEELAEAEERLE 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1698 QAQQERDeladeianssgkgalALEEKRRLEARIAQLEEELeeeqgntelinDRLKKANLQIDQintdLNLERSHAQKNE 1777
Cdd:COG4913 635 ALEAELD---------------ALQERREALQRLAEYSWDE-----------IDVASAEREIAE----LEAELERLDASS 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1778 NARQQLERQNKELKAKLQEMESAVKSKYKAsIAALEAKIAQLEEQLDNETKERQAASKQVR-----RAEKKLKDVLLQvE 1852
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGE-IGRLEKELEQAEEELDELQDRLEAAEDLARlelraLLEERFAAALGD-A 762
|
570 580
....*....|....*....|....*..
gi 806638593 1853 DERRNAEQFKDQADKASTRLKQLKRQL 1879
Cdd:COG4913 763 VERELRENLEERIDALRARLNRAEEEL 789
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1612-1922 |
2.66e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 85.37 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1612 RKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMR------ELDDTRAS-----REEILAQAKENEKKLKSMEA 1680
Cdd:COG1196 174 KEEAERKLEATEENLERLEDILGELERQLEPLERQAEKAERyrelkeELKELEAEllllkLRELEAELEELEAELEELEA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1681 EMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQID 1760
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1761 QINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSKyKASIAALEAKIAQLEEQLDNETKERQAASKQVRRA 1840
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA-EEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1841 EKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNK 1920
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
..
gi 806638593 1921 LR 1922
Cdd:COG1196 493 LL 494
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
849-1442 |
2.81e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 85.58 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 849 AKEAELTKVREKHLAAENRLTEMETMQSQL---MAEKLQLQEQLQAETELCAEAEELRARLTAKKQ------ELEEICHD 919
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAkkkAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKadeakkKAEEKKKA 1433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 920 LEARVEEEEERCQ---YLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKlKKLEEDQIIMEDQNCKLAKEKKL 996
Cdd:PTZ00121 1434 DEAKKKAEEAKKAdeaKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAK-KKAEEAKKKADEAKKAAEAKKKA 1512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 997 LEDRVAEFTTNL-----MEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRrklEGDSTDLSDQIAELQAQI 1071
Cdd:PTZ00121 1513 DEAKKAEEAKKAdeakkAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKK---AEEDKNMALRKAEEAKKA 1589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1072 AELK----MQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESEracRNKAEKQKRDlgEELEALKTE 1147
Cdd:PTZ00121 1590 EEARieevMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE---KKKAEELKKA--EEENKIKAA 1664
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1148 LEdtldstaAQQELRSKREQEVsiLKKTLEDEAKTHEAQIQEMRQKhsQAVEELAEQLEQTKRVKATLEKAkqtlENERG 1227
Cdd:PTZ00121 1665 EE-------AKKAEEDKKKAEE--AKKAEEDEKKAAEALKKEAEEA--KKAEELKKKEAEEKKKAEELKKA----EEENK 1729
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1228 ELANEVKallqgKGDSEHKRKKVEAQLQE------LQVKFSEGERVRTELADKVSKLQVELDSVTGLLNQSDSKSSKLTK 1301
Cdd:PTZ00121 1730 IKAEEAK-----KEAEEDKKKAEEAKKDEeekkkiAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIF 1804
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1302 DFSALESQLQDTQELLQeeNRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLE 1381
Cdd:PTZ00121 1805 DNFANIIEGGKEGNLVI--NDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEE 1882
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 806638593 1382 TAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDhQRQSVSNLEKK 1442
Cdd:PTZ00121 1883 EIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEE-TREEIIKISKK 1942
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
965-1707 |
4.12e-16 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 85.02 E-value: 4.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 965 EKVTTEAKLKKLEEDQII--MEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKS--KSLAKLKNKHEAMITDLEERLRREE 1040
Cdd:TIGR00618 164 EKKELLMNLFPLDQYTQLalMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTyhERKQVLEKELKHLREALQQTQQSHA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1041 KQRQELEK--TRRKLEGDSTDLSDQIAELQAQIAELkmQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQE 1118
Cdd:TIGR00618 244 YLTQKREAqeEQLKKQQLLKQLRARIEELRAQEAVL--EETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMR 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1119 DLESERACRNKAEKQKRDLGEELEALKTELedtldstaaQQELRSKREQEVSILKKTLEDEAKTHEaqiqemrqkhsQAV 1198
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQSSIEEQRRLLQTLH---------SQEIHIRDAHEVATSIREISCQQHTLT-----------QHI 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1199 EELAEQLEQTKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVSKL 1278
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1279 QveldsvtgllnqsdskssKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEeeakrNLEKQ 1358
Cdd:TIGR00618 462 Q------------------ESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHP-----NPARQ 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1359 IATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSN 1438
Cdd:TIGR00618 519 DIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQD 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1439 LEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLAraLEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGK 1518
Cdd:TIGR00618 599 LTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA--LKLTALHALQLTLTQERVREHALSIRVLPKELLA 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1519 SVHELEKSKRALEQQVEEMKTQLEELEDELQATEDA--KLRLEVN-LQAMKAQFERDLQGRDEQSEEKKKQLVRQVREME 1595
Cdd:TIGR00618 677 SRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHieEYDREFNeIENASSSLGSDLAAREDALNQSLKELMHQARTVL 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1596 AELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEK-K 1674
Cdd:TIGR00618 757 KARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLsR 836
|
730 740 750
....*....|....*....|....*....|...
gi 806638593 1675 LKSMEAEMIQLQEELAAAERAKRQAQQERDELA 1707
Cdd:TIGR00618 837 LEEKSATLGEITHQLLKYEECSKQLAQLTQEQA 869
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1006-1730 |
6.32e-16 |
|
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: 84.50 E-value: 6.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1006 TNLMEEEEKSKSL-AKLKNKHEAmITDLEERLRREEKQRQELEKTRR-KLEGDSTDLSDQIAELQAQIAELKMQLAKKEE 1083
Cdd:pfam12128 244 TKLQQEFNTLESAeLRLSHLHFG-YKSDETLIASRQEERQETSAELNqLLRTLDDQWKEKRDELNGELSAADAAVAKDRS 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1084 ELQAA--------LARVEEEAAQKNMALKKIRELETQISELQEDLESERACRNKAEKQKRDLGEELealKTELEDTLDST 1155
Cdd:pfam12128 323 ELEALedqhgaflDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQN---NRDIAGIKDKL 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1156 AAQQELRSKREQEVSILKKTLEDEAKT-HEAQIQEM----------------RQKHSQAVEELAEQLEQTKrvkATLEKA 1218
Cdd:pfam12128 400 AKIREARDRQLAVAEDDLQALESELREqLEAGKLEFneeeyrlksrlgelklRLNQATATPELLLQLENFD---ERIERA 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1219 KQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVSKLQVELDSVTGLLNQSDSK--S 1296
Cdd:pfam12128 477 REEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKviS 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1297 SKLTK----DFSALESQLQDTQEL----LQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTD 1368
Cdd:pfam12128 557 PELLHrtdlDPEVWDGSVGGELNLygvkLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEK 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1369 MKKKMEDGVGCLETAEEAKRRLQkdleglsqrlEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSvsnLEKKQKKFDQ 1448
Cdd:pfam12128 637 ASREETFARTALKNARLDLRRLF----------DEKQSEKDKKNKALAERKDSANERLNSLEAQLKQ---LDKKHQAWLE 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1449 LLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAmEQKAELERLNKQFRTEMedlmsskddvgksvheleKSKR 1528
Cdd:pfam12128 704 EQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRS-GAKAELKALETWYKRDL------------------ASLG 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1529 ALEQQVEEMKTQLEELEDELQatedaklRLEVNLQAMkAQFERDLQgrdEQSEEKKKQLVRQVREMEAELEDerkqrsia 1608
Cdd:pfam12128 765 VDPDVIAKLKREIRTLERKIE-------RIAVRRQEV-LRYFDWYQ---ETWLQRRPRLATQLSNIERAISE-------- 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1609 maarkkLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDtRASREEILAQAKENEKKLKSMEAEMIQLQEE 1688
Cdd:pfam12128 826 ------LQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRC-EMSKLATLKEDANSEQAQGSIGERLAQLEDL 898
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 806638593 1689 LAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEAR 1730
Cdd:pfam12128 899 KLKRDYLSESVKKYVEHFKNVIADHSGSGLAETWESLREEDH 940
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1102-1920 |
1.66e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 83.27 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1102 ALKKIRELETQISELQEDLESERACRNKAE---KQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLED 1178
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEearKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1179 EAKTHEAQIQEMRQKhsqavEELAEQLEQTKRVKAtLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQ 1258
Cdd:PTZ00121 1163 ARKAEEARKAEDAKK-----AEAARKAEEVRKAEE-LRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAK 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1259 VKFSEGERVRTELADKVSKLQVELDSVTGLLNQSDSKSSKLTKdfsalesqlqdTQELLQEENRQKlslSTKLKQMEDEK 1338
Cdd:PTZ00121 1237 KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK-----------ADELKKAEEKKK---ADEAKKAEEKK 1302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1339 NSfrEQLEEEEEAKRNLEkqiatlhaqvtDMKKKMEDGVgclETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRL 1418
Cdd:PTZ00121 1303 KA--DEAKKKAEEAKKAD-----------EAKKKAEEAK---KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1419 QQELDDLLVDLDHQRQSVSNLEKKQKkfdqllAEEktisAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERL 1498
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKK------ADE----AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA 1436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1499 NKQFRTEME-DLMSSKDDVGKSVHELEKsKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRD 1577
Cdd:PTZ00121 1437 KKKAEEAKKaDEAKKKAEEAKKAEEAKK-KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA 1515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1578 EQSEEKKKQLVRQVREMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQmkdcmrELDDT 1657
Cdd:PTZ00121 1516 KKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE------EAKKA 1589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1658 RASREEILAQAKENEKKLKSmeaemiqlqEELAAAERAKRQAQQERDELADEIANSSGKGALAlEEKRRLEariaqleee 1737
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKA---------EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA-EEKKKAE--------- 1650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1738 leeeqgntelindRLKKANlqidqintdlnlershaQKNENARQQLERQNKELKAKLQEMESAVKSKYKASIAAL-EAKI 1816
Cdd:PTZ00121 1651 -------------ELKKAE-----------------EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKkEAEE 1700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1817 AQLEEQLDNETKERQAASKQVRRAEKKLKdvlLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKL 1896
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEELKKAEEENK---IKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
810 820
....*....|....*....|....
gi 806638593 1897 QRELEDATETADAMNREVSSLKNK 1920
Cdd:PTZ00121 1778 EAVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
855-1717 |
2.38e-15 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 82.33 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 855 TKVREKHLAAENRLTEMETMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQYL 934
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 935 QAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEK 1014
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1015 SKSLAKLKNKHEamITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEE 1094
Cdd:pfam02463 325 KAEKELKKEKEE--IEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1095 EAAQKNMALKKIRELETQISELQEDLESERACRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVSILKK 1174
Cdd:pfam02463 403 EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1175 TLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQTLENERGELA---------NEVKALLQGKGDSEH 1245
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVenykvaistAVIVEVSATADEVEE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1246 KRKKVEAQLQELQVKFSEGERVRTELADKVSKLQVELDSVTGLLNQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKL 1325
Cdd:pfam02463 563 RQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAK 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1326 SLSTKLKQMEDEKnsfREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEdgvgcLETAEEAKRRLQKDLEGLSQRLEEKV 1405
Cdd:pfam02463 643 AKESGLRKGVSLE---EGLAEKSEVKASLSELTKELLEIQELQEKAESE-----LAKEEILRRQLEIKKKEQREKEELKK 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1406 AAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFD-------QLLAEEKTISAKYAEERDRAEAEAREKETKA 1478
Cdd:pfam02463 715 LKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRlkkeekeEEKSELSLKEKELAEEREKTEKLKVEEEKEE 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1479 LSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRL 1558
Cdd:pfam02463 795 KLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLL 874
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1559 EVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQrsIAMAARKKLEMDLKDLEAHIDTANKNREEAIK 1638
Cdd:pfam02463 875 KEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIE--ERIKEEAEILLKYEEEPEELLLEEADEKEKEE 952
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1639 QLRKLQAQMKDCM-RELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKG 1717
Cdd:pfam02463 953 NNKEEEEERNKRLlLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKG 1032
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1161-1730 |
2.54e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.01 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1161 LRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQTLENERGELAnEVKALlqgk 1240
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE-ELETL---- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1241 gdsehkrkkvEAQLQELQVKFSEGERVRTELADKVSKLQVELDSVtgllnqSDSKSSKLTKdfSALESQLQDTQELLQEE 1320
Cdd:PRK02224 257 ----------EAEIEDLRETIAETEREREELAEEVRDLRERLEEL------EEERDDLLAE--AGLDDADAEAVEARREE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1321 -NRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQ 1399
Cdd:PRK02224 319 lEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1400 RLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAkyaeerdraeaearEKETKAL 1479
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPEC--------------GQPVEGS 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1480 SLARALEEAMEQKAELERLNKQFRTEMEDLmSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDaklRLE 1559
Cdd:PRK02224 465 PHVETIEEDRERVEELEAELEDLEEEVEEV-EERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRE---RAE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1560 vNLQAMKAQFERDLQGRDEQSEEKKKQlVRQVREMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREEaikq 1639
Cdd:PRK02224 541 -ELRERAAELEAEAEEKREAAAEAEEE-AEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREK---- 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1640 lRKLQAQMKDCMRELDDTRASREEILAqAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKgal 1719
Cdd:PRK02224 615 -REALAELNDERRERLAEKRERKRELE-AEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENE--- 689
|
570
....*....|.
gi 806638593 1720 aLEEKRRLEAR 1730
Cdd:PRK02224 690 -LEELEELRER 699
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
960-1851 |
1.29e-14 |
|
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: 80.09 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 960 QKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLL---EDRVAEFTTNLMEEEEKSKSLAKLKNKheamITDLEERL 1036
Cdd:TIGR00606 203 QEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVksyENELDPLKNRLKEIEHNLSKIMKLDNE----IKALKSRK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1037 RREEKQRQELEKTRRK-LEGDSTDLSDQIAELQAQIAElkmqlakKEEELQAALARVEEEAAQKNMALKKIRELETQISE 1115
Cdd:TIGR00606 279 KQMEKDNSELELKMEKvFQGTDEQLNDLYHNHQRTVRE-------KERELVDCQRELEKLNKERRLLNQEKTELLVEQGR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1116 LQEdleseRACRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREqevsILKKTLEDEAKTHEAQIQEMRQKHS 1195
Cdd:TIGR00606 352 LQL-----QADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHT----LVIERQEDEAKTAAQLCADLQSKER 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1196 QAVEELAEQLEQTKRVKATLEKAKQTLENERGELANEVKALLQGKGDS------EHKRKKVEAQLQEL------QVKFSE 1263
Cdd:TIGR00606 423 LKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSdrilelDQELRKAERELSKAeknsltETLKKE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1264 GERVRTELADKVSKLQV------ELDSVTGLLNQSDS-KSSKLTKDFSALESQLQDTQELLQE----ENRQKL-----SL 1327
Cdd:TIGR00606 503 VKSLQNEKADLDRKLRKldqemeQLNHHTTTRTQMEMlTKDKMDKDEQIRKIKSRHSDELTSLlgyfPNKKQLedwlhSK 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1328 STKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGClETAEEAKRRLQKDLEGLSQR---LEEK 1404
Cdd:TIGR00606 583 SKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLERLKEEIEKSSKQramLAGA 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1405 VAAY------------------DKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDR 1466
Cdd:TIGR00606 662 TAVYsqfitqltdenqsccpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1467 AEAEAREKETKALSLARaleEAMEQKAELERLNKQFRTEMEDLMSSKD---DVGksvhelekSKRALEQQVEEMKTQLEE 1543
Cdd:TIGR00606 742 KEKEIPELRNKLQKVNR---DIQRLKNDIEEQETLLGTIMPEEESAKVcltDVT--------IMERFQMELKDVERKIAQ 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1544 LEDELQATEDAKLRLEVNLQAMKAQFERD-----LQGRDEQSEEKKKQlVRQVREMEAELEDERKQRSIAMAARKKLEMD 1618
Cdd:TIGR00606 811 QAAKLQGSDLDRTVQQVNQEKQEKQHELDtvvskIELNRKLIQDQQEQ-IQHLKSKTNELKSEKLQIGTNLQRRQQFEEQ 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1619 LKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMrelddtraSREEILAQAKENEKKLKSMEAEMI--QLQEELAAAERAK 1696
Cdd:TIGR00606 890 LVELSTEVQSLIREIKDAKEQDSPLETFLEKDQ--------QEKEELISSKETSNKKAQDKVNDIkeKVKNIHGYMKDIE 961
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1697 RQAQQERDELADEIANSSGKGALALEEKRRLEARIaQLEEELEEEQGNTELINDRLKKANLQIDQINTDLN-LERSHAQK 1775
Cdd:TIGR00606 962 NKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKI-NEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKeVEEELKQH 1040
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 806638593 1776 NENARQQLERQNKELKAKLQEMESAVKSKykasiaalEAKIAQLEEQLDNETK--ERQAASKQVRRAEKKLKDVLLQV 1851
Cdd:TIGR00606 1041 LKEMGQMQVLQMKQEHQKLEENIDLIKRN--------HVLALGRQKGYEKEIKhfKKELREPQFRDAEEKYREMMIVM 1110
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
850-1393 |
1.31e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.19 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 850 KEAELTKVREKHLAAENRLTEMETMQSQLmaeKLQLQEQLQAEtELCAEAEELRARLTAKKQELEEICHDLEARVEEEEE 929
Cdd:PTZ00121 1279 KADELKKAEEKKKADEAKKAEEKKKADEA---KKKAEEAKKAD-EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEA 1354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 930 RCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKlKKLEEDQIIMEDQNCKLAKEKKLLEdrvaefttnLM 1009
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK-KKAEEDKKKADELKKAAAAKKKADE---------AK 1424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1010 EEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQelEKTRRKLEgdstdlsdqiAELQAQIAELKMQLAKKEEELQaal 1089
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA--EEAKKKAE----------EAKKADEAKKKAEEAKKADEAK--- 1489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1090 aRVEEEAAQKNMALKKIRELETQISELQEDLESERA--CRNKAEKQKRDlgeelEALKTELEDTLDSTAAQQELRSKREQ 1167
Cdd:PTZ00121 1490 -KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAdeAKKAEEAKKAD-----EAKKAEEKKKADELKKAEELKKAEEK 1563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1168 EVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKA----TLEKAKQTLENERGELANEVKALLQGKGDS 1243
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAeeakKAEEAKIKAEELKKAEEEKKKVEQLKKKEA 1643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1244 EHKRKKVEAQLQELQVKFSEGERVRTELADK-----VSKLQVELDSVTGLLNQSDSKSSKLTKDFSALESQLQDTQELLQ 1318
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKKAEEDKkkaeeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK 1723
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 806638593 1319 EENRQKLSLStKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKD 1393
Cdd:PTZ00121 1724 AEEENKIKAE-EAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
833-1452 |
3.09e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 78.86 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 833 KVKPLLNSIRHEDELLAKEAELTKVREKHLAAENRLTEMETMQSQLMAEKLQLQEQLQAETELCAEAEELRArltakKQE 912
Cdd:TIGR00618 281 ETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHS-----QEI 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 913 LEEICHDLEARVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKL--KKLEEDQIIMEDQNCKL 990
Cdd:TIGR00618 356 HIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTsaFRDLQGQLAHAKKQQEL 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 991 AKEKKLLEDRVAEFTTN--LMEEEEKSKSLAKLKNKHEaMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQ 1068
Cdd:TIGR00618 436 QQRYAELCAAAITCTAQceKLEKIHLQESAQSLKEREQ-QLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPN 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1069 AqiaelKMQLAKKEEELQAALARVEEEAAQKNMALKKIR----ELETQISELQEDLESERACRNKAEKQKRDLGEELEAL 1144
Cdd:TIGR00618 515 P-----ARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYhqltSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1145 KTELEDTLDSTAAQQELRSKREQEVSILKKTLEdeaktHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQTlen 1224
Cdd:TIGR00618 590 QNITVRLQDLTEKLSEAEDMLACEQHALLRKLQ-----PEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVR--- 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1225 ergelanevKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVSKLQVELDSV---TGLLNQSDSKSSKLTK 1301
Cdd:TIGR00618 662 ---------EHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIeeyDREFNEIENASSSLGS 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1302 DFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQL-EEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCL 1380
Cdd:TIGR00618 733 DLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEI 812
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 806638593 1381 ETAEEAK----RRLQKDLEGLSQRLEEkvaaydklektKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAE 1452
Cdd:TIGR00618 813 PSDEDILnlqcETLVQEEEQFLSRLEE-----------KSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1385-1901 |
3.22e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.57 E-value: 3.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1385 EAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEER 1464
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1465 DRAEaEAREKETKALSLARALEEAMEQKAELERLNKqfrtEMEDLMSSKDDVGKSVHELEKSKRALEQQV---EEMKTQL 1541
Cdd:PRK03918 266 ERIE-ELKKEIEELEEKVKELKELKEKAEEYIKLSE----FYEEYLDELREIEKRLSRLEEEINGIEERIkelEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1542 EELEDELQATEDAKLRLEVNLQAmkaqFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSIAMAARKKLEMDLKD 1621
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHEL----YEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1622 LEAHIdtanKNREEAIKQLRKLQAQMKDCMRELDDTRasREEILAqakENEKKLKSMEAEMIQLQEELAAAERAKRQAQQ 1701
Cdd:PRK03918 417 LKKEI----KELKKAIEELKKAKGKCPVCGRELTEEH--RKELLE---EYTAELKRIEKELKEIEEKERKLRKELRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1702 ERD---------ELADEIANSSGK-GALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERS 1771
Cdd:PRK03918 488 VLKkeseliklkELAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1772 HAQKNENARQQLERQN----KELKAKLQEMESAVK-----SKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRAEK 1842
Cdd:PRK03918 568 LEEELAELLKELEELGfesvEELEERLKELEPFYNeylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 806638593 1843 KLKDVLLQVEDERRnaEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELE 1901
Cdd:PRK03918 648 ELEELEKKYSEEEY--EELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE 704
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
846-1413 |
3.48e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.57 E-value: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 846 ELLAKEAELTKVREKHLAAENRLTEMETMQ---SQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEa 922
Cdd:PRK03918 208 EINEISSELPELREELEKLEKEVKELEELKeeiEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 923 RVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQlekvtteAKLKKLEEDQIIMEdqncKLAKEKKLLEDRVA 1002
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIE-------ERIKELEEKEERLE----ELKKKLKELEKRLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1003 EFTTNLmEEEEKSKSLAKLKNKHEAMITDLEerLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKmqlaKKE 1082
Cdd:PRK03918 356 ELEERH-ELYEEAKAKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK----KAI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1083 EELQAA------LARVEEEAAQKNMALKKIRELETQISELQEDLESERACRNKAEKQKRDLGEELEALKteLEDTLDsta 1156
Cdd:PRK03918 429 EELKKAkgkcpvCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK--LKELAE--- 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1157 aqqELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQ--AVEELAEQLEQTKRVKATLEKAKQTLENERGELANEVK 1234
Cdd:PRK03918 504 ---QLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEikSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELE 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1235 ALlqGKGDSEHKRKKVEaQLQELQVKFSEGERVRTELADKVSKLQVELDSvtglLNQSDSKSSKLTKDFSALESQLQDTQ 1314
Cdd:PRK03918 581 EL--GFESVEELEERLK-ELEPFYNEYLELKDAEKELEREEKELKKLEEE----LDKAFEELAETEKRLEELRKELEELE 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1315 ELLQEENRQKlsLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDgvgcLETAEEAKRRLqkdl 1394
Cdd:PRK03918 654 KKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE----LEKLEKALERV---- 723
|
570
....*....|....*....
gi 806638593 1395 eglsQRLEEKVAAYDKLEK 1413
Cdd:PRK03918 724 ----EELREKVKKYKALLK 738
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
931-1709 |
5.15e-14 |
|
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: 77.84 E-value: 5.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 931 CQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLK----KLEEDQIIMEDQNcKLAKEKKLLEDRVaefTT 1006
Cdd:pfam05483 59 CHYQEGLKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKqkenKLQENRKIIEAQR-KAIQELQFENEKV---SL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1007 NLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAelqaqiaelKMQLAKKEEELQ 1086
Cdd:pfam05483 135 KLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIE---------KMILAFEELRVQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1087 AALARVEEEAaqknmalkKIRELETQISELQEDLESERacrNKAEKQKRDLGEELEALKTELEDTldsTAAQQELRSKRE 1166
Cdd:pfam05483 206 AENARLEMHF--------KLKEDHEKIQHLEEEYKKEI---NDKEKQVSLLLIQITEKENKMKDL---TFLLEESRDKAN 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1167 QevsilkktLEDEAKTHEAQIQEMRQKHSQAVEELAEqleqtkrVKATLEKAKQTLENERGELANEVKALLQgkgdsehK 1246
Cdd:pfam05483 272 Q--------LEEKTKLQDENLKELIEKKDHLTKELED-------IKMSLQRSMSTQKALEEDLQIATKTICQ-------L 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1247 RKKVEAQLQELQVKFSEGERVRTELADKVSKLQVELDSVTGLLNQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLS 1326
Cdd:pfam05483 330 TEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1327 LSTKLKQME---DEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEE 1403
Cdd:pfam05483 410 LKKILAEDEkllDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIE 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1404 KVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKfdqLLAEEKTISAKYAEERDRAEAEAREKETKALSLAR 1483
Cdd:pfam05483 490 LTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEER---MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKC 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1484 ALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQ 1563
Cdd:pfam05483 567 KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELA 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1564 AMKAQFERDLQGRDEQSEEKK---KQLVRQVREMEAELEDERK-QRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQ 1639
Cdd:pfam05483 647 SAKQKFEEIIDNYQKEIEDKKiseEKLLEEVEKAKAIADEAVKlQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSE 726
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1640 LrklqAQMKDCMRELDDTRASREEILAQAKENEKKLKSmeaemiQLQEELAAAERAKRQAQQERDELADE 1709
Cdd:pfam05483 727 L----GLYKNKEQEQSSAKAALEIELSNIKAELLSLKK------QLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
847-1412 |
6.46e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 77.39 E-value: 6.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 847 LLAKEAELTKVREKHLAAenRLTEMETMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEArvee 926
Cdd:PRK02224 189 LDQLKAQIEEKEEKDLHE--RLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIED---- 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 927 eeercqyLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTT 1006
Cdd:PRK02224 263 -------LRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1007 NLMEEEEKSKSLAKlknkheaMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQ 1086
Cdd:PRK02224 336 AAQAHNEEAESLRE-------DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLG 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1087 AALARVEEEAAQKNMALKKIRELETQISELQEDLESERACRNK----------AEKQKRDLGEELEALKTELEDTLDSTA 1156
Cdd:PRK02224 409 NAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1157 AQQELRSKREQEVSILKKTledeakthEAQIQEMRQKHSQAVEELAEQLEqtkRVKATLEKAkQTLENERGELanevkal 1236
Cdd:PRK02224 489 EEVEEVEERLERAEDLVEA--------EDRIERLEERREDLEELIAERRE---TIEEKRERA-EELRERAAEL------- 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1237 lqgkgDSEHKRKKVEAQLQElqvkfSEGERVRTELADKVSKLQVELDSVTGL--LNQSDSKSSKLTKDFSALESQLQDTQ 1314
Cdd:PRK02224 550 -----EAEAEEKREAAAEAE-----EEAEEAREEVAELNSKLAELKERIESLerIRTLLAAIADAEDEIERLREKREALA 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1315 ElLQEENRQKLS-LSTKLKQMEDEKN-----SFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKmedgVGCLETAEEAKR 1388
Cdd:PRK02224 620 E-LNDERRERLAeKRERKRELEAEFDearieEAREDKERAEEYLEQVEEKLDELREERDDLQAE----IGAVENELEELE 694
|
570 580
....*....|....*....|....
gi 806638593 1389 RLQKDLEGLSQRLEEKVAAYDKLE 1412
Cdd:PRK02224 695 ELRERREALENRVEALEALYDEAE 718
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
913-1668 |
9.71e-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: 77.08 E-value: 9.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 913 LEEICHDLEARVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKL----------------QLEKVTTEAKLKK- 975
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMadirrresqsqedlrnQLQNTVHELEAAKc 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 976 LEEDqiIMEDQNCKLAKEKKLL---EDRVAEFTTNLMEEEEKS-------------------KSLAKLKNKHEAMITDLE 1033
Cdd:pfam15921 160 LKED--MLEDSNTQIEQLRKMMlshEGVLQEIRSILVDFEEASgkkiyehdsmstmhfrslgSAISKILRELDTEISYLK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1034 ERLRREEKQRQELE-KTRRKLEGDSTDLSDQIAELQAQ-------IAELKMQLAKKEEELQAALARVEEEAAQKN-MALK 1104
Cdd:pfam15921 238 GRIFPVEDQLEALKsESQNKIELLLQQHQDRIEQLISEheveitgLTEKASSARSQANSIQSQLEIIQEQARNQNsMYMR 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1105 KIRELETQISELQEDL-ESERACRNKAEKQKRDL---GEELEALKTE----------LEDTLDSTAA-----QQELRSKR 1165
Cdd:pfam15921 318 QLSDLESTVSQLRSELrEAKRMYEDKIEELEKQLvlaNSELTEARTErdqfsqesgnLDDQLQKLLAdlhkrEKELSLEK 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1166 EQE-------------VSILKKTLED------------EAKTHEAQIQEMRQKHS--------QAVEELAEQLEQTKRV- 1211
Cdd:pfam15921 398 EQNkrlwdrdtgnsitIDHLRRELDDrnmevqrleallKAMKSECQGQMERQMAAiqgkneslEKVSSLTAQLESTKEMl 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1212 ----------KATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRteladkvsKLQVE 1281
Cdd:pfam15921 478 rkvveeltakKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR--------NVQTE 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1282 LDSVTGLLNQSDsksskltKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIAT 1361
Cdd:pfam15921 550 CEALKLQMAEKD-------KVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRE 622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1362 LHAQVTDM---------------------KKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVaayDKLEKTKTRLQQ 1420
Cdd:pfam15921 623 LEARVSDLelekvklvnagserlravkdiKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKS---EEMETTTNKLKM 699
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1421 ELDDLLVDLDHQRQSVSNLEKKQKKFDQL-LAEEKTISAKyaeerdRAEAEARekETKALSLARALEEAMEQKAELERLN 1499
Cdd:pfam15921 700 QLKSAQSELEQTRNTLKSMEGSDGHAMKVaMGMQKQITAK------RGQIDAL--QSKIQFLEEAMTNANKEKHFLKEEK 771
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1500 KQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERD---LQGR 1576
Cdd:pfam15921 772 NKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDvkeLQGP 851
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1577 DEQSEEKKKQLVRQVREMEAELEDERKQRSIAmaarkklemdlKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDD 1656
Cdd:pfam15921 852 GYTSNSSMKPRLLQPASFTRTHSNVPSSQSTA-----------SFLSHHSRKTNALKEDPTRDLKQLLQELRSVINEEPT 920
|
890
....*....|..
gi 806638593 1657 TRASREEILAQA 1668
Cdd:pfam15921 921 VQLSKAEDKGRA 932
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1034-1907 |
1.85e-13 |
|
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: 76.53 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1034 ERLRREEKQRQELEKTRRKLegdsTDLSDQIAELQAQIAELKMQLAKKEEELQAA---LARVEEEAAQKnmalKKIRELE 1110
Cdd:COG3096 282 ELSERALELRRELFGARRQL----AEEQYRLVEMARELEELSARESDLEQDYQAAsdhLNLVQTALRQQ----EKIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1111 TQISELQEDLESERACRNKAEKQKRDLGEELEA-------LKTELED---TLDS--TAA---QQELRSKRE-QEVSILKK 1174
Cdd:COG3096 354 EDLEELTERLEEQEEVVEEAAEQLAEAEARLEAaeeevdsLKSQLADyqqALDVqqTRAiqyQQAVQALEKaRALCGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1175 TLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQTLEN-----ERGELANEVKALLQGKGDSEH---K 1246
Cdd:COG3096 434 LTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKiagevERSQAWQTARELLRRYRSQQAlaqR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1247 RKKVEAQLQELQVKFSEGERVRTELADkvsklqveldsvtglLNQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLS 1326
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQNAERLLEE---------------FCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVE 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1327 LSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVtdmkkkmedgvGC-LETAEEAKRRLQKDLEglsqRLEEKV 1405
Cdd:COG3096 579 QRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQS-----------GEaLADSQEVTAAMQQLLE----REREAT 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1406 AAYDKLEKTKTRLQQElddllvdldhqrqsVSNLEKKQKKFD-QLLAEEKTISAKYAEE-------RDRAEAEAREKETK 1477
Cdd:COG3096 644 VERDELAARKQALESQ--------------IERLSQPGGAEDpRLLALAERLGGVLLSEiyddvtlEDAPYFSALYGPAR 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1478 ALSLARALEEAMEQKAELERLnkqfrteMEDLM------SSKDDVGKSVHELEK------SKRAL--------------- 1530
Cdd:COG3096 710 HAIVVPDLSAVKEQLAGLEDC-------PEDLYliegdpDSFDDSVFDAEELEDavvvklSDRQWrysrfpevplfgraa 782
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1531 -EQQVEEMKTQLEELEDELqatedAKLRLEVN-LQAMKAQFERDLQGR-----DEQSEEKKKQLVRQVREMEAELED--- 1600
Cdd:COG3096 783 rEKRLEELRAERDELAEQY-----AKASFDVQkLQRLHQAFSQFVGGHlavafAPDPEAELAALRQRRSELERELAQhra 857
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1601 -ERKQRSIAMAARKKLEMdLKDLEAHI-----DTANKNREEAIKQLRKLQaQMKDCMRELDDTRASREEILAQakenekk 1674
Cdd:COG3096 858 qEQQLRQQLDQLKEQLQL-LNKLLPQAnlladETLADRLEELREELDAAQ-EAQAFIQQHGKALAQLEPLVAV------- 928
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1675 LKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSgkgALALEEKRRLEAriaqleeeleeeqGNTELiNDRLKK 1754
Cdd:COG3096 929 LQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRP---HFSYEDAVGLLG-------------ENSDL-NEKLRA 991
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1755 anlqidqintdlNLERSHAQKNEnARQQLERQNKELKAKLQEMESAvKSKYKAS---IAALEAKIAQLEEQLDNETKERQ 1831
Cdd:COG3096 992 ------------RLEQAEEARRE-AREQLRQAQAQYSQYNQVLASL-KSSRDAKqqtLQELEQELEELGVQADAEAEERA 1057
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 806638593 1832 AASKQVRRAEkklkdvlLQVEDERRNaeqfkdqadkastrlkQLKRQLEEAEEEAQRANASRRKLQRELEDATETA 1907
Cdd:COG3096 1058 RIRRDELHEE-------LSQNRSRRS----------------QLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQV 1110
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1450-1923 |
8.74e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.92 E-value: 8.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1450 LAEEKTISAKYAEERDRAEA----------EAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKS 1519
Cdd:PRK02224 215 LAELDEEIERYEEQREQAREtrdeadevleEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1520 VHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERdLQGRDEQSEEKKKQLVRQVREMEAELE 1599
Cdd:PRK02224 295 RDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAES-LREDADDLEERAEELREEAAELESELE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1600 DERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSME 1679
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGK 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1680 A-EMIQLQEELAAAERAKrQAQQERDELADEIANssgkgalALEEKRRLEARIAQLEEELEEEQGnTELINDRLKKANLQ 1758
Cdd:PRK02224 454 CpECGQPVEGSPHVETIE-EDRERVEELEAELED-------LEEEVEEVEERLERAEDLVEAEDR-IERLEERREDLEEL 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1759 IDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSKYKAsIAALEAKIAQLEEQLDNETK------ERQA 1832
Cdd:PRK02224 525 IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE-VAELNSKLAELKERIESLERirtllaAIAD 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1833 ASKQVRRAEKKLKDvLLQVEDERRnaeqfkDQADKASTRLKQLKRQ-----LEEAEEEAQRANASRRKLQRELEDATETA 1907
Cdd:PRK02224 604 AEDEIERLREKREA-LAELNDERR------ERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREER 676
|
490
....*....|....*.
gi 806638593 1908 DAMNREVSSLKNKLRR 1923
Cdd:PRK02224 677 DDLQAEIGAVENELEE 692
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1042-1298 |
1.49e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 71.72 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1042 QRQELEKTRRKLEgdstDLSDQIAELQAQIAELKmqlaKKEEELQAALARVEEEAAQKNmalKKIRELETQISELQEDLe 1121
Cdd:COG4942 18 QADAAAEAEAELE----QLQQEIAELEKELAALK----KEEKALLKQLAALERRIAALA---RRIRALEQELAALEAEL- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1122 seracrNKAEKQKRDLGEELEALKTELEDTLDstAAQQelRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEEL 1201
Cdd:COG4942 86 ------AELEKEIAELRAELEAQKEELAELLR--ALYR--LGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1202 AEQLEQTKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVSKLQVE 1281
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
250
....*....|....*..
gi 806638593 1282 LDSVTGLLNQSDSKSSK 1298
Cdd:COG4942 236 AAAAAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1436-1924 |
1.60e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.49 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1436 VSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLmsskdD 1515
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----E 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1516 VGKSVHELEKSKRALEQQVEEMKTQLEELED---ELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVR 1592
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERLEELEErleELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1593 EMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNRE-EAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKEN 1671
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1672 -------EKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQgN 1744
Cdd:COG4717 283 lgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE-E 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1745 TELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSKYKA-SIAALEAKIAQLEEQL 1823
Cdd:COG4717 362 ELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAlDEEELEEELEELEEEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1824 DNETKERQAASKQVRRAEKKLKdvllQVEDERRnaeqfkdqADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDA 1903
Cdd:COG4717 442 EELEEELEELREELAELEAELE----QLEEDGE--------LAELLQELEELKAELRELAEEWAALKLALELLEEAREEY 509
|
490 500
....*....|....*....|..
gi 806638593 1904 TET-ADAMNREVSSLKNKLRRG 1924
Cdd:COG4717 510 REErLPPVLERASEYFSRLTDG 531
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1477-1933 |
1.81e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.03 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1477 KALSL-ARALeeAMEQkaeLERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRAlEQQVEEMKTQ---LEELEDELQATE 1552
Cdd:COG4913 192 KALRLlHKTQ--SFKP---IGDLDDFVREYMLEEPDTFEAADALVEHFDDLERA-HEALEDAREQielLEPIRELAERYA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1553 DAKLRLEVnLQAMKAQFerdlqgRDEQSEEKKKQLVRQVREMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKN 1632
Cdd:COG4913 266 AARERLAE-LEYLRAAL------RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1633 REEAIK-QLRKLQAQMKDCMRELDDTRA-----------SREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQ 1700
Cdd:COG4913 339 RLEQLErEIERLERELEERERRRARLEAllaalglplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1701 QERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEE---------------------------QGNT-------- 1745
Cdd:COG4913 419 RELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAElpfvgelievrpeeerwrgaiervlggFALTllvppehy 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1746 ----ELINDRLKKANLQIDQINTDL-NLERSHAQKNENAR-----------------------------QQLER------ 1785
Cdd:COG4913 499 aaalRWVNRLHLRGRLVYERVRTGLpDPERPRLDPDSLAGkldfkphpfrawleaelgrrfdyvcvdspEELRRhprait 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1786 ------QNKELKAKlqEMESAVKSKY------KASIAALEAKIAQLEEQLD------NETKERQAASKQVRRAEKKLKDV 1847
Cdd:COG4913 579 ragqvkGNGTRHEK--DDRRRIRSRYvlgfdnRAKLAALEAELAELEEELAeaeerlEALEAELDALQERREALQRLAEY 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1848 ------LLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKL 1921
Cdd:COG4913 657 swdeidVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
570
....*....|..
gi 806638593 1922 RRGDMPFVVTRR 1933
Cdd:COG4913 737 EAAEDLARLELR 748
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1066-1796 |
1.85e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 72.75 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1066 ELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERacrNKAEKQKRDLGEELEALK 1145
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNK---DKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1146 TEledtldstaaqQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQaVEELAEQLEQTKRVKATLEKAKQTLENE 1225
Cdd:TIGR04523 114 ND-----------KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE-LEKLNNKYNDLKKQKEELENELNLLEKE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1226 RGELANEVKallqgkgDSEHKRKKVEAQLQELQVKFSEgervRTELADKVSKLQVELDSVTGLLNQSDSKSSKLTKDFSA 1305
Cdd:TIGR04523 182 KLNIQKNID-------KIKNKLLKLELLLSNLKKKIQK----NKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1306 LESQLQDTQELLQEENRQklsLSTKLKQMEDEKNSFReqleeeeeakrNLEKQIATLHAQVTDMKKKMEDGV-----GCL 1380
Cdd:TIGR04523 251 TQTQLNQLKDEQNKIKKQ---LSEKQKELEQNNKKIK-----------ELEKQLNQLKSEISDLNNQKEQDWnkelkSEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1381 ETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEK-KQKKFDQLLAEEKTISAk 1459
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKeNQSYKQEIKNLESQIND- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1460 yaeerdrAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKT 1539
Cdd:TIGR04523 396 -------LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1540 QLEELEDELQATEdaklrlevnlqamkaqferdlqgrdEQSEEKKKQLVRQVREMEaELEDERKQrsiamaarkkLEMDL 1619
Cdd:TIGR04523 469 QLKVLSRSINKIK-------------------------QNLEQKQKELKSKEKELK-KLNEEKKE----------LEEKV 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1620 KDLEAHIDTANKNREEAIKQLRKLQAQMKDCMREL--DDTRASREEILAQAKENEKKLKsmeaemiQLQEELAAAERAKR 1697
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkDDFELKKENLEKEIDEKNKEIE-------ELKQTQKSLKKKQE 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1698 QAQQERDELADEIANSSGKgalaLEEKrrlEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNE 1777
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKE----IEEK---EKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
730
....*....|....*....
gi 806638593 1778 NARQQLERQNKELKAKLQE 1796
Cdd:TIGR04523 659 NKWPEIIKKIKESKTKIDD 677
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1478-1721 |
1.99e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 71.33 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1478 ALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLR 1557
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1558 LEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSIAmAARKKLEMDLKDLEAHIDTANKNREEAI 1637
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLA-PARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1638 KQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKG 1717
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
....
gi 806638593 1718 ALAL 1721
Cdd:COG4942 254 KLPW 257
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1326-1921 |
2.49e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 72.36 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1326 SLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKV 1405
Cdd:TIGR04523 44 TIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1406 AAYDKLEKTK--------------TRLQQELDDLLVDLDHQRQSVSNLEKKQKKF-DQLLAEEKTIsakyaeerDRAEAE 1470
Cdd:TIGR04523 124 VELNKLEKQKkenkknidkflteiKKKEKELEKLNNKYNDLKKQKEELENELNLLeKEKLNIQKNI--------DKIKNK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1471 AREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQ---QVEEMKTQLEELEDE 1547
Cdd:TIGR04523 196 LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQlkdEQNKIKKQLSEKQKE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1548 LQATEDAKLRLEVNLQAMKAQFErDLqgRDEQSEEKKKQLVRQVREMEAELEDERKQRSIAMAARKKLEMDLKDLEAHID 1627
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEIS-DL--NNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1628 TANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELaaaerakRQAQQERDELA 1707
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI-------KKLQQEKELLE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1708 DEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQN 1787
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1788 KELKAKLQEMESAVKSkYKASIAALEAKIAQLEEQLDNetKERQAASKQVRRAEKKLKDVLLQVEDERRNAEQFKDQADK 1867
Cdd:TIGR04523 506 KELEEKVKDLTKKISS-LKEKIEKLESEKKEKESKISD--LEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKK 582
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 806638593 1868 ASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKL 1921
Cdd:TIGR04523 583 KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNI 636
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
991-1852 |
2.57e-12 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 72.68 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 991 AKEKKLLEDRVAEFTTNLMEEEeksKSLAKLKNKHEAMitdleerlRREEkqrQELEKTRRKLEGDSTDLSDQIAELQAq 1070
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSR---RQLAAEQYRLVEM--------AREL---AELNEAESDLEQDYQAASDHLNLVQT- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1071 iaelKMQLAKKEEELQAALARVEEEAAQKNMALKKIREletQISELQEDLESeracrnkAEkqkrdlgEELEALKTELED 1150
Cdd:PRK04863 343 ----ALRQQEKIERYQADLEELEERLEEQNEVVEEADE---QQEENEARAEA-------AE-------EEVDELKSQLAD 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1151 TLDSTAAQQELRSKREQEVSILKKTLE---------DEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQT 1221
Cdd:PRK04863 402 YQQALDVQQTRAIQYQQAVQALERAKQlcglpdltaDNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQL 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1222 L-----ENERGELANEVKALLQgkgdsEHKRKKVEA-QLQELQVKFSEGERvRTELADKVSKLqveLDSVTGLLNQSDSK 1295
Cdd:PRK04863 482 VrkiagEVSRSEAWDVARELLR-----RLREQRHLAeQLQQLRMRLSELEQ-RLRQQQRAERL---LAEFCKRLGKNLDD 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1296 SSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEknsfREQLEEEEEAKRNLEKQIATLHAQVTDMkkkmed 1375
Cdd:PRK04863 553 EDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQAR----IQRLAARAPAWLAAQDALARLREQSGEE------ 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1376 gvgcLETAEEAKRRLQKDLEglsqRLEEKVAAYDKLEKTKTRLQQelddllvdldhQRQSVSNLEKKQKKFDQLLAEE-- 1453
Cdd:PRK04863 623 ----FEDSQDVTEYMQQLLE----RERELTVERDELAARKQALDE-----------EIERLSQPGGSEDPRLNALAERfg 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1454 -KTISAKYA--EERDRAEAEAREKETKALSLARALEEAMEQKAELERLnkqfrteMEDLM------SSKDDVGKSVHELE 1524
Cdd:PRK04863 684 gVLLSEIYDdvSLEDAPYFSALYGPARHAIVVPDLSDAAEQLAGLEDC-------PEDLYliegdpDSFDDSVFSVEELE 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1525 KS----------------------KRALEQQVEEMKTQLEELEDELqatedAKLRLEVN-LQAMKAQFERDLQGR----- 1576
Cdd:PRK04863 757 KAvvvkiadrqwrysrfpevplfgRAAREKRIEQLRAEREELAERY-----ATLSFDVQkLQRLHQAFSRFIGSHlavaf 831
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1577 DEQSEEKKKQLVRQVREMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANK-NREEAIKQLRKLQAQMKDCmreLD 1655
Cdd:PRK04863 832 EADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLlADETLADRVEEIREQLDEA---EE 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1656 DTR--ASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANssgKGALALEEKRRLEAriaq 1733
Cdd:PRK04863 909 AKRfvQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQR---RAHFSYEDAAEMLA---- 981
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1734 leeeleEEQGNTELINDRLKKANLQIDQINTDLNLERS-HAQKNE------NARQQLERQNKELKAKLQEM--------- 1797
Cdd:PRK04863 982 ------KNSDLNEKLRQRLEQAEQERTRAREQLRQAQAqLAQYNQvlaslkSSYDAKRQMLQELKQELQDLgvpadsgae 1055
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*..
gi 806638593 1798 --ESAVKSKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRAEKKLKDVLLQVE 1852
Cdd:PRK04863 1056 erARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVV 1112
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
999-1240 |
2.89e-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: 70.56 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 999 DRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQL 1078
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1079 AKKEEELQAALArveeeAAQKNMALKKIRELETQISELQedLESERACRNKAEKQKRDLGEELEALKTELEDTLDSTAAQ 1158
Cdd:COG4942 100 EAQKEELAELLR-----ALYRLGRQPPLALLLSPEDFLD--AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1159 QELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQTLENERGELANEVKALLQ 1238
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
..
gi 806638593 1239 GK 1240
Cdd:COG4942 253 GK 254
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1686-1937 |
2.94e-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: 70.56 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1686 QEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTD 1765
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1766 LNLERSHAQKNENARQQLERQNKeLKAKLQEMESAVKSKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRAEKKLK 1845
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPP-LALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1846 DVLLQVEDERRNAEQFKDQADKAstrLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKLRRGD 1925
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
250
....*....|..
gi 806638593 1926 MPFVVTRRIVRK 1937
Cdd:COG4942 255 LPWPVSGRVVRR 266
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1041-1888 |
3.56e-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: 71.92 E-value: 3.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1041 KQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDL 1120
Cdd:TIGR00618 124 KKSETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRS 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1121 ESERACRNKAEKQKRDLGEELEALKTELEDtldstaAQQELRSKREQevsilkktledeaKTHEAQIQEMRQKHSQAVEE 1200
Cdd:TIGR00618 204 QLLTLCTPCMPDTYHERKQVLEKELKHLRE------ALQQTQQSHAY-------------LTQKREAQEEQLKKQQLLKQ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1201 LAEQLEQTKRVKATLEKAkqtleNERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRteladkvsklqv 1280
Cdd:TIGR00618 265 LRARIEELRAQEAVLEET-----QERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLL------------ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1281 eldsvtgllnqsdSKSSKLTKDFSALESQLQDTQELLQEENRqklslstkLKQMEDEKNSFREQLEEEEEakrnLEKQIA 1360
Cdd:TIGR00618 328 -------------MKRAAHVKQQSSIEEQRRLLQTLHSQEIH--------IRDAHEVATSIREISCQQHT----LTQHIH 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1361 TLHAQVTDMKKKMEdgVGCLETAEEAKRRLQKDLEGLSQRLEE--KVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSN 1438
Cdd:TIGR00618 383 TLQQQKTTLTQKLQ--SLCKELDILQREQATIDTRTSAFRDLQgqLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIH 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1439 LEKKQKKFDQLLAEEKtisakyaeerDRAEAEAREKETKALSLARALEEAmEQKAELERLNKQFRTEMEDLMSSKDDVGK 1518
Cdd:TIGR00618 461 LQESAQSLKEREQQLQ----------TKEQIHLQETRKKAVVLARLLELQ-EEPCPLCGSCIHPNPARQDIDNPGPLTRR 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1519 ------SVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQgrdeqseekkkQLVRQVR 1592
Cdd:TIGR00618 530 mqrgeqTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQN-----------ITVRLQD 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1593 EMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLrklqaqmkdcmrelddTRASREEILAQAKENE 1672
Cdd:TIGR00618 599 LTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLT----------------ALHALQLTLTQERVRE 662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1673 KKLKSMEAE---MIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELIN 1749
Cdd:TIGR00618 663 HALSIRVLPkelLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALN 742
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1750 DRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAvkskykasIAALEAKIAQLEEQLDNETKE 1829
Cdd:TIGR00618 743 QSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRL--------REEDTHLLKTLEAEIGQEIPS 814
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 806638593 1830 RQAAskqvrraekklkdVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQR 1888
Cdd:TIGR00618 815 DEDI-------------LNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQ 860
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1060-1698 |
4.12e-12 |
|
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: 71.39 E-value: 4.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1060 LSDQIAELQAQIAELKMQLAKKEEELQAALARVE---EEAAQKNMALKKirELETQISELQEdleseracrnkaekQKRD 1136
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLGSSMNSIKtfwSPELKKERALRK--EEAARISVLKE--------------QYRV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1137 LGEELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAvEELAEQLEQTKR----VK 1212
Cdd:pfam10174 65 TQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEH-ERQAKELFLLRKtleeME 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1213 ATLEKAKQTLeNERGELANEVKALLQGKG--------DSEHKRKKVEAQLQ------ELQVKFSEGERVRTELADKVSKL 1278
Cdd:pfam10174 144 LRIETQKQTL-GARDESIKKLLEMLQSKGlpkksgeeDWERTRRIAEAEMQlghlevLLDQKEKENIHLREELHRRNQLQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1279 Q--VELDSVTGLLNQSDSKSSKLTKDFSALESQLQ--DTQELLQEENRQKlslstKLKQMEDEKNSFR------EQLEEE 1348
Cdd:pfam10174 223 PdpAKTKALQTVIEMKDTKISSLERNIRDLEDEVQmlKTNGLLHTEDREE-----EIKQMEVYKSHSKfmknkiDQLKQE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1349 EEAKRN----LEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDD 1424
Cdd:pfam10174 298 LSKKESellaLQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKST 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1425 LLVDLDHQRQSVSNLEKK----QKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLArALEEAMEQKAE-LERLN 1499
Cdd:pfam10174 378 LAGEIRDLKDMLDVKERKinvlQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALT-TLEEALSEKERiIERLK 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1500 KQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQ------ATEDAKLR-LEVNLQAMKAQFERd 1572
Cdd:pfam10174 457 EQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASslassgLKKDSKLKsLEIAVEQKKEECSK- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1573 LQGRD------EQSEEKKKQLVRQVREMEAELEDERKQRSIA-------MAARKKLEMDLKDLEAHIDTANKNREEAIKQ 1639
Cdd:pfam10174 536 LENQLkkahnaEEAVRTNPEINDRIRLLEQEVARYKEESGKAqaeverlLGILREVENEKNDKDKKIAELESLTLRQMKE 615
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 806638593 1640 LRKLQAQMKDCMRELddtRASREEILAQAKENEKKLKSMEAEmIQLQEELAAAERAKRQ 1698
Cdd:pfam10174 616 QNKKVANIKHGQQEM---KKKGAQLLEEARRREDNLADNSQQ-LQLEELMGALEKTRQE 670
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1228-1699 |
4.17e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 71.34 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1228 ELANEVKALLQGKGDsehKRKKVEAQLQELQVKFSEGERVRTELAdkvsKLQVELDSVTGLLNQSDSKSSKLTKDFSALE 1307
Cdd:COG4717 50 RLEKEADELFKPQGR---KPELNLKELKELEEELKEAEEKEEEYA----ELQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1308 SQLQ--DTQELLQEENRQKLSLSTKLKQMEDEknsfREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEdgvgclETAEE 1385
Cdd:COG4717 123 KLLQllPLYQELEALEAELAELPERLEELEER----LEELRELEEELEELEAELAELQEELEELLEQLS------LATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1386 AKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQrqsvsNLEKKQKKFDQLLAEEKTISAKYAEERD 1465
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA-----ALEERLKEARLLLLIAAALLALLGLGGS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1466 RAEAEAREKETKALSLA----------RALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVE 1535
Cdd:COG4717 268 LLSLILTIAGVLFLVLGllallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1536 EMKTQLEELEDELQ--ATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKkQLVRQVREMEAELEDERKQRSIAMAARK 1613
Cdd:COG4717 348 ELQELLREAEELEEelQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEALD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1614 K--LEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCM--RELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEEL 1689
Cdd:COG4717 427 EeeLEEELEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAELRELAEEWAALKLALELLEEAR 506
|
490
....*....|
gi 806638593 1690 AAAERAKRQA 1699
Cdd:COG4717 507 EEYREERLPP 516
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1012-1498 |
7.15e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 7.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1012 EEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALAR 1091
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1092 VEEEAAQKNMAL--KKIRELETQISELQEDLESERACRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEV 1169
Cdd:COG4717 132 QELEALEAELAElpERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1170 SILKKTLEDEAKTHEAQIQEMRQKhsQAVEELAEQLEQTKRVK------ATLEKAKQTLENERGELANEVKALLQ----G 1239
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENE--LEAAALEERLKEARLLLliaaalLALLGLGGSLLSLILTIAGVLFLVLGllalL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1240 KGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVSKLQVELDSVTGLLNQSDSKSSKLTKDFSALESQlqdTQELLQE 1319
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL---EEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1320 ENRQKLSLSTKLKQMEDEKnSFREQLeEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEeakrrLQKDLEGLSQ 1399
Cdd:COG4717 367 ELEQEIAALLAEAGVEDEE-ELRAAL-EQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE-----LEEELEELEE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1400 RLEEKVAAYDKLEKTKTRLQQElddllvdldhqrqsVSNLEKkqkkfDQLLAEektisAKYAEERDRAEAEAREKETKAL 1479
Cdd:COG4717 440 ELEELEEELEELREELAELEAE--------------LEQLEE-----DGELAE-----LLQELEELKAELRELAEEWAAL 495
|
490
....*....|....*....
gi 806638593 1480 SLARALEEAMEQKAELERL 1498
Cdd:COG4717 496 KLALELLEEAREEYREERL 514
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1196-1915 |
1.29e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 70.33 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1196 QAVEELAEQLEQTKRVKATLEKAKQtlenergelanEVKALLQGKGD-SEHKRKKVEAQLQELQVKFSEGERVRTELAdk 1274
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDARE-----------QIELLEPIRELaERYAAARERLAELEYLRAALRLWFAQRRLE-- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1275 vsKLQVELDSVTGLLNQSDSKSSKLTKDFSALESQLQD-TQELLQEENRQKLSLSTKLKQMEDEKNSFREQLeeeeeakR 1353
Cdd:COG4913 292 --LLEAELEELRAELARLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRR-------A 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1354 NLEKQIATLHAQVTDMKkkmedgvgclETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQR 1433
Cdd:COG4913 363 RLEALLAALGLPLPASA----------EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1434 QSVSNLEKKQKKFDQLLAEEKTISAK----YAEERDRAEAEAR-----EKE--TKALSL------ARALEEAMEQKAELE 1496
Cdd:COG4913 433 RRKSNIPARLLALRDALAEALGLDEAelpfVGELIEVRPEEERwrgaiERVlgGFALTLlvppehYAAALRWVNRLHLRG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1497 RLNKQF-RTEMEDLMSSKDDVGKSVHELE----KSKRALEQQVEEMK-----TQLEELEDELQA-TEDAKLRLEvnlqam 1565
Cdd:COG4913 513 RLVYERvRTGLPDPERPRLDPDSLAGKLDfkphPFRAWLEAELGRRFdyvcvDSPEELRRHPRAiTRAGQVKGN------ 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1566 KAQFERDLQGRDEQ-------SEEKKKQLVRQVREMEAELEDerkqrsiamaarkkLEMDLKDLEAHIDTANKnREEAIK 1638
Cdd:COG4913 587 GTRHEKDDRRRIRSryvlgfdNRAKLAALEAELAELEEELAE--------------AEERLEALEAELDALQE-RREALQ 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1639 QLRKLQAQMKDcMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANssgkga 1718
Cdd:COG4913 652 RLAEYSWDEID-VASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ------ 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1719 lALEEKRRLEARIAQLEEELEEEQgnTELINDRLKKANLQidqintdlNLERSHAQKNENARQQLERQNKELKAKLQEME 1798
Cdd:COG4913 725 -AEEELDELQDRLEAAEDLARLEL--RALLEERFAAALGD--------AVERELRENLEERIDALRARLNRAEEELERAM 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1799 SAVKSKYKASIAALEAKIAQLEE------QLDNE---TKERQAASKQVRRAEKKLKDVLLQVEDERRNAEQfkdqadkas 1869
Cdd:COG4913 794 RAFNREWPAETADLDADLESLPEylalldRLEEDglpEYEERFKELLNENSIEFVADLLSKLRRAIREIKE--------- 864
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 806638593 1870 tRLKQLKRQLEEAE---------EEAQRANASRRKLQRELEDATETADAMNREVS 1915
Cdd:COG4913 865 -RIDPLNDSLKRIPfgpgrylrlEARPRPDPEVREFRQELRAVTSGASLFDEELS 918
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1277-1936 |
1.73e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 69.76 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1277 KLQVELDSVTGLLNQSDSKS-SKLTKDFSaleSQLQDTQELLQEEN----RQK-------LSLSTKLKQMEDEKNSFREQ 1344
Cdd:pfam15921 56 KYEVELDSPRKIIAYPGKEHiERVLEEYS---HQVKDLQRRLNESNelheKQKfylrqsvIDLQTKLQEMQMERDAMADI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1345 LEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDD 1424
Cdd:pfam15921 133 RRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMST 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1425 LlvdldHQRQSVSNLEKKQKKFDqllAEEKTISAKYAEERDRAEAEAREKETKalslaraleeameqkaeLERLNKQFRT 1504
Cdd:pfam15921 213 M-----HFRSLGSAISKILRELD---TEISYLKGRIFPVEDQLEALKSESQNK-----------------IELLLQQHQD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1505 EMEDLMSSKDDVGKSVHELEKSKRAleqQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKK 1584
Cdd:pfam15921 268 RIEQLISEHEVEITGLTEKASSARS---QANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1585 KQLVRQVREMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEI 1664
Cdd:pfam15921 345 EELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDR 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1665 LAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSgkgalalEEKRRLEARIAQLEEELEEEQGN 1744
Cdd:pfam15921 425 NMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTK-------EMLRKVVEELTAKKMTLESSERT 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1745 TELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESavkskYKASIAALEAKIAQLEEQLD 1824
Cdd:pfam15921 498 VSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEA-----LKLQMAEKDKVIEILRQQIE 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1825 NETK-----ERQAASKQVRRAEKKLkdvllQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQR-ANASRRKLqR 1898
Cdd:pfam15921 573 NMTQlvgqhGRTAGAMQVEKAQLEK-----EINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKlVNAGSERL-R 646
|
650 660 670
....*....|....*....|....*....|....*...
gi 806638593 1899 ELEDATETADAMNREVSSLKNKLRRGDMPFVVTRRIVR 1936
Cdd:pfam15921 647 AVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFR 684
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1443-1846 |
3.33e-11 |
|
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: 68.00 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1443 QKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHE 1522
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1523 LEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKaqferdlqgrdeqseEKKKQLVRQVREMEAELEDER 1602
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMK---------------ERAKKAGAQRKEEEAERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1603 KQRSIAMAARKKLEMDLKDLEAHIDtankNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEM 1682
Cdd:pfam07888 178 AKLQQTEEELRSLSKEFQELRNSLA----QRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1683 IQLQEELAAAERAKRQAQQERDELADEIANSSGKGA---LALEEKRrleariAQLEEELEEEQGNTELINDRLKKANLQI 1759
Cdd:pfam07888 254 EGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLAdasLALREGR------ARWAQERETLQQSAEADKDRIEKLSAEL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1760 DQINTDLNLERSHAQK-----------NENARQQLERQNKELKAKLQEMESAvKSKYKASIAALEAKIAQLEEQLDNET- 1827
Cdd:pfam07888 328 QRLEERLQEERMEREKlevelgrekdcNRVQLSESRRELQELKASLRVAQKE-KEQLQAEKQELLEYIRQLEQRLETVAd 406
|
410 420
....*....|....*....|
gi 806638593 1828 -KERQAASKQVRRAEKKLKD 1846
Cdd:pfam07888 407 aKWSEAALTSTERPDSPLSD 426
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1031-1205 |
4.02e-11 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 64.95 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1031 DLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMAlKKIRELE 1110
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1111 TqiseLQEDLESERACRNKAEKQKRDLGEELEALKTELEDTldstaaqQELRSKREQEVSILKKTLEDEAKTHEAQIQEM 1190
Cdd:COG1579 93 A----LQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|....*
gi 806638593 1191 RQKHSQAVEELAEQL 1205
Cdd:COG1579 162 EAEREELAAKIPPEL 176
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1304-1898 |
4.25e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.17 E-value: 4.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1304 SALESQLQDTQELLQEENRQKLSLSTKLKQMEDEK---NSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCL 1380
Cdd:PRK03918 196 KEKEKELEEVLREINEISSELPELREELEKLEKEVkelEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1381 ETAEEAKRRLqKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKY 1460
Cdd:PRK03918 276 EELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1461 AEERDRAEAeareketkalslaraLEEAMEQKAELERLNKQFRTEmedlmsSKDDVGKSVHELEKSKRALEQQVEEMKTQ 1540
Cdd:PRK03918 355 EELEERHEL---------------YEEAKAKKEELERLKKRLTGL------TPEKLEKELEELEKAKEEIEEEISKITAR 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1541 LEELEDELQATEDAKLRLEvnlqamKAQFERDLQGRdEQSEEKKKQLVRqvrEMEAELEDERKQRSIAMAARKKLEMDLK 1620
Cdd:PRK03918 414 IGELKKEIKELKKAIEELK------KAKGKCPVCGR-ELTEEHRKELLE---EYTAELKRIEKELKEIEEKERKLRKELR 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1621 DLEAHIdtankNREEAIKQLRKLQAQMKDCMRELDDTRAsrEEILAQAKENEK---KLKSMEAEMIQLQEELAAAERAKr 1697
Cdd:PRK03918 484 ELEKVL-----KKESELIKLKELAEQLKELEEKLKKYNL--EELEKKAEEYEKlkeKLIKLKGEIKSLKKELEKLEELK- 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1698 qaqqerdeladeianssGKGALALEEKRRLEARIAqleeeleeeqgntELINDRLKKANLQIDQINTDLN-LERSHAQKN 1776
Cdd:PRK03918 556 -----------------KKLAELEKKLDELEEELA-------------ELLKELEELGFESVEELEERLKeLEPFYNEYL 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1777 E--NARQQLERQNKELKAKLQEMESAVK--SKYKASIAALEAKIAQLEEQLDNETKERqaASKQVRRAEKKLKDVLLQVE 1852
Cdd:PRK03918 606 ElkDAEKELEREEKELKKLEEELDKAFEelAETEKRLEELRKELEELEKKYSEEEYEE--LREEYLELSRELAGLRAELE 683
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 806638593 1853 DERRNAEQFKDQADKastrLKQLKRQLEEAEEEAQRANASRRKLQR 1898
Cdd:PRK03918 684 ELEKRREEIKKTLEK----LKEELEEREKAKKELEKLEKALERVEE 725
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1273-1852 |
9.28e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 66.97 E-value: 9.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1273 DKVSKLQVELDSVTGLLNQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAK 1352
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1353 RNLEKQIATLHAQVTDMKKKMEDgvgcLETAEEAKRRLQKDLEGLSQRLEEKVAaydKLEKTKTRLQQELDDLLVDLDHQ 1432
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQ----ISELKKQNNQLKDNIEKKQQEINEKTT---EISNTQTQLNQLKDEQNKIKKQL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1433 RQSVSNLEKKQKKFDQLLAEEKTIsakyaeerdRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSS 1512
Cdd:TIGR04523 270 SEKQKELEQNNKKIKELEKQLNQL---------KSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1513 KDDVG---KSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFE------RDLQGRDEQSEEK 1583
Cdd:TIGR04523 341 NEQISqlkKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQnqeklnQQKDEQIKKLQQE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1584 KKQLVRQVREMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREE 1663
Cdd:TIGR04523 421 KELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1664 ILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANssgkgalaleekrrleariaqleeeleeeqg 1743
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK------------------------------- 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1744 ntelINDRLKKANLQIDQINTDLNLERSHAQKNEnarqqLERQNKELKAKLQEMESAVKsKYKASIAALEAKIAQLEEQL 1823
Cdd:TIGR04523 550 ----DDFELKKENLEKEIDEKNKEIEELKQTQKS-----LKKKQEEKQELIDQKEKEKK-DLIKEIEEKEKKISSLEKEL 619
|
570 580
....*....|....*....|....*....
gi 806638593 1824 DNETKERQAASKQVRRAEKKLKDVLLQVE 1852
Cdd:TIGR04523 620 EKAKKENEKLSSIIKNIKSKKNKLKQEVK 648
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
794-1589 |
1.16e-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: 67.07 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 794 LARKAFAKRQQQ---LTAMKVLQRNCaaylRLRNWQWWRLFTKVKPLLNSIRHE--DELLAKEAELTKVREKHLAAENRL 868
Cdd:pfam15921 283 LTEKASSARSQAnsiQSQLEIIQEQA----RNQNSMYMRQLSDLESTVSQLRSElrEAKRMYEDKIEELEKQLVLANSEL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 869 TEMETMQSQLMAEKLQLQEQLQA--------ETELCAEAEE---LRARLTAKKQELEEICHDLEARVEEEEERCQYLQAE 937
Cdd:pfam15921 359 TEARTERDQFSQESGNLDDQLQKlladlhkrEKELSLEKEQnkrLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAM 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 938 KKKMQQNIQELEEQLEEEESARQKL-----QLE-------KVTTEAKLKK--LEEDQIIMEDQNCKLAKEKKLLEDRVAE 1003
Cdd:pfam15921 439 KSECQGQMERQMAAIQGKNESLEKVssltaQLEstkemlrKVVEELTAKKmtLESSERTVSDLTASLQEKERAIEATNAE 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1004 FTTNLMEEEEKSKSLAKLKNKHEAMITDLEE----RLRREEKQRQeLEKTRRKLEgDSTDLSDQIAELQAQIAELKMQLa 1079
Cdd:pfam15921 519 ITKLRSRVDLKLQELQHLKNEGDHLRNVQTEcealKLQMAEKDKV-IEILRQQIE-NMTQLVGQHGRTAGAMQVEKAQL- 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1080 kkEEELQAALARVEEEAAQKNMALKKIRELETQISELQedLESERACRNKAEKQK--RDLGEELEALKTELEDTldstaa 1157
Cdd:pfam15921 596 --EKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE--LEKVKLVNAGSERLRavKDIKQERDQLLNEVKTS------ 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1158 QQELRSKREqEVSILKKTLEDEAKTHEAQIQEMRQkhsqaveelaeqleQTKRVKATLEKAKQTLENERGELANEVKALL 1237
Cdd:pfam15921 666 RNELNSLSE-DYEVLKRNFRNKSEEMETTTNKLKM--------------QLKSAQSELEQTRNTLKSMEGSDGHAMKVAM 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1238 QGKGDSEHKRKKVEA---QLQELQVKFSEGERVRTELADKVSKLQVELDSV-------TGLLNQSDSKSSKLTKDFSALE 1307
Cdd:pfam15921 731 GMQKQITAKRGQIDAlqsKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVateknkmAGELEVLRSQERRLKEKVANME 810
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1308 S-------QLQDTQELLQEENRQKLSLstKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATL--HAQVTDMKKKMEDGVG 1378
Cdd:pfam15921 811 ValdkaslQFAECQDIIQRQEQESVRL--KLQHTLDVKELQGPGYTSNSSMKPRLLQPASFTrtHSNVPSSQSTASFLSH 888
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1379 CLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKK----QKKFDQLLAEEK 1454
Cdd:pfam15921 889 HSRKTNALKEDPTRDLKQLLQELRSVINEEPTVQLSKAEDKGRAPSLGALDDRVRDCIIESSLRsdicHSSSNSLQTEGS 968
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1455 TISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSS--KDDVG--------KSVHELE 1524
Cdd:pfam15921 969 KSSETCSREPVLLHAGELEDPSSCFTFPSTASPSVKNSASRSFHSSPKKSPVHSLLTSsaEGSIGsssqyrsaKTIHSPD 1048
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 806638593 1525 KSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFeRDLQGRDEQSEEKKKQLVR 1589
Cdd:pfam15921 1049 SVKDSQSLPIETTGKTCRKLQNRLESLQTLVEDLQLKNQAMSSMI-RNQEKRIQKVKDQEKMLLK 1112
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1270-1913 |
1.63e-10 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 66.79 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1270 ELADKVSKLQVELDSVTGLLNQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSfreQLEEEE 1349
Cdd:pfam12128 238 KIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNG---ELSAAD 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1350 EAKRNLEKQIATLHAQvtdMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQ---ELDDLL 1426
Cdd:pfam12128 315 AAVAKDRSELEALEDQ---HGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSkikEQNNRD 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1427 VDLDHQRQSVSnlekKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEA--------------MEQK 1492
Cdd:pfam12128 392 IAGIKDKLAKI----REARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELklrlnqatatpellLQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1493 AELERLNK------QFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQA---TEDAKLRLEVNL- 1562
Cdd:pfam12128 468 NFDERIERareeqeAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPqagTLLHFLRKEAPDw 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1563 -QAMKAQFERDLQGR-DEQSEEKKKQLVRQVREMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQL 1640
Cdd:pfam12128 548 eQSIGKVISPELLHRtDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQL 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1641 RKLQAQMKDCMRELDDTRASreeiLAQAKENEKKLKS-MEAEMIQLQEelaAAERAKRQAQQERDELADEIANSSGKGAL 1719
Cdd:pfam12128 628 VQANGELEKASREETFARTA----LKNARLDLRRLFDeKQSEKDKKNK---ALAERKDSANERLNSLEAQLKQLDKKHQA 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1720 ALEEKRR--LEARIAQLEEELeeeqgntELINDRlkkaNLQIDQINTDLNLERSHAQKNENArqqLERQNK-ELKAKlqE 1796
Cdd:pfam12128 701 WLEEQKEqkREARTEKQAYWQ-------VVEGAL----DAQLALLKAAIAARRSGAKAELKA---LETWYKrDLASL--G 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1797 MESAVKSKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRAEKKLKDVLLQVEDERRNAE-QFKDQADKASTRLKQL 1875
Cdd:pfam12128 765 VDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQqQLARLIADTKLRRAKL 844
|
650 660 670
....*....|....*....|....*....|....*...
gi 806638593 1876 KRQLEEAEEEAQRANASRRKLQRELEDATETADAMNRE 1913
Cdd:pfam12128 845 EMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSE 882
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1535-1923 |
2.02e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1535 EEMKTQLEELEDELQATEDAKLRLEVN-LQAMKAQFERDLqgrdEQSEEKKKQLVRQVREMEAELEDERKQRsiamAARK 1613
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEKEEKDLHERLNgLESELAELDEEI----ERYEEQREQARETRDEADEVLEEHEERR----EELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1614 KLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAE 1693
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECR 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1694 RAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHA 1773
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1774 QKNENARQQLERQNKELKAKLQEMESAVK---------------------------SKYKASIAALEAKIAQLEEQLD-- 1824
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVEeaealleagkcpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEev 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1825 ----NETKERQAASKQVRRAEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQranasrrKLQREL 1900
Cdd:PRK02224 495 eerlERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAA-------EAEEEA 567
|
410 420
....*....|....*....|...
gi 806638593 1901 EDATETADAMNREVSSLKNKLRR 1923
Cdd:PRK02224 568 EEAREEVAELNSKLAELKERIES 590
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
842-1296 |
2.28e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.83 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 842 RHE---DELLAKEAELTKVREKHLAAEnrlTEMETMQSQLMAEKLQLQEQLQAETELCAEAEELRA---RLTAKKQELEE 915
Cdd:PRK02224 245 EHEerrEELETLEAEIEDLRETIAETE---REREELAEEVRDLRERLEELEEERDDLLAEAGLDDAdaeAVEARREELED 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 916 ICHDLEARVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQ--------- 986
Cdd:PRK02224 322 RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEieelrerfg 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 987 ------------NCKLAKEKKLLEDRVAEFTTNLM-----------------------------------EEEEKSKSLA 1019
Cdd:PRK02224 402 dapvdlgnaedfLEELREERDELREREAELEATLRtarerveeaealleagkcpecgqpvegsphvetieEDRERVEELE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1020 KLKNKHEAMITDLEERLRREEkQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQA--ALARVEEEAA 1097
Cdd:PRK02224 482 AELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAEleAEAEEKREAA 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1098 QKNM-----ALKKIRELETQISELQEDLESERACRNKAEKQKrDLGEELEALKTELEDtldsTAAQQELRSKREQEVSIL 1172
Cdd:PRK02224 561 AEAEeeaeeAREEVAELNSKLAELKERIESLERIRTLLAAIA-DAEDEIERLREKREA----LAELNDERRERLAEKRER 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1173 KKTLEDEAKthEAQIQEMRQKHSQAVEELAEQLEQTKRvkatLEKAKQTLENERGELANEVKALLQGKgdseHKRKKVEA 1252
Cdd:PRK02224 636 KRELEAEFD--EARIEEAREDKERAEEYLEQVEEKLDE----LREERDDLQAEIGAVENELEELEELR----ERREALEN 705
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 806638593 1253 QLQELQVKFSEGE-------RVRTEL-ADKVSKLQVELDSVTGLLNQSDSKS 1296
Cdd:PRK02224 706 RVEALEALYDEAEelesmygDLRAELrQRNVETLERMLNETFDLVYQNDAYS 757
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
851-1508 |
5.30e-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: 64.74 E-value: 5.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 851 EAELTKVREKHLAAENRLTEMETMQSQLMAEKLQLQEQLQAETElcaEAEELRARLTAKKQELEEICHDLEARVEEEEER 930
Cdd:pfam05483 193 EKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEIN---DKEKQVSLLLIQITEKENKMKDLTFLLEESRDK 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 931 CQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKlledrvaefttNLME 1010
Cdd:pfam05483 270 ANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKE-----------AQME 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1011 EEEKSKSLAKL-KNKHEAMITDLEERLRREEkqrQELEKTrrklegdstdlsdqiaelQAQIAELKMQLAKKEEELqaal 1089
Cdd:pfam05483 339 ELNKAKAAHSFvVTEFEATTCSLEELLRTEQ---QRLEKN------------------EDQLKIITMELQKKSSEL---- 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1090 arvEEEAAQKNMALKKIRELETQISELQEDLESeracrnkaEKQKRDLGEELEAlkteledtldstaaqqelrskREQEV 1169
Cdd:pfam05483 394 ---EEMTKFKNNKEVELEELKKILAEDEKLLDE--------KKQFEKIAEELKG---------------------KEQEL 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1170 SILKKTLEDEAKTHEAQIQEMR---QKHSQAVEELAEQL--EQTKRVKATLEKAKQTLENER--GELANEVKALLQGKGD 1242
Cdd:pfam05483 442 IFLLQAREKEIHDLEIQLTAIKtseEHYLKEVEDLKTELekEKLKNIELTAHCDKLLLENKEltQEASDMTLELKKHQED 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1243 SEHKRKKVEAQLQELQVKFSEGERVRTELADKVSKLQVELDSVTGLLNQSDSKSSKLTKDFSALESQLQDTQELLQEENR 1322
Cdd:pfam05483 522 IINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKK 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1323 QKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLE 1402
Cdd:pfam05483 602 QIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAK 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1403 EKVAAYDKLEKTKTRLQQELDDllvdldhqrQSVSNLEKKQKKFDQLLaeektisakyaEERDRAEAEAREKETKALSLA 1482
Cdd:pfam05483 682 AIADEAVKLQKEIDKRCQHKIA---------EMVALMEKHKHQYDKII-----------EERDSELGLYKNKEQEQSSAK 741
|
650 660
....*....|....*....|....*..
gi 806638593 1483 RALE-EAMEQKAELERLNKQFRTEMED 1508
Cdd:pfam05483 742 AALEiELSNIKAELLSLKKQLEIEKEE 768
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1392-1822 |
6.34e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.40 E-value: 6.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1392 KDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDqLLAEEKTISAKYAEERDRAEA-E 1470
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP-LYQELEALEAELAELPERLEElE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1471 AREKETKAL--SLARALEEAMEQKAELERLNKQF----RTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEEL 1544
Cdd:COG4717 153 ERLEELRELeeELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1545 EDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQ------------------LVRQVREMEAELEDERKQRS 1606
Cdd:COG4717 233 ENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllallfllLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1607 IAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCmreldDTRASREEILAQAKENEKKLKSMEAEMIQLQ 1686
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA-----EELEEELQLEELEQEIAALLAEAGVEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1687 EELAAAERAKRQAQQERDELADEIANSSG--KGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINT 1764
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELLGelEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 806638593 1765 DLNLERshaqknenARQQLERQNKELKAKLQEmesavKSKYKASIAALEAKIAQLEEQ 1822
Cdd:COG4717 468 DGELAE--------LLQELEELKAELRELAEE-----WAALKLALELLEEAREEYREE 512
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
27-72 |
6.75e-10 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 55.90 E-value: 6.75e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 806638593 27 AAKKLVWVPSTKNGFEPASLKEEVGEEAIVELvENGKKVKVNKDDI 72
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1305-1557 |
7.25e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.24 E-value: 7.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1305 ALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLeeeeeakRNLEKQIATLHAQVTDMKKKMEDGVGCLETAE 1384
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL-------AALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1385 EAKRRLQKDLEGLSQRLEEKVAAydklektktrLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEER 1464
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRA----------LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1465 DRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEEL 1544
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
250
....*....|...
gi 806638593 1545 EDELQATEDAKLR 1557
Cdd:COG4942 240 AERTPAAGFAALK 252
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
843-1370 |
9.78e-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: 63.97 E-value: 9.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 843 HEDELLAKEAELTKVREKHLAAENRLTEMETMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTakkQELEEICHDLEA 922
Cdd:pfam05483 231 YKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLT---KELEDIKMSLQR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 923 RVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEdqiIMEDQNCKLAKEkkllEDRVA 1002
Cdd:pfam05483 308 SMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE---LLRTEQQRLEKN----EDQLK 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1003 EFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEK---QRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQL- 1078
Cdd:pfam05483 381 IITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKlldEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLt 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1079 ---------AKKEEELQAALARVE----EEAAQKNMALKKIRELETQISELQEDLESERACRNKAEKQKRDLGEELEALK 1145
Cdd:pfam05483 461 aiktseehyLKEVEDLKTELEKEKlkniELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1146 ---TELEDTLDSTaaQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKH----------------SQAVEELAEQLE 1206
Cdd:pfam05483 541 ekeMNLRDELESV--REEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKilenkcnnlkkqienkNKNIEELHQENK 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1207 QTKRVKATLEKAKQTLENERGELANEVKALLQGKGD-SEHKRKKVEAQLQELQVKFSEGERVRTeLADKVSKLQVELD-- 1283
Cdd:pfam05483 619 ALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEiIDNYQKEIEDKKISEEKLLEEVEKAKA-IADEAVKLQKEIDkr 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1284 ---SVTGLLNQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIA 1360
Cdd:pfam05483 698 cqhKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
570
....*....|
gi 806638593 1361 TLHAQVTDMK 1370
Cdd:pfam05483 778 ENTAILKDKK 787
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1470-1917 |
1.68e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1470 EAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQ 1549
Cdd:PRK03918 145 ESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1550 ATEDAKLRLE--VNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSIAMAARKKLEMDLKdLEAHID 1627
Cdd:PRK03918 225 KLEKEVKELEelKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK-LSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1628 TANKNREEAIKQLRKLQAQMKDCMRELDDtrasREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKrQAQQERDELA 1707
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKE----LEEKEERLEELKKKLKELEKRLEELEERHELYEEAK-AKKEELERLK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1708 DEIANssgkgalalEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQN 1787
Cdd:PRK03918 379 KRLTG---------LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEH 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1788 K-----ELKAKLQEMESAVKsKYKASIAALEAKIAQLEEQLDNE---TKERQAAsKQVRRAEKKLKDVLLQ-VEDERRNA 1858
Cdd:PRK03918 450 RkelleEYTAELKRIEKELK-EIEEKERKLRKELRELEKVLKKEselIKLKELA-EQLKELEEKLKKYNLEeLEKKAEEY 527
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 806638593 1859 EQFKDQADKASTRLKQLKRQLEEAEEEAQRanasRRKLQRELEDATETADAMNREVSSL 1917
Cdd:PRK03918 528 EKLKEKLIKLKGEIKSLKKELEKLEELKKK----LAELEKKLDELEEELAELLKELEEL 582
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
870-1468 |
1.79e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.01 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 870 EMETMQSQLMA-EKL-QLQEQLQAETELCAEAEELRARLTAKKQELEEicHDLEARVEEEEERCQYLQAEKKKMQQNIQE 947
Cdd:COG4913 243 ALEDAREQIELlEPIrELAERYAAARERLAELEYLRAALRLWFAQRRL--ELLEAELEELRAELARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 948 LEEQLEEEESARQKLQLEKVTT-EAKLKKLEEDQiimedqncklaKEKKLLEDRVAEFTTNL-MEEEEKSKSLAKLKNKH 1025
Cdd:COG4913 321 LREELDELEAQIRGNGGDRLEQlEREIERLEREL-----------EERERRRARLEALLAALgLPLPASAEEFAALRAEA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1026 EAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELkmqlakkEEELQAALARVEEEAAQKNMALKK 1105
Cdd:COG4913 390 AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNI-------PARLLALRDALAEALGLDEAELPF 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1106 IRELeTQISELQEDLES--ERACRNKA------EKQKRDLGEELEALKTELE-DTLDSTAAQQELRSKREQEVSILKKTl 1176
Cdd:COG4913 463 VGEL-IEVRPEEERWRGaiERVLGGFAltllvpPEHYAAALRWVNRLHLRGRlVYERVRTGLPDPERPRLDPDSLAGKL- 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1177 edEAKTHEAQ---IQEMRQKHSQAVEELAEQLE----------QTKRVKATLEK------------------AKQTLENE 1225
Cdd:COG4913 541 --DFKPHPFRawlEAELGRRFDYVCVDSPEELRrhpraitragQVKGNGTRHEKddrrrirsryvlgfdnraKLAALEAE 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1226 RGELANEVKALLQGKGDSEHKRKKVEAQLQELQ--VKFSEGERVRTELADKVSKLQVELDSvtglLNQSDSksskltkDF 1303
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELER----LDASSD-------DL 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1304 SALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDmkkKMEDGVGCLETA 1383
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE---ERFAAALGDAVE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1384 EEAKRRLQKDLEGLSQRLEEkvaAYDKLEKTKTRLQQELDDLLV------------DLDHQRQSVSNLEKKQKKFDQLLA 1451
Cdd:COG4913 765 RELRENLEERIDALRARLNR---AEEELERAMRAFNREWPAETAdldadleslpeyLALLDRLEEDGLPEYEERFKELLN 841
|
650 660
....*....|....*....|..
gi 806638593 1452 EEKT-----ISAKYAEERDRAE 1468
Cdd:COG4913 842 ENSIefvadLLSKLRRAIREIK 863
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
838-1122 |
2.31e-09 |
|
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: 62.45 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 838 LNSIRHEDellaKEAELTKVREKHLAAE-NRLTEMETMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEI 916
Cdd:pfam17380 350 LERIRQEE----RKRELERIRQEEIAMEiSRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 917 CHDLEarvEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNcklakeKKL 996
Cdd:pfam17380 426 RAEQE---EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQR------RKI 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 997 LEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELE-KTRRKLEGDSTDLSDQIAELQAQIAELK 1075
Cdd:pfam17380 497 LEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEmEERRRIQEQMRKATEERSRLEAMERERE 576
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 806638593 1076 MQLAKKEEELQaalaRVEEEAAQKNMALKKIreLETQISELQ-EDLES 1122
Cdd:pfam17380 577 MMRQIVESEKA----RAEYEATTPITTIKPI--YRPRISEYQpPDVES 618
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1178-1410 |
2.37e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1178 DEAKTHEAQIQEMRQKhsqaVEELAEQLEQTKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQEL 1257
Cdd:COG4942 20 DAAAEAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1258 QVKFsegERVRTELADKVSKLQV--ELDSVTGLLNQSDSksSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQME 1335
Cdd:COG4942 96 RAEL---EAQKEELAELLRALYRlgRQPPLALLLSPEDF--LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 806638593 1336 DEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDgvgcLETAEEAKRRLQKDLEGLSQRLEEKVAAYDK 1410
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAE----LAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
965-1260 |
5.36e-09 |
|
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: 61.29 E-value: 5.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 965 EKVTTEAKLKKLEED----QIIMEDQNCKLAKEKKLLEDRVAEFttNLMEEEEKSKSLAKLKNKHEAM----ITDLE--- 1033
Cdd:pfam17380 307 EKAREVERRRKLEEAekarQAEMDRQAAIYAEQERMAMEREREL--ERIRQEERKRELERIRQEEIAMeisrMRELErlq 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1034 -ERLRREEKQRQELEKTRRKlegdSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKnmaLKKIRELET- 1111
Cdd:pfam17380 385 mERQQKNERVRQELEAARKV----KILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERARE---MERVRLEEQe 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1112 ---QISELQEDLESERACRNKAEKQKRD--LGEEL--EALKTELEDTLDSTAAQQELRSKREQEVSILKKTLEDEAKTHE 1184
Cdd:pfam17380 458 rqqQVERLRQQEEERKRKKLELEKEKRDrkRAEEQrrKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRRE 537
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 806638593 1185 AQIQEMRQKhsqaveelaeQLEQTKRVKATLEKAkqTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVK 1260
Cdd:pfam17380 538 AEEERRKQQ----------EMEERRRIQEQMRKA--TEERSRLEAMEREREMMRQIVESEKARAEYEATTPITTIK 601
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1062-1265 |
6.00e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.23 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1062 DQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERAcrnKAEKQKRDLGEEL 1141
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA---EIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1142 EALKTE------LEDTLDSTAAQQELRSkreqeVSILKKTLEDEAKTHEaQIQEMRQKHSQAVEELAEQLEQTKRVKATL 1215
Cdd:COG3883 93 RALYRSggsvsyLDVLLGSESFSDFLDR-----LSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 806638593 1216 EKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGE 1265
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1051-1253 |
6.16e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.23 E-value: 6.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1051 RKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESeracRNKA 1130
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE----RARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1131 EKQKRDLGEELEALK--TELEDTLDSTAAQQELRSKREQEVSILKKtLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQT 1208
Cdd:COG3883 95 LYRSGGSVSYLDVLLgsESFSDFLDRLSALSKIADADADLLEELKA-DKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 806638593 1209 KRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQ 1253
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
826-1640 |
8.09e-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: 61.14 E-value: 8.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 826 QWWRLFTKVKPLLNSIRHEDELLAKEAELTK--VREKHLAAENRLTEMETMQSQLMAEKLQLQE---QLQAETELCAEae 900
Cdd:TIGR00618 177 QYTQLALMEFAKKKSLHGKAELLTLRSQLLTlcTPCMPDTYHERKQVLEKELKHLREALQQTQQshaYLTQKREAQEE-- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 901 elrarltakKQELEEICHDLEARVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQ 980
Cdd:TIGR00618 255 ---------QLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 981 IIMEDQNckLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEamITDLEERLRREEKQRQELEKTRRKLEGDSTDL 1060
Cdd:TIGR00618 326 LLMKRAA--HVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIRE--ISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1061 SDQIAELQAQIAELkmQLAKKEEELQAALARVEEEAAQKNMALKKIR-ELETQISELQEDLESERACRNKAEKQKrdLGE 1139
Cdd:TIGR00618 402 LDILQREQATIDTR--TSAFRDLQGQLAHAKKQQELQQRYAELCAAAiTCTAQCEKLEKIHLQESAQSLKEREQQ--LQT 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1140 ELEALKTELEDTLDSTAAQQELrskREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEqtkrvkatlekak 1219
Cdd:TIGR00618 478 KEQIHLQETRKKAVVLARLLEL---QEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLE------------- 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1220 QTLENERGELANEVKallqgkgdsehKRKKVEAQLQELQVKFSEGERVRTELADKVSKLQVELDSVtgllnqsdsksskl 1299
Cdd:TIGR00618 542 TSEEDVYHQLTSERK-----------QRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRL-------------- 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1300 tkdfsalesqLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRnLEKQIATLHAQVTDMKKkmedgvgc 1379
Cdd:TIGR00618 597 ----------QDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQE-LALKLTALHALQLTLTQ-------- 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1380 lETAEEAKRRLQKDLEglsQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAK 1459
Cdd:TIGR00618 658 -ERVREHALSIRVLPK---ELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSD 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1460 YAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSskddvgksvhELEKSKRALEQQVEEMKT 1539
Cdd:TIGR00618 734 LAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAA----------EIQFFNRLREEDTHLLKT 803
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1540 QLEELEDELQATEDAKLRLEVNLQAMKAQFERDLqgrdeqseEKKKQLVRQVREMEAELEDERKQRSIAMAARKKLEMDL 1619
Cdd:TIGR00618 804 LEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRL--------EEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
810 820
....*....|....*....|.
gi 806638593 1620 KDLEAHIDTANKNREEAIKQL 1640
Cdd:TIGR00618 876 DKLNGINQIKIQFDGDALIKF 896
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1631-1913 |
9.80e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 9.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1631 KNREEAIKQLRKLQ---AQMKDCMRELD------DTRASREEILA--QAKENEKKLKSMEAEMIQLQEELAAAERAKRQA 1699
Cdd:TIGR02168 172 ERRKETERKLERTRenlDRLEDILNELErqlkslERQAEKAERYKelKAELRELELALLVLRLEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1700 QQERDELADEIANSSGKgalaLEEkrrLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINtdlnlershaqkneNA 1779
Cdd:TIGR02168 252 EEELEELTAELQELEEK----LEE---LRLEVSELEEEIEELQKELYALANEISRLEQQKQILR--------------ER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1780 RQQLERQNKELKAKLQEMESavkskykaSIAALEAKIAQLEEQLDNETKERQAASKQVRRAEKKLKDVLLQVEDERRNAE 1859
Cdd:TIGR02168 311 LANLERQLEELEAQLEELES--------KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 806638593 1860 QFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNRE 1913
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1383-1614 |
1.39e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1383 AEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKK----QKKFDQLLAEEKTISA 1458
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQElaalEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1459 KYAEERDR-------AEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALE 1531
Cdd:COG4942 98 ELEAQKEElaellraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1532 QQVEEMKTQLEELEDELQATEDAKLRLEVNLQAmkaqferdLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSIAMAA 1611
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAE--------LAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
...
gi 806638593 1612 RKK 1614
Cdd:COG4942 250 ALK 252
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1203-1846 |
1.45e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 60.12 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1203 EQLEQTKRVKATLEKAKQTLENERGELANEVKallQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKV--SKLQV 1280
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELK---QKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIqeNKDLI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1281 ELDSVT----GLLNQSDSKSSKLTKDF---------------SALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSF 1341
Cdd:pfam05483 148 KENNATrhlcNLLKETCARSAEKTKKYeyereetrqvymdlnNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1342 REQLEEEEEAKrnlEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDL----EGLSQRLEEKVAAYDKLEKTKTR 1417
Cdd:pfam05483 228 EEEYKKEINDK---EKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTklqdENLKELIEKKDHLTKELEDIKMS 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1418 LQQELDDllvdldhQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELER 1497
Cdd:pfam05483 305 LQRSMST-------QKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNED 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1498 LNKQFRTEMEDLMSSKDDVGKSVH----ELEKSKRAL--EQQVEEMKTQLEELEDELQATEDAKLRLevnLQAMKAQFEr 1571
Cdd:pfam05483 378 QLKIITMELQKKSSELEEMTKFKNnkevELEELKKILaeDEKLLDEKKQFEKIAEELKGKEQELIFL---LQAREKEIH- 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1572 DLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSIAMAARKKLEMDLK-----------DLEAHIDTANKNREEAIKQL 1640
Cdd:pfam05483 454 DLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKeltqeasdmtlELKKHQEDIINCKKQEERML 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1641 RKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALA 1720
Cdd:pfam05483 534 KQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEEL 613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1721 LEEKRRLEARIAQLEEE---------------LEEEQGNTELINDRLKKANLQ-IDQINTDLNLERSHAQKNENARQQ-- 1782
Cdd:pfam05483 614 HQENKALKKKGSAENKQlnayeikvnklelelASAKQKFEEIIDNYQKEIEDKkISEEKLLEEVEKAKAIADEAVKLQke 693
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1783 --------------------------LERQNKEL---KAKLQEmESAVKSKYKASIAALEAKIAQLEEQLDNETKERQAA 1833
Cdd:pfam05483 694 idkrcqhkiaemvalmekhkhqydkiIEERDSELglyKNKEQE-QSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKL 772
|
730
....*....|...
gi 806638593 1834 SKQVRRAEKKLKD 1846
Cdd:pfam05483 773 KMEAKENTAILKD 785
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1504-1879 |
1.63e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 59.80 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1504 TEMEDLMSSKDDvgksvhELEKSKRALEQqveeMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRdEQSEEK 1583
Cdd:pfam01576 1 TRQEEEMQAKEE------ELQKVKERQQK----AESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMR-ARLAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1584 KKQLVRQVREMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDtanknREEAIKQlrKLQAQMKDCmrelddtrasree 1663
Cdd:pfam01576 70 KQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLD-----EEEAARQ--KLQLEKVTT------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1664 ilaqakenEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEqg 1743
Cdd:pfam01576 130 --------EAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKE-- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1744 ntELINDRLKKANLQIDQINTDLNLERSHAQKN-ENARQQLERQNKELKAKLQ--EMESAVKSKYKASIAALEAKIAQLE 1820
Cdd:pfam01576 200 --EKGRQELEKAKRKLEGESTDLQEQIAELQAQiAELRAQLAKKEEELQAALArlEEETAQKNNALKKIRELEAQISELQ 277
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 806638593 1821 EQLDNETKERQAASKQVRRAEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQL 1879
Cdd:pfam01576 278 EDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKAL 336
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1628-1871 |
1.93e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.69 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1628 TANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELA 1707
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1708 DEIANSSGKGALaleekrrLEARIAQleeeleeeQGNTELInDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQN 1787
Cdd:COG3883 93 RALYRSGGSVSY-------LDVLLGS--------ESFSDFL-DRLSALSKIADADADLLEELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1788 KELKAKLQEMESAvKSKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRAEKKLKDVLLQVEDERRNAEQFKDQADK 1867
Cdd:COG3883 157 AELEALKAELEAA-KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
....
gi 806638593 1868 ASTR 1871
Cdd:COG3883 236 AAAA 239
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1063-1235 |
2.63e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 56.86 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1063 QIAELQAQIAELKMQLAKKEEELQAALARVEEeaaqknmALKKIRELETQISELQEDLESERACRNKAEKQKRDLG--EE 1140
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEA-------AKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1141 LEALKTELEdtldSTAAQQELRSKREQEvsilkktLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQ 1220
Cdd:COG1579 91 YEALQKEIE----SLKRRISDLEDEILE-------LMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
170
....*....|....*
gi 806638593 1221 TLENERGELANEVKA 1235
Cdd:COG1579 160 ELEAEREELAAKIPP 174
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1443-1905 |
3.12e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 59.29 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1443 QKKFDQLLAEEKTISAkyaEERDRAEAEAREKETKALSLARALEEAMEQKAELERlnKQFRTEMEDLMSSKDDVGKSVHE 1522
Cdd:TIGR00606 172 KQKFDEIFSATRYIKA---LETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIR--DQITSKEAQLESSREIVKSYENE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1523 LEKSKRALeQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDER 1602
Cdd:TIGR00606 247 LDPLKNRL-KEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1603 KQRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLK--SMEA 1680
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVieRQED 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1681 EMIQLQEELAAAERAKRQAQQERDELADEIansSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKanlqiD 1760
Cdd:TIGR00606 406 EAKTAAQLCADLQSKERLKQEQADEIRDEK---KGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILEL-----D 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1761 QINTDLNLERSHAQKNENARQQLERQnKELKAKlqemesavKSKYKASIAALEAKIAQLE------EQLDNETKERQAAS 1834
Cdd:TIGR00606 478 QELRKAERELSKAEKNSLTETLKKEV-KSLQNE--------KADLDRKLRKLDQEMEQLNhhtttrTQMEMLTKDKMDKD 548
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 806638593 1835 KQVRRAEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATE 1905
Cdd:TIGR00606 549 EQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE 619
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1083-1550 |
3.38e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1083 EELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERACRNKAEKQKR--DLGEELEALKTELEDT---LDSTAA 1157
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELperLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1158 QQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQTLENERGELANEVKALl 1237
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1238 qgkgDSEHKRKKVEAQLQELQVkfsegervrteladkvskLQVELDSVTGLLNQSDSKSSKLTKDFSALESQLQDTQELL 1317
Cdd:COG4717 233 ----ENELEAAALEERLKEARL------------------LLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1318 QEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQkdLEGL 1397
Cdd:COG4717 291 LLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEEL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1398 SQRLEEKVAAYDklektktrlqQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAR--EKE 1475
Cdd:COG4717 369 EQEIAALLAEAG----------VEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEEleELE 438
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 806638593 1476 TKALSLARALEEAMEQKAELErlnkqfrTEMEDLMSSkddvgksvHELEKskraLEQQVEEMKTQLEELEDELQA 1550
Cdd:COG4717 439 EELEELEEELEELREELAELE-------AELEQLEED--------GELAE----LLQELEELKAELRELAEEWAA 494
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1666-1910 |
3.69e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.49 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1666 AQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDeladeIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNT 1745
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG-----LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1746 ELINDRLKKANLQIDQINTDLNLershaqknenarQQLERQNKELKAKLQEMESAVKSKYKAsIAALEAKIAQLEEQLDN 1825
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVI------------QQLRAQLAELEAELAELSARYTPNHPD-VIALRAQIAALRAQLQQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1826 ETKErqaaskqvrraekklkdVLLQVEDERRNAEQfkdQADKASTRLKQLKRQLEEAEEEAQRAnasrRKLQRELEDATE 1905
Cdd:COG3206 310 EAQR-----------------ILASLEAELEALQA---REASLQAQLAQLEARLAELPELEAEL----RRLEREVEVARE 365
|
....*
gi 806638593 1906 TADAM 1910
Cdd:COG3206 366 LYESL 370
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1026-1826 |
4.12e-08 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 58.91 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1026 EAMITDLEERLRREEKQRQELEKTRRKL-----EGDSTDLSDQIAELQAQI-AELKMQLAK-------KEEELQAALARV 1092
Cdd:TIGR01612 695 KAKLDDLKSKIDKEYDKIQNMETATVELhlsniENKKNELLDIIVEIKKHIhGEINKDLNKiledfknKEKELSNKINDY 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1093 EEEAAQKNMALKKIRELETQISElQEDLESeracrNKAEKQKRDLGEELEALKTeledtldsTAAQQELRSKREQEVsil 1172
Cdd:TIGR01612 775 AKEKDELNKYKSKISEIKNHYND-QINIDN-----IKDEDAKQNYDKSKEYIKT--------ISIKEDEIFKIINEM--- 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1173 kKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQL-EQTKRVKATLEKAKQTLE----NERGELANEVKALLQGKGDSEHKR 1247
Cdd:TIGR01612 838 -KFMKDDFLNKVDKFINFENNCKEKIDSEHEQFaELTNKIKAEISDDKLNDYekkfNDSKSLINEINKSIEEEYQNINTL 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1248 KKVEAQLQ------ELQVKFSEGERVRTELADKVSKLQVELDSV-TGLLNQSDS----KSSKLTKDFS--ALESQLQDTQ 1314
Cdd:TIGR01612 917 KKVDEYIKicentkESIEKFHNKQNILKEILNKNIDTIKESNLIeKSYKDKFDNtlidKINELDKAFKdaSLNDYEAKNN 996
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1315 ELLQEENRQKLSLSTklkqmeDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVgcLETAEEAKRRLQKDL 1394
Cdd:TIGR01612 997 ELIKYFNDLKANLGK------NKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSI--YNIIDEIEKEIGKNI 1068
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1395 EGLSQRLEEKVAAydklektktrlqqelddllvdldhqrqSVSNLEKKQKK-----FDQLLAEEktiSAKYAEERDRAea 1469
Cdd:TIGR01612 1069 ELLNKEILEEAEI---------------------------NITNFNEIKEKlkhynFDDFGKEE---NIKYADEINKI-- 1116
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1470 eareketkalslaraleeameqKAELERLNKQfrtemedlmsskddVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQ 1549
Cdd:TIGR01612 1117 ----------------------KDDIKNLDQK--------------IDHHIKALEEIKKKSENYIDEIKAQINDLEDVAD 1160
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1550 AT---EDAKlRLEVNLQAMKAQFERDLQGRDEQseekkKQLVRQVREMEAELEDERKQRSIAMAARKKLEmdlKDLEAHI 1626
Cdd:TIGR01612 1161 KAisnDDPE-EIEKKIENIVTKIDKKKNIYDEI-----KKLLNEIAEIEKDKTSLEEVKGINLSYGKNLG---KLFLEKI 1231
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1627 DTANKNREEAIKQLRKLqaqmkdcMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEelaaaERAKRQAQQERDEL 1706
Cdd:TIGR01612 1232 DEEKKKSEHMIKAMEAY-------IEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDD-----DKDHHIISKKHDEN 1299
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1707 ADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKK-AN----LQIDQINTDLNLERSHAQKnenarq 1781
Cdd:TIGR01612 1300 ISDIREKSLKIIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEiANiyniLKLNKIKKIIDEVKEYTKE------ 1373
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 806638593 1782 qLERQNKELKAKLQEMESAVKsKYKASIAALEAKiAQLEEQLDNE 1826
Cdd:TIGR01612 1374 -IEENNKNIKDELDKSEKLIK-KIKDDINLEECK-SKIESTLDDK 1415
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1199-1821 |
4.72e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.37 E-value: 4.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1199 EELAEQLEQTKRVKATLEKAKQTLENERGELAN--EVKALLQGKGDSEHKRKKveaQLQELQVKFSEGERVRTELADKVS 1276
Cdd:PRK01156 152 KKILDEILEINSLERNYDKLKDVIDMLRAEISNidYLEEKLKSSNLELENIKK---QIADDEKSHSITLKEIERLSIEYN 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1277 KLQVELDSVTGLLNQSDSKSSKLTKdfsaLESQLQDTQELLQEEnrqkLSLSTKLKQMEDEKNsfrEQLEEEEEAKRNLE 1356
Cdd:PRK01156 229 NAMDDYNNLKSALNELSSLEDMKNR----YESEIKTAESDLSME----LEKNNYYKELEERHM---KIINDPVYKNRNYI 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1357 KQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQkDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDldhqrqsV 1436
Cdd:PRK01156 298 NDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLS-VLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSY-------L 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1437 SNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEA--------------REKETKALSLARALEEAMEQKAELER----L 1498
Cdd:PRK01156 370 KSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPdaikkelneinvklQDISSKVSSLNQRIRALRENLDELSRnmemL 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1499 NKQFR-----TEMEDLMSSK--DDVGKSVHELEKSKRALEQQV---EEMKTQLEELEDELQATEDAKLRLEVN-LQAMKA 1567
Cdd:PRK01156 450 NGQSVcpvcgTTLGEEKSNHiiNHYNEKKSRLEEKIREIEIEVkdiDEKIVDLKKRKEYLESEEINKSINEYNkIESARA 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1568 QFERDL--QGRDEQSEEKKKQLVRQVREMEAE-LEDERKQRSIAMAARKKLEmdlkdleahIDTANKNREEAIKQLRKLQ 1644
Cdd:PRK01156 530 DLEDIKikINELKDKHDKYEEIKNRYKSLKLEdLDSKRTSWLNALAVISLID---------IETNRSRSNEIKKQLNDLE 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1645 AQMKDCMRELDDTRASreeilaqakeNEKKLKSMEAEMIQLQEELAAAERAKRQaqqeRDELADEIANssgkgalaleek 1724
Cdd:PRK01156 601 SRLQEIEIGFPDDKSY----------IDKSIREIENEANNLNNKYNEIQENKIL----IEKLRGKIDN------------ 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1725 rrLEARIAQLEEeleeeqgntelINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSK 1804
Cdd:PRK01156 655 --YKKQIAEIDS-----------IIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDI 721
|
650
....*....|....*....
gi 806638593 1805 YK--ASIAALEAKIAQLEE 1821
Cdd:PRK01156 722 NEtlESMKKIKKAIGDLKR 740
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1317-1888 |
5.00e-08 |
|
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: 58.21 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1317 LQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEA-KRNLEKQIATLHAQVTDM----KKKMEDGVGCLETAEEAkRRLQ 1391
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASAlKRQLDRESDRNQELQKRIrlleKREAEAEEALREQAELN-RLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1392 KDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERD------ 1465
Cdd:pfam05557 83 KYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQnlekqq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1466 --RAEAEAREKE--------TKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQvE 1535
Cdd:pfam05557 163 ssLAEAEQRIKElefeiqsqEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLERE-E 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1536 EMKTQLEELEDELQATEdAKLRLEVNLQAMKAQFER---DLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRsiamaar 1612
Cdd:pfam05557 242 KYREEAATLELEKEKLE-QELQSWVKLAQDTGLNLRspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKAR------- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1613 KKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRA---SREEILAQAKENEKKLKSME--AEMIQLQE 1687
Cdd:pfam05557 314 RELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAileSYDKELTMSNYSPQLLERIEeaEDMTQKMQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1688 ELAAAERAkrqaqqeRDELADEIANSSGKGALALEekRRLEARIAQLEEELeeeQGNTELINDRLKKANlqidqinTDLN 1767
Cdd:pfam05557 394 AHNEEMEA-------QLSVAEEELGGYKQQAQTLE--RELQALRQQESLAD---PSYSKEEVDSLRRKL-------ETLE 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1768 LERshaqknenarQQLERQNKELKAKLQEMESAVKSKYKASiaaleaKIAQLEEQLDNETKERQAASKQVRRAE-KKLKD 1846
Cdd:pfam05557 455 LER----------QRLREQKNELEMELERRCLQGDYDPKKT------KVLHLSMNPAAEAYQQRKNQLEKLQAEiERLKR 518
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 806638593 1847 VLLQVEDERRNAEQFKDQADK-ASTRLKQLKRQLEEAEEEAQR 1888
Cdd:pfam05557 519 LLKKLEDDLEQVLRLPETTSTmNFKEVLDLRKELESAELKNQR 561
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1268-1497 |
5.33e-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: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1268 RTELADKVSKLQVELDSVTGLLNQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEE 1347
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1348 EeeaKRNLEKQIATLHaqvtdmKKKMEDGVGCL---ETAEEAKRRLQkDLEGLSQRLEEKVaayDKLEKTKTRLQQELDD 1424
Cdd:COG4942 102 Q---KEELAELLRALY------RLGRQPPLALLlspEDFLDAVRRLQ-YLKYLAPARREQA---EELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 806638593 1425 LLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELER 1497
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
833-1534 |
6.39e-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: 6.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 833 KVKPLLNSIRHEDELLAKEAELTK-VREKHLAAENRLTEmetmqSQLMAEKLQLQEQLQAETELCAEAEELRAR------ 905
Cdd:TIGR00606 459 VIKELQQLEGSSDRILELDQELRKaERELSKAEKNSLTE-----TLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhhttt 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 906 ------LTAKKQELEEICHDLEARVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEkvtteakLKKLEED 979
Cdd:TIGR00606 534 rtqmemLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKE-------LASLEQN 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 980 QIIMEDQNCKLAKEKKLLEDRVAEFTT---------NLMEEEEKSKS----LAKLKNKHEAMITDLEERLRREEKQRQEL 1046
Cdd:TIGR00606 607 KNHINNELESKEEQLSSYEDKLFDVCGsqdeesdleRLKEEIEKSSKqramLAGATAVYSQFITQLTDENQSCCPVCQRV 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1047 EKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERAC 1126
Cdd:TIGR00606 687 FQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKND 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1127 RNKAEKQKRDLGEELEALKTELEDTldsTAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEEL---AE 1203
Cdd:TIGR00606 767 IEEQETLLGTIMPEEESAKVCLTDV---TIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELdtvVS 843
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1204 QLEQTKRVKATLEKAKQTLENERGELANEVKALlqgkGDSEHKRKKVEAQLQElqvKFSEGERVRTELADkvsklqveld 1283
Cdd:TIGR00606 844 KIELNRKLIQDQQEQIQHLKSKTNELKSEKLQI----GTNLQRRQQFEEQLVE---LSTEVQSLIREIKD---------- 906
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1284 svtgllnqsdsKSSKLTKDFSALESQLQDTQELLQEENRQKlslstklKQMEDEKNSFREQLEEEEEAKRNLEKQIAT-L 1362
Cdd:TIGR00606 907 -----------AKEQDSPLETFLEKDQQEKEELISSKETSN-------KKAQDKVNDIKEKVKNIHGYMKDIENKIQDgK 968
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1363 HAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQElddllvdldhqrQSVSNLEKK 1442
Cdd:TIGR00606 969 DDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRE------------NELKEVEEE 1036
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1443 QKKFDQLLAEEKTISAKYAEERDRAEAEA-REKETKALSLARALEEAMEQkAELERLNKQFRTEME---DLMSSKDDVGK 1518
Cdd:TIGR00606 1037 LKQHLKEMGQMQVLQMKQEHQKLEENIDLiKRNHVLALGRQKGYEKEIKH-FKKELREPQFRDAEEkyrEMMIVMRTTEL 1115
|
730
....*....|....*.
gi 806638593 1519 SVHELEKSKRALEQQV 1534
Cdd:TIGR00606 1116 VNKDLDIYYKTLDQAI 1131
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
958-1374 |
6.45e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 6.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 958 ARQKLQLEKvTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAefttnLMEEEEKSKSLAKLKNKHEAMITDLEERLR 1037
Cdd:COG4717 76 LEEELKEAE-EKEEEYAELQEELEELEEELEELEAELEELREELE-----KLEKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1038 REEKQRQELEKTRRKLEgdstDLSDQIAELQAQIAELKMQL-AKKEEELQAALARVEEEAAQKNMALKKIRELETQISEL 1116
Cdd:COG4717 150 ELEERLEELRELEEELE----ELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1117 QEDLESERACRNKAEKQKR-----------DLGEELEALKTELEDTLDSTAA------------------QQELRSKREQ 1167
Cdd:COG4717 226 EEELEQLENELEAAALEERlkearlllliaAALLALLGLGGSLLSLILTIAGvlflvlgllallflllarEKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1168 EVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKA-KQTLENERGELANEVKALLQGKGDSEhk 1246
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAeELEEELQLEELEQEIAALLAEAGVED-- 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1247 rkkvEAQLQELQVKFSEGERVRTELADKVSKLQVELDSVTGLLNQSDSKSskLTKDFSALESQLQDTQELLQEENRQKLS 1326
Cdd:COG4717 384 ----EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE--LEEELEELEEELEELEEELEELREELAE 457
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 806638593 1327 LSTKLKQMEDEKN--SFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKME 1374
Cdd:COG4717 458 LEAELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALELLEEARE 507
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1652-1871 |
6.80e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.72 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1652 RELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEE--LAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEA 1729
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1730 RIAQLEEELEEEQGNTELINDRLkkanlQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSKYKASI 1809
Cdd:COG3206 248 QLGSGPDALPELLQSPVIQQLRA-----QLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAEL 322
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 806638593 1810 AALEAKIAQLEEQLDNETKERQAASKQvrraEKKLKDVLLQVEDERRNAEQFKDQADKASTR 1871
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELPEL----EAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
897-1125 |
7.24e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 7.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 897 AEAEELRARLTAKKQELEEICHDLEArveeeeercqyLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKL 976
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAA-----------LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 977 EEDQIIMEDQnckLAKEKKLLEDRVAEFTTN-------LMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKT 1049
Cdd:COG4942 89 EKEIAELRAE---LEAQKEELAELLRALYRLgrqpplaLLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 806638593 1050 RRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERA 1125
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
827-1219 |
7.49e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 7.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 827 WWRLFTKVKPLLNSIRhedELLAKEAELT--KVREKHLAAENRLTEMETMQSQLMAEKLQLQ---EQLQAETELCAEA-- 899
Cdd:PRK03918 360 RHELYEEAKAKKEELE---RLKKRLTGLTpeKLEKELEELEKAKEEIEEEISKITARIGELKkeiKELKKAIEELKKAkg 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 900 ----------EELRARLTAK-KQELEEIchdlEARVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVT 968
Cdd:PRK03918 437 kcpvcgreltEEHRKELLEEyTAELKRI----EKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKL 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 969 TEAKLKKLEEDqiimedqncklAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAmitdLEERLRREEKQRQELEK 1048
Cdd:PRK03918 513 KKYNLEELEKK-----------AEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE----LEKKLDELEEELAELLK 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1049 TRRKLE-GDSTDLSDQIAELQ-------------AQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQIS 1114
Cdd:PRK03918 578 ELEELGfESVEELEERLKELEpfyneylelkdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS 657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1115 ELQ-EDLESERACRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLED-----------EAKT 1182
Cdd:PRK03918 658 EEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERveelrekvkkyKALL 737
|
410 420 430
....*....|....*....|....*....|....*..
gi 806638593 1183 HEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAK 1219
Cdd:PRK03918 738 KERALSKVGEIASEIFEELTEGKYSGVRVKAEENKVK 774
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1658-1926 |
7.54e-08 |
|
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: 57.77 E-value: 7.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1658 RASREEiLAQAKENEKKLKSMEAEMIQ----LQEELAAAERAKRQAQQERDELADEIANSSGKgalALEEKRRLEARIAQ 1733
Cdd:TIGR02169 173 EKALEE-LEEVEENIERLDLIIDEKRQqlerLRREREKAERYQALLKEKREYEGYELLKEKEA---LERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1734 leeeleeeqgntelINDRLKKANLQIDQINtdlnlERSHAqknenARQQLERQNKELKAKLQEMESAVKSK---YKASIA 1810
Cdd:TIGR02169 249 --------------LEEELEKLTEEISELE-----KRLEE-----IEQLLEELNKKIKDLGEEEQLRVKEKigeLEAEIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1811 ALEAKIAQLEEQLDNETKERQAASKQVRRAEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRAN 1890
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
250 260 270
....*....|....*....|....*....|....*.
gi 806638593 1891 ASRRKLQRELEDATETADAMNREVSSLKNKLRRGDM 1926
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1620-1923 |
8.52e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 57.61 E-value: 8.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1620 KDLEAHIDTANKNREeaikqlrkLQAQMKDCMRELDDTRASREEILAQAKENEkklksmeaemiQLQEELAAAERAKRQA 1699
Cdd:PRK11281 39 ADVQAQLDALNKQKL--------LEAEDKLVQQDLEQTLALLDKIDRQKEETE-----------QLKQQLAQAPAKLRQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1700 QQERDELADEiANSSGKGALALEEKRRLEARIAQleeeleeeqgntelINDRLKKANLQIDQINTDL-----NLERSHAQ 1774
Cdd:PRK11281 100 QAELEALKDD-NDEETRETLSTLSLRQLESRLAQ--------------TLDQLQNAQNDLAEYNSQLvslqtQPERAQAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1775 KNENAR--QQLERQNKELKAKLQEMESAVKSKYKASIAALEAKIAQLEEQLDNET-------KERQAASKQVRRAEKKLK 1845
Cdd:PRK11281 165 LYANSQrlQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTqlqdllqKQRDYLTARIQRLEHQLQ 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 806638593 1846 dvLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANasrRKLQRELEDATETADAMNREVSSLKNKLRR 1923
Cdd:PRK11281 245 --LLQEAINSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEIN---LQLSQRLLKATEKLNTLTQQNLRVKNWLDR 317
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
838-1226 |
9.23e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 9.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 838 LNSIRHEDELLAKEAELTKVREKHLAAENRLTEMETMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEic 917
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL-- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 918 hdlearveEEEERCQYLQAEKKKMQQNIQELEEqleeeesARQKLQLEKVTTEAKLKKLEEDQIIMEDQNC-KLAKEKKL 996
Cdd:COG4717 189 --------ATEEELQDLAEELEELQQRLAELEE-------ELEEAQEELEELEEELEQLENELEAAALEERlKEARLLLL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 997 LEDRVAEFTTNLMEEEEKSKSLA------------------KLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDST 1058
Cdd:COG4717 254 IAAALLALLGLGGSLLSLILTIAgvlflvlgllallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1059 -------DLSDQIAELQAQIAEL-----KMQLAKKEEELQAALARV----EEEAAQKNMALKKIRELETQISELQEDLES 1122
Cdd:COG4717 334 lspeellELLDRIEELQELLREAeeleeELQLEELEQEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLEE 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1123 ER--ACRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVSILKKtledeakthEAQIQEMRQKHSQAVEE 1200
Cdd:COG4717 414 LLgeLEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE---------DGELAELLQELEELKAE 484
|
410 420
....*....|....*....|....*....
gi 806638593 1201 LAEQLEQTKRVK---ATLEKAKQTLENER 1226
Cdd:COG4717 485 LRELAEEWAALKlalELLEEAREEYREER 513
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1522-1720 |
1.06e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1522 ELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQ---FERDLQGRDEQSEEKKKQLVRQVREME--- 1595
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEidkLQAEIAEAEAEIEERREELGERARALYrsg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1596 ---------------AELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRAS 1660
Cdd:COG3883 100 gsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1661 REEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALA 1720
Cdd:COG3883 180 QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
844-1226 |
1.19e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 844 EDELLAKEAELTKVREKHLAAENRLTEMETMQS--QLMAEKLQLQEQLQaetELCAEAEELRARLTAKKQELEEICHDLE 921
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELA---ELPERLEELEERLEELRELEEELEELEA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 922 ARVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDR- 1000
Cdd:COG4717 171 ELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARl 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1001 -------VAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQrqeLEKTRRKLEGDSTDLSDQIAELQAQIAE 1073
Cdd:COG4717 251 llliaaaLLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAS---LGKEAEELQALPALEELEEEELEELLAA 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1074 LKMQLAKKEEELQAALARVEEeaaqknmalkkIRELETQISELQEDLESERACRNKAEKQKRDLGEELEALKTELEDTLD 1153
Cdd:COG4717 328 LGLPPDLSPEELLELLDRIEE-----------LQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEE 396
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 806638593 1154 STAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQTLENER 1226
Cdd:COG4717 397 YQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG 469
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1010-1324 |
1.48e-07 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 56.83 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1010 EEEEKSKSLAKLKNkheAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAal 1089
Cdd:PLN02939 114 EQQTNSKDGEQLSD---FQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKL-- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1090 arveeeAAQKNMALKKIRE-LETQISELQEDLESERACRNKaekqkrdLGEELEALKTE---LEDtlDSTAAQQELRSKR 1165
Cdd:PLN02939 189 ------AAQEKIHVEILEEqLEKLRNELLIRGATEGLCVHS-------LSKELDVLKEEnmlLKD--DIQFLKAELIEVA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1166 EQEVSILKktLEDEAKTHEAQIQEMRQKHSQAVEELAEQleQTKRVKATLEKAkQTLENERGELANEVK---ALLQGKGD 1242
Cdd:PLN02939 254 ETEERVFK--LEKERSLLDASLRELESKFIVAQEDVSKL--SPLQYDCWWEKV-ENLQDLLDRATNQVEkaaLVLDQNQD 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1243 SEHKRKKVEAQLQELQV-KFSegervrtelADKVSKLQVELDSVTGLLNQSDSKSSKLTKDFSALESQLQDTQELLQEEN 1321
Cdd:PLN02939 329 LRDKVDKLEASLKEANVsKFS---------SYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEES 399
|
...
gi 806638593 1322 RQK 1324
Cdd:PLN02939 400 KKR 402
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1381-1910 |
1.55e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 56.65 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1381 ETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKY 1460
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1461 AEERDRAEAEAREKETKALSLARALE------EAMEQKAELERLNKQFR--TEMEDLMSSKDDVGKSVHELEKSKRALEQ 1532
Cdd:pfam05483 168 AEKTKKYEYEREETRQVYMDLNNNIEkmilafEELRVQAENARLEMHFKlkEDHEKIQHLEEEYKKEINDKEKQVSLLLI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1533 QVEEMKTQLEELEDELQATEDAKLRLEvnlqamkaqferdlqGRDEQSEEKKKQLVRQVREMEAELEDERKQRSIAMAAR 1612
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKANQLE---------------EKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQ 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1613 KKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKE----NEKKLKSMEAEMIQLQEE 1688
Cdd:pfam05483 313 KALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQrlekNEDQLKIITMELQKKSSE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1689 LAAAERAKRQAQQERDEL--------------------ADEIANSSGKGALALEEKRR----LEARI-----AQLEEELE 1739
Cdd:pfam05483 393 LEEMTKFKNNKEVELEELkkilaedeklldekkqfekiAEELKGKEQELIFLLQAREKeihdLEIQLtaiktSEEHYLKE 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1740 EEQGNTELINDRLKKANL------------QIDQINTDLNLE-RSHAQKNENARQQLERQNKELKaKLQEMES------- 1799
Cdd:pfam05483 473 VEDLKTELEKEKLKNIELtahcdklllenkELTQEASDMTLElKKHQEDIINCKKQEERMLKQIE-NLEEKEMnlrdele 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1800 AVKSKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRAEKKLKDVLLQVEDERRNAEQFKDQAdkastrlKQLKRQL 1879
Cdd:pfam05483 552 SVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQEN-------KALKKKG 624
|
570 580 590
....*....|....*....|....*....|.
gi 806638593 1880 EEAEEEAQRANASRRKLQRELEDATETADAM 1910
Cdd:pfam05483 625 SAENKQLNAYEIKVNKLELELASAKQKFEEI 655
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1026-1230 |
1.55e-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: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1026 EAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKK 1105
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1106 IRELETQISELQEDLESE--------RACRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLE 1177
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSEsfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 806638593 1178 DEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQTLENERGELA 1230
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1012-1228 |
1.78e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 56.37 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1012 EEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLakkEEELQAALAR 1091
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKE 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1092 VEEEAAQknmALKKIRELETQISELQEDLESERACRNKAEKQkrdlgEELEALKTELEDTLDSTAAQQELR-SKREQEVS 1170
Cdd:PRK00409 582 AKKEADE---IIKELRQLQKGGYASVKAHELIEARKRLNKAN-----EKKEKKKKKQKEKQEELKVGDEVKyLSLGQKGE 653
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 806638593 1171 ILKKTLEDEAkTHEAQIQEMRQKHSQaVEELAEQLEQTKRVKATLEKAKQTLENE---RGE 1228
Cdd:PRK00409 654 VLSIPDDKEA-IVQAGIMKMKVPLSD-LEKIQKPKKKKKKKPKTVKPKPRTVSLEldlRGM 712
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
881-1525 |
2.14e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 55.98 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 881 EKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQYLQAEKKK--------------MQQNIQ 946
Cdd:pfam10174 68 ENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERqakelfllrktleeMELRIE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 947 ELEEQLEEEESARQKLqLEKVTTEAKLKKLEEDQ-------IIMEDQNCKL-----AKEKKLLEDRVAEFTTN-LMEEEE 1013
Cdd:pfam10174 148 TQKQTLGARDESIKKL-LEMLQSKGLPKKSGEEDwertrriAEAEMQLGHLevlldQKEKENIHLREELHRRNqLQPDPA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1014 KSKSLAKLKNKHEAMITDLEERLRREEkqrQELEKTRRKLEGDSTDLSDQIAELQA----------QIAELKMQLAKKEE 1083
Cdd:pfam10174 227 KTKALQTVIEMKDTKISSLERNIRDLE---DEVQMLKTNGLLHTEDREEEIKQMEVykshskfmknKIDQLKQELSKKES 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1084 ELQAALARVEE------------EAAQKNMALKKIRE--LETQISELQEDLESERACRNKAEKQKRDLGEELEALKTELE 1149
Cdd:pfam10174 304 ELLALQTKLETltnqnsdckqhiEVLKESLTAKEQRAaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIR 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1150 DTLDstaaqqeLRSKREQEVSILKKTLE---DEAKTHEAQIQEMRqkhsQAVEELAEQLEQTKRVKATLEKA----KQTL 1222
Cdd:pfam10174 384 DLKD-------MLDVKERKINVLQKKIEnlqEQLRDKDKQLAGLK----ERVKSLQTDSSNTDTALTTLEEAlsekERII 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1223 ENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVSKLQVELDSVTGLLNQSDSKSSKLTKD 1302
Cdd:pfam10174 453 ERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEE 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1303 FSALESQLQDTQElLQEENRQKLSLSTKLKQMEDEKNSFREQ--------------LEEEEEAKRNLEKQIATLHAQVTD 1368
Cdd:pfam10174 533 CSKLENQLKKAHN-AEEAVRTNPEINDRIRLLEQEVARYKEEsgkaqaeverllgiLREVENEKNDKDKKIAELESLTLR 611
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1369 MKKKMEDGVGCLETAEEAKRRlqkdleGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDhqRQSVSNLEKKQKKFDQ 1448
Cdd:pfam10174 612 QMKEQNKKVANIKHGQQEMKK------KGAQLLEEARRREDNLADNSQQLQLEELMGALEKT--RQELDATKARLSSTQQ 683
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 806638593 1449 LLAEEKTISAKYAEERDRAEAEAREKETKALsLArALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEK 1525
Cdd:pfam10174 684 SLAEKDGHLTNLRAERRKQLEEILEMKQEAL-LA-AISEKDANIALLELSSSKKKKTQEEVMALKREKDRLVHQLKQ 758
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
862-1100 |
2.28e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 862 LAAENRLTEMETMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQYLQAEKKKM 941
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 942 QQNIQELEEQLEEEESARQKLQLekvTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKL 1021
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGR---QPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 806638593 1022 KNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKN 1100
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
842-1559 |
2.47e-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: 55.91 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 842 RHEDELLAKEAELTKVREKHLAAENRLTemetmqsqlmAEKLQLQEQLQAETELCAEAEELRARLTAKkqelEEICHDLE 921
Cdd:pfam07111 70 RQLQELRRLEEEVRLLRETSLQQKMRLE----------AQAMELDALAVAEKAGQAEAEGLRAALAGA----EMVRKNLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 922 ARVEEEEERCQYLQAEkkkmQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQncklaKEKKLLEDRV 1001
Cdd:pfam07111 136 EGSQRELEEIQRLHQE----QLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQ-----KEAELLRKQL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1002 AEfttnLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKK 1081
Cdd:pfam07111 207 SK----TQEELEAQVTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQ 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1082 EEELQ---AALARVEEEAAQKNMALkkIRELETQISELQEDLESERACRNKAEKQKRDLGEELealkteledtldstaaq 1158
Cdd:pfam07111 283 EEELTrkiQPSDSLEPEFPKKCRSL--LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAEL----------------- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1159 QELRSKREQEVSILKKTLEDeaKTHEAQIQEMRQKHSQAveELAEQLEQTKRVKATLEKAKQTLENERGELaNEVKALLQ 1238
Cdd:pfam07111 344 QEQVTSQSQEQAILQRALQD--KAAEVEVERMSAKGLQM--ELSRAQEARRRQQQQTASAEEQLKFVVNAM-SSTQIWLE 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1239 GkgdSEHKRKKVEAQLQELQVKFSEGER----VRTELADKVSKLQVELDsvtgllnqsdskSSKLTKDFSALESQLQ-DT 1313
Cdd:pfam07111 419 T---TMTRVEQAVARIPSLSNRLSYAVRkvhtIKGLMARKVALAQLRQE------------SCPPPPPAPPVDADLSlEL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1314 QELLQEENRQKLSLSTKLKQMEDEKNSFREQ----LEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGV-GCLETAEEA-- 1386
Cdd:pfam07111 484 EQLREERNRLDAELQLSAHLIQQEVGRAREQgeaeRQQLSEVAQQLEQELQRAQESLASVGQQLEVARqGQQESTEEAas 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1387 -KRRLQKDLEGLSQRLEEKVAaydkleKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISakyaEERD 1465
Cdd:pfam07111 564 lRQELTQQQEIYGQALQEKVA------EVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERN----QELR 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1466 RAEAEAREKEtkALSLARALEE----------AMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQV- 1534
Cdd:pfam07111 634 RLQDEARKEE--GQRLARRVQElerdknlmlaTLQQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPRPECSASAPIPAAVp 711
|
730 740
....*....|....*....|....*..
gi 806638593 1535 --EEMKTQLEELEDELQATEDAKLRLE 1559
Cdd:pfam07111 712 trESIKGSLTVLLDNLQGLSEAISREE 738
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
990-1222 |
2.64e-07 |
|
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: 55.07 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 990 LAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQA 1069
Cdd:pfam19220 81 AEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1070 QIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQ-------ISELQEDLESERACRNKAEKQkrdLGEELE 1142
Cdd:pfam19220 161 ELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQldatrarLRALEGQLAAEQAERERAEAQ---LEEAVE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1143 ALKTELE------DTLDSTAAQ-----QELRSK---REQEVSILKKTLED---EAKTHEAQIQEMRQKHSQAVEELAEql 1205
Cdd:pfam19220 238 AHRAERAslrmklEALTARAAAteqllAEARNQlrdRDEAIRAAERRLKEasiERDTLERRLAGLEADLERRTQQFQE-- 315
|
250
....*....|....*..
gi 806638593 1206 eqTKRVKATLEKAKQTL 1222
Cdd:pfam19220 316 --MQRARAELEERAEML 330
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1383-1923 |
2.66e-07 |
|
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: 56.13 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1383 AEEAKRRLQKDLEGLSQRLEEKVAAYDKL-EKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYA 1461
Cdd:pfam02463 206 AKKALEYYQLKEKLELEEEYLLYLDYLKLnEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1462 EERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQL 1541
Cdd:pfam02463 286 EELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQ 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1542 EELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEqsEEKKKQLVRQVREMEAELEDERKQRsiamaARKKLEMDLKD 1621
Cdd:pfam02463 366 EKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE--EEKEAQLLLELARQLEDLLKEEKKE-----ELEILEEEEES 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1622 LEAHIDTANKNREEAIKQLRKLQAQMKD-----------------CMRELDDTRASREEILAQAKENEKKLKSMEAEMIQ 1684
Cdd:pfam02463 439 IELKQGKLTEEKEELEKQELKLLKDELElkksedllketqlvklqEQLELLLSRQKLEERSQKESKARSGLKVLLALIKD 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1685 LQEELAAAERAKRQAQQERDEL---ADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQ 1761
Cdd:pfam02463 519 GVGGRIISAHGRLGDLGVAVENykvAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLE 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1762 INTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRAE 1841
Cdd:pfam02463 599 IDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEI 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1842 KKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKR--------QLEEAEEEAQRANASRRKLQRELEDATETADAMNRE 1913
Cdd:pfam02463 679 QELQEKAESELAKEEILRRQLEIKKKEQREKEELKKlkleaeelLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLK 758
|
570
....*....|
gi 806638593 1914 VSSLKNKLRR 1923
Cdd:pfam02463 759 KEEKEEEKSE 768
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1406-1918 |
2.86e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 55.68 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1406 AAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTIsakyAEERDRAEAEAREKETKALSLARAL 1485
Cdd:PRK01156 166 RNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSIT----LKEIERLSIEYNNAMDDYNNLKSAL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1486 EEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKR-----------------ALEQQVEEMKTQLEELEDEL 1548
Cdd:PRK01156 242 NELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKiindpvyknrnyindyfKYKNDIENKKQILSNIDAEI 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1549 QATEDAKLRLEVnLQAMKAQFERDLQGRDE---------QSEEKKKQLVRQVREMEAELEDERKQRSIAMAARKKLemdL 1619
Cdd:PRK01156 322 NKYHAIIKKLSV-LQKDYNDYIKKKSRYDDlnnqileleGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEI---L 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1620 KDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEI-------------------LAQAKENE------KK 1674
Cdd:PRK01156 398 KIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELsrnmemlngqsvcpvcgttLGEEKSNHiinhynEK 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1675 LKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKK 1754
Cdd:PRK01156 478 KSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKS 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1755 ANLQI-DQINTDLNleRSHAQKN----ENARQQLERQNKELK---AKLQEMESA---VKSKYKASIAALEAKIAQLEEQL 1823
Cdd:PRK01156 558 LKLEDlDSKRTSWL--NALAVISlidiETNRSRSNEIKKQLNdleSRLQEIEIGfpdDKSYIDKSIREIENEANNLNNKY 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1824 dNETKERQAASKQVRRAEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDA 1903
Cdd:PRK01156 636 -NEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINEL 714
|
570
....*....|....*
gi 806638593 1904 TETADAMNREVSSLK 1918
Cdd:PRK01156 715 SDRINDINETLESMK 729
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
873-1703 |
3.28e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.73 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 873 TMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLeARVEEEEErcqylQAEK-KKMQQNIQELEEQ 951
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHL-NLVQTALR-----QQEKiERYQADLEELEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 952 LEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFtTNLMEEEEKSKSLAKLKNKHEAMITD 1031
Cdd:PRK04863 364 LEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQY-QQAVQALERAKQLCGLPDLTADNAED 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1032 LEERLRREEKQR-QELEKTRRKLegdstDLSDQIAELQAQIAELKMQLAKKEEELQA------ALARVEEE---AAQKNM 1101
Cdd:PRK04863 443 WLEEFQAKEQEAtEELLSLEQKL-----SVAQAAHSQFEQAYQLVRKIAGEVSRSEAwdvareLLRRLREQrhlAEQLQQ 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1102 ALKKIRELEtQISELQEDLESERACRNKAEKQKRDLGEELEALKTELEDTLDStaAQQELRSKREQevsilKKTLEDEAK 1181
Cdd:PRK04863 518 LRMRLSELE-QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLES--LSESVSEARER-----RMALRQQLE 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1182 THEAQIQEMRQKHSQ------AVEELAEQleqtkrVKATLEKAkQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQ 1255
Cdd:PRK04863 590 QLQARIQRLAARAPAwlaaqdALARLREQ------SGEEFEDS-QDVTEYMQQLLERERELTVERDELAARKQALDEEIE 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1256 EL-QVKFSEGERVRTeLADKVSKLQVEL--DSVT--------GLLNQsdSKSSKLTKDFSALESQLQ---DTQE--LLQE 1319
Cdd:PRK04863 663 RLsQPGGSEDPRLNA-LAERFGGVLLSEiyDDVSledapyfsALYGP--ARHAIVVPDLSDAAEQLAgleDCPEdlYLIE 739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1320 ENRQKL------------SLSTKLKQMEDEKNSFREQLEEEEEAKrnlEKQIATLHAQVTDMKKKmedgvgcLETAEEAK 1387
Cdd:PRK04863 740 GDPDSFddsvfsveelekAVVVKIADRQWRYSRFPEVPLFGRAAR---EKRIEQLRAEREELAER-------YATLSFDV 809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1388 RRLQKDLEGLSQRLEEKVA-AYD-----KLEKTKTRLQQ---ELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISA 1458
Cdd:PRK04863 810 QKLQRLHQAFSRFIGSHLAvAFEadpeaELRQLNRRRVElerALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLAD 889
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1459 KYAEERdraeaeareketkalslARALEEAMEQKAELERLNKQFrtemedlmsskddvGKSVHELEKSKRAL---EQQVE 1535
Cdd:PRK04863 890 ETLADR-----------------VEEIREQLDEAEEAKRFVQQH--------------GNALAQLEPIVSVLqsdPEQFE 938
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1536 EMKTQLEELEDELQATeDAKLRLEVNLQAMKAQFE-RDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQ-RSIAMAARK 1613
Cdd:PRK04863 939 QLKQDYQQAQQTQRDA-KQQAFALTEVVQRRAHFSyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQlRQAQAQLAQ 1017
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1614 KLEMdLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELddTRASREEILAQAKEN-------EKKLKSMEAEMIQLQ 1686
Cdd:PRK04863 1018 YNQV-LASLKSSYDAKRQMLQELKQELQDLGVPADSGAEER--ARARRDELHARLSANrsrrnqlEKQLTFCEAEMDNLT 1094
|
890
....*....|....*..
gi 806638593 1687 EELAAAERAKRQAQQER 1703
Cdd:PRK04863 1095 KKLRKLERDYHEMREQV 1111
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
874-1343 |
3.81e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 55.61 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 874 MQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQYLQAEKKKmqqniqeleeqle 953
Cdd:pfam12128 598 SEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQS------------- 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 954 eeesarQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLE 1033
Cdd:pfam12128 665 ------EKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAI 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1034 ERLRREEKQRQELEKTRRKLEGDSTDLS-DQIAELQAQIAELKMQLAKKEEELQAALAR---VEEEAAQKNMALK-KIRE 1108
Cdd:pfam12128 739 AARRSGAKAELKALETWYKRDLASLGVDpDVIAKLKREIRTLERKIERIAVRRQEVLRYfdwYQETWLQRRPRLAtQLSN 818
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1109 LETQISELQEDL---ESERACRNKAEKQKRDLGEELEALKTELEDTLDStaaqqELRSKREQEVSILKKTLEDEAKTHEA 1185
Cdd:pfam12128 819 IERAISELQQQLarlIADTKLRRAKLEMERKASEKQQVRLSENLRGLRC-----EMSKLATLKEDANSEQAQGSIGERLA 893
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1186 QIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAK--QTLENERGELANEVKALLQgkgdSEHKRKKVEAQLQELQVKFSE 1263
Cdd:pfam12128 894 QLEDLKLKRDYLSESVKKYVEHFKNVIADHSGSGlaETWESLREEDHYQNDKGIR----LLDYRKLVPYLEQWFDVRVPQ 969
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1264 GERVrteLADKVSKLQVELDSVTGLL----NQSDSKSSKLTKDFSALE-----SQLQDTQELLQEEnrqkLSLSTKLKQM 1334
Cdd:pfam12128 970 SIMV---LREQVSILGVDLTEFYDVLadfdRRIASFSRELQREVGEEAffegvSESAVRIRSKVSE----LEYWPELRVF 1042
|
....*....
gi 806638593 1335 EDEKNSFRE 1343
Cdd:pfam12128 1043 VKAFRLWKS 1051
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1061-1328 |
3.92e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1061 SDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERACRNKAEKQKRDLGEE 1140
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1141 LEALKTELEDTLDstAAQqelRSKREQEVSILKKTledeakTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQ 1220
Cdd:COG4942 99 LEAQKEELAELLR--ALY---RLGRQPPLALLLSP------EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1221 TLEnergelanevkallqgkgdsehkrkkveAQLQELQVKFSEGERVRTELADKVSKLQVELDSVTGLLNQSDSKSSKLT 1300
Cdd:COG4942 168 ELE----------------------------AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
250 260
....*....|....*....|....*...
gi 806638593 1301 KDFSALESQLQDTQELLQEENRQKLSLS 1328
Cdd:COG4942 220 QEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1353-1900 |
4.08e-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: 55.14 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1353 RNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLlvdldHQ 1432
Cdd:pfam07111 76 RRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQRELEEIQRL-----HQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1433 RQSVSNLEKKQKKFDQLLAE----EKTISA---KYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTE 1505
Cdd:pfam07111 151 EQLSSLTQAHEEALSSLTSKaeglEKSLNSletKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKYVGEQ 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1506 MEDLMSS------KDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFER-------- 1571
Cdd:pfam07111 231 VPPEVHSqtweleRQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKkcrsllnr 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1572 ----------DLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSIAM------AARKKLE-MDLKDLEAHIDTANKNRE 1634
Cdd:pfam07111 311 wrekvfalmvQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQralqdkAAEVEVErMSAKGLQMELSRAQEARR 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1635 EAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEM------IQLQEELAAAERAKRQAQQERDELAD 1708
Cdd:pfam07111 391 RQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLsyavrkVHTIKGLMARKVALAQLRQESCPPPP 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1709 EIANSSGKGALALEEKR----------RLEARIAQLEEELEEEQGNTEliNDRLKKANLQIDQ---------INTDLNLE 1769
Cdd:pfam07111 471 PAPPVDADLSLELEQLReernrldaelQLSAHLIQQEVGRAREQGEAE--RQQLSEVAQQLEQelqraqeslASVGQQLE 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1770 RSHAQKNE------NARQQLERQNKELKAKLQEMESAVKSKYKASIAALEAKIAQL-EEQLDNETKERQAASKQVRraEK 1842
Cdd:pfam07111 549 VARQGQQEsteeaaSLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEArREQAKAVVSLRQIQHRATQ--EK 626
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 806638593 1843 KLKDVLLQVEDERRnaeqfKDQADKASTRLKQLKR-QLEEAEEEAQRANASRRKLQREL 1900
Cdd:pfam07111 627 ERNQELRRLQDEAR-----KEEGQRLARRVQELERdKNLMLATLQQEGLLSRYKQQRLL 680
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1141-1602 |
4.31e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1141 LEALKTELEDTLDstAAQQELRSKREQEVSILKKTLEDEakthEAQIQEMRQKHSQaVEELAEQLEQTKRVKATLEKAKQ 1220
Cdd:COG4717 40 LAFIRAMLLERLE--KEADELFKPQGRKPELNLKELKEL----EEELKEAEEKEEE-YAELQEELEELEEELEELEAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1221 TLENERGELANEVKA--LLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELA---DKVSKLQVELDSVTGLLNQSDSK 1295
Cdd:COG4717 113 ELREELEKLEKLLQLlpLYQELEALEAELAELPERLEELEERLEELRELEEELEeleAELAELQEELEELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1296 S-SKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKnsFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKME 1374
Cdd:COG4717 193 ElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL--EAAALEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1375 DGVGCLETA-------EEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFD 1447
Cdd:COG4717 271 LILTIAGVLflvlgllALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1448 QLLAEEKTISAKYAEERDRAEAEAREKETKA------LSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKsvH 1521
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAALLAEAGVedeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--E 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1522 ELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLE--VNLQAMKAQFERDLQGRDEQSEE-KKKQLVRQV-REMEAE 1597
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAELRELAEEwAALKLALELlEEAREE 508
|
....*
gi 806638593 1598 LEDER 1602
Cdd:COG4717 509 YREER 513
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1085-1310 |
4.72e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1085 LQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERACRNKAEKQKRDLGEELEALKTEL---EDTLDSTAAQQ-E 1160
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELaalEAELAELEKEIaE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1161 LRSKREQEVSILKKTLEDEAKTHE-------------AQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQTLENERG 1227
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1228 ELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVSKLQVELDSVTGLLNQSDSKSSklTKDFSALE 1307
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP--AAGFAALK 252
|
...
gi 806638593 1308 SQL 1310
Cdd:COG4942 253 GKL 255
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
897-1335 |
6.01e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 54.75 E-value: 6.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 897 AEAEELRARLTAKKQELE--EICH-----DLEARVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQK----LQLE 965
Cdd:pfam05557 2 AELIESKARLSQLQNEKKqmELEHkrariELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREqaelNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 966 KVTTEAKLKKLEEDqiimEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLaklknKHEAMitDLEERLRREEKQRQE 1045
Cdd:pfam05557 82 KKYLEALNKKLNEK----ESQLADAREVISCLKNELSELRRQIQRAELELQST-----NSELE--ELQERLDLLKAKASE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1046 LEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEE------------ELQAALARVEEEAAQKNMALKKIRELETQI 1113
Cdd:pfam05557 151 AEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIvknskselaripELEKELERLREHNKHLNENIENKLLLKEEV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1114 SELQEDLESERACRNKA---EKQKRDLGEELEALKTELEDTLDSTAAQQELRSK------REQEVSILKKTLEDEAKTHE 1184
Cdd:pfam05557 231 EDLKRKLEREEKYREEAatlELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRieqlqqREIVLKEENSSLTSSARQLE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1185 AQIQEMRQKHSQA---VEELAEQLEQTKRVKATLEKAKQTLENERG-------------ELANEVKALLQGKGDSEHKRK 1248
Cdd:pfam05557 311 KARRELEQELAQYlkkIEDLNKKLKRHKALVRRLQRRVLLLTKERDgyrailesydkelTMSNYSPQLLERIEEAEDMTQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1249 KVEAQLQELQVKFSEGERVRTELADKVSKLQVELDSVTGLLNQSDSKSSKltKDFSALESQLQDTQELLQEENRQKLSLS 1328
Cdd:pfam05557 391 KMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSK--EEVDSLRRKLETLELERQRLREQKNELE 468
|
....*..
gi 806638593 1329 TKLKQME 1335
Cdd:pfam05557 469 MELERRC 475
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1440-1922 |
6.27e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.84 E-value: 6.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1440 EKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKEtkalslaraleeamEQKAELERLNKQFRTEmedlmssKDDVGKS 1519
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQE--------------ERQETSAELNQLLRTL-------DDQWKEK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1520 VHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLqgrdEQSEEKKKQLVRQVREMEAELE 1599
Cdd:pfam12128 303 RDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSEL----ENLEERLKALTGKHQDVTAKYN 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1600 DERKQRSIAMAArkKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMrelddtrasrEEILAQAKENEKKLKSME 1679
Cdd:pfam12128 379 RRRSKIKEQNNR--DIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQL----------EAGKLEFNEEEYRLKSRL 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1680 AEMIQLQEELAAAERAKRQ--AQQERDELADEIANSSGKGALALE-EKRRLEARIAQLEEELEEEQGNTELINDRLKKAN 1756
Cdd:pfam12128 447 GELKLRLNQATATPELLLQleNFDERIERAREEQEAANAEVERLQsELRQARKRRDQASEALRQASRRLEERQSALDELE 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1757 LQID-QINTDLNLERSHAQKNEN------ARQQLERQNKE----------------LKAKLQEMESavkSKYKASIAALE 1813
Cdd:pfam12128 527 LQLFpQAGTLLHFLRKEAPDWEQsigkviSPELLHRTDLDpevwdgsvggelnlygVKLDLKRIDV---PEWAASEEELR 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1814 AKIAQLEEQLDNETKERQAASKQVRRAEKKLkdvllqvederrnaeqfkdqaDKASTRLKQLKRQLEEAEEEAQRANASR 1893
Cdd:pfam12128 604 ERLDKAEEALQSAREKQAAAEEQLVQANGEL---------------------EKASREETFARTALKNARLDLRRLFDEK 662
|
490 500 510
....*....|....*....|....*....|
gi 806638593 1894 RKLQRELEDATETA-DAMNREVSSLKNKLR 1922
Cdd:pfam12128 663 QSEKDKKNKALAERkDSANERLNSLEAQLK 692
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
795-1277 |
7.53e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 7.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 795 ARKAFAKRQQQLTAMKVLQRNCAAYLRLRN-----------WQWWRLFTKVKPLLNSIRHEDELLAK-EAELTKVREKHL 862
Cdd:COG4913 240 AHEALEDAREQIELLEPIRELAERYAAARErlaeleylraaLRLWFAQRRLELLEAELEELRAELARlEAELERLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 863 AAENRLTEMETmqsQLMAEKLQLQEQLQAEtelCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQYLQAEKKKMQ 942
Cdd:COG4913 320 ALREELDELEA---QIRGNGGDRLEQLERE---IERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 943 QNIQELEEQLEEE----ESARQKLQLEKVTTEAKLKKLE-------EDQIIMEDQnckLAKEKKLLEDR---VAE----- 1003
Cdd:COG4913 394 EALEEELEALEEAlaeaEAALRDLRRELRELEAEIASLErrksnipARLLALRDA---LAEALGLDEAElpfVGElievr 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1004 ----------------FTTNLMEEEEKSKSLAKLKNKHeamitDLEERLRREEKQRQELEKTRRKLEGDStdLSDQIA-E 1066
Cdd:COG4913 471 peeerwrgaiervlggFALTLLVPPEHYAAALRWVNRL-----HLRGRLVYERVRTGLPDPERPRLDPDS--LAGKLDfK 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1067 LQAQIAELKMQLAKK--------EEELQ--------AALARVEEEAAQKNM-------------ALKKIRELETQISELQ 1117
Cdd:COG4913 544 PHPFRAWLEAELGRRfdyvcvdsPEELRrhpraitrAGQVKGNGTRHEKDDrrrirsryvlgfdNRAKLAALEAELAELE 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1118 EDLESERACRNKAEKQKRDLGEELEALKTELE---DTLDSTAAQQELRSKREQ---------EVSILKKTLED---EAKT 1182
Cdd:COG4913 624 EELAEAEERLEALEAELDALQERREALQRLAEyswDEIDVASAEREIAELEAElerldassdDLAALEEQLEEleaELEE 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1183 HEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQvkfS 1262
Cdd:COG4913 704 LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALR---A 780
|
570
....*....|....*
gi 806638593 1263 EGERVRTELADKVSK 1277
Cdd:COG4913 781 RLNRAEEELERAMRA 795
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
978-1803 |
9.69e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 54.29 E-value: 9.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 978 EDQIIMEDQNCKLAKE-KKLLEDRVAEFTTNLMEEEEKskslaklKNKHEAMITDLEERLRRE-----EKQRQELEKTRR 1051
Cdd:TIGR01612 693 EDKAKLDDLKSKIDKEyDKIQNMETATVELHLSNIENK-------KNELLDIIVEIKKHIHGEinkdlNKILEDFKNKEK 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1052 KLEGDSTDLS---DQIAELQAQIAELKMQLAKkeeelQAALARVEEEAAQKNMALKK-------IRELET-----QISEL 1116
Cdd:TIGR01612 766 ELSNKINDYAkekDELNKYKSKISEIKNHYND-----QINIDNIKDEDAKQNYDKSKeyiktisIKEDEIfkiinEMKFM 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1117 QEDLES--------ERACRNKAEKQKRDLGEELEALKTELEDTL---------DSTAAQQELRSKREQE---VSILKKTL 1176
Cdd:TIGR01612 841 KDDFLNkvdkfinfENNCKEKIDSEHEQFAELTNKIKAEISDDKlndyekkfnDSKSLINEINKSIEEEyqnINTLKKVD 920
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1177 E--DEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRV----KATLEKAKQTLENERGELANEVKALlqGKGDSEHKRKKV 1250
Cdd:TIGR01612 921 EyiKICENTKESIEKFHNKQNILKEILNKNIDTIKESnlieKSYKDKFDNTLIDKINELDKAFKDA--SLNDYEAKNNEL 998
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1251 EAQLQELQV------------KFSEGERVRTELADKVSKLQ-----VELDSVTGLLNQSDSKSSKLTKDFSALESQLQDT 1313
Cdd:TIGR01612 999 IKYFNDLKAnlgknkenmlyhQFDEKEKATNDIEQKIEDANknipnIEIAIHTSIYNIIDEIEKEIGKNIELLNKEILEE 1078
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1314 QELlQEENRQKLSLSTKLKQMED---EKN-SFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLET------- 1382
Cdd:TIGR01612 1079 AEI-NITNFNEIKEKLKHYNFDDfgkEENiKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAqindled 1157
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1383 ------AEEAKRRLQKDLEGLSQRLEEKVAAYD----------KLEKTKTRLQQEL---------------DDLLVDLDH 1431
Cdd:TIGR01612 1158 vadkaiSNDDPEEIEKKIENIVTKIDKKKNIYDeikkllneiaEIEKDKTSLEEVKginlsygknlgklflEKIDEEKKK 1237
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1432 QRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERD-RAEAEA--------------REKETKALSLAR----ALEEAMEQK 1492
Cdd:TIGR01612 1238 SEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDiKAEMETfnishdddkdhhiiSKKHDENISDIRekslKIIEDFSEE 1317
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1493 AELERLNKQFRTEMEDLMSSKDDVGKSVHE---------LEKSKRALEQqVEEMKTQLEE----LEDELQATED--AKLR 1557
Cdd:TIGR01612 1318 SDINDIKKELQKNLLDAQKHNSDINLYLNEianiynilkLNKIKKIIDE-VKEYTKEIEEnnknIKDELDKSEKliKKIK 1396
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1558 LEVNLQAMKAQFERDLQGRD-----EQSEEKKKQLVRQVREMEAELEDERKQ--------RSIAMAARKK---------- 1614
Cdd:TIGR01612 1397 DDINLEECKSKIESTLDDKDideciKKIKELKNHILSEESNIDTYFKNADENnenvlllfKNIEMADNKSqhilkikkdn 1476
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1615 ----LEMDLKDLEAHIDTANKNREEAIKQLRKLQA------QMKDCMREL-------------DDTRASREEILAQAKEN 1671
Cdd:TIGR01612 1477 atndHDFNINELKEHIDKSKGCKDEADKNAKAIEKnkelfeQYKKDVTELlnkysalaiknkfAKTKKDSEIIIKEIKDA 1556
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1672 EKKLkSMEAEmiqlqeelaAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEA------RIAQLEEELEEEQGNT 1745
Cdd:TIGR01612 1557 HKKF-ILEAE---------KSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENfenkflKISDIKKKINDCLKET 1626
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 806638593 1746 ELINDRLkkANLQIDQINTDLNLERSHAQKNENARQQLERQNKEL---KAKLQEMESAVKS 1803
Cdd:TIGR01612 1627 ESIEKKI--SSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIedkKKELDELDSEIEK 1685
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
963-1297 |
9.75e-07 |
|
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: 53.81 E-value: 9.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 963 QLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQ 1042
Cdd:COG5185 225 AKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKS 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1043 RQELEKTRRKLEgdstdlsdqiaelQAQIAELKMQLAKKEEELQAALARVEEEAAQKNmalkkiRELETQISELQEDLES 1122
Cdd:COG5185 305 IDIKKATESLEE-------------QLAAAEAEQELEESKRETETGIQNLTAEIEQGQ------ESLTENLEAIKEEIEN 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1123 ERACRNKAEKQkrdlgEELEALKTELEDTLDSTAAQQELRSKREQEvsiLKKTLEDEAKTHEAQIQEMRQKHSQAVEELA 1202
Cdd:COG5185 366 IVGEVELSKSS-----EELDSFKDTIESTKESLDEIPQNQRGYAQE---ILATLEDTLKAADRQIEELQRQIEQATSSNE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1203 EQLEQ--------TKRVKATLEKAKQTLENERGELANEVKallQGKGDSEHKRKKVEAQLQELQvkfSEGERVRTELADK 1274
Cdd:COG5185 438 EVSKLlneliselNKVMREADEESQSRLEEAYDEINRSVR---SKKEDLNEELTQIESRVSTLK---ATLEKLRAKLERQ 511
|
330 340
....*....|....*....|...
gi 806638593 1275 VSKLQVELDSVTGLLNQSDSKSS 1297
Cdd:COG5185 512 LEGVRSKLDQVAESLKDFMRARG 534
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1116-1340 |
1.03e-06 |
|
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: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1116 LQEDLESERAcrnKAEKQKRDLGEELEALKTELEdtldstAAQQELRSKREQEVSIlkkTLEDEAKTHEAQIQEMRQKHS 1195
Cdd:COG3206 162 LEQNLELRRE---EARKALEFLEEQLPELRKELE------EAEAALEEFRQKNGLV---DLSEEAKLLLQQLSELESQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1196 QAVEELAEQLEQTKRVKATLEKAK------------QTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKF-S 1262
Cdd:COG3206 230 EARAELAEAEARLAALRAQLGSGPdalpellqspviQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLqQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1263 EGERVRTELADKVSKLQVELDSVTGLLNQSDSKSSKLTK---DFSALESQLQDTQELLQeenrqklSLSTKLKQMEDEKN 1339
Cdd:COG3206 310 EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEleaELRRLEREVEVARELYE-------SLLQRLEEARLAEA 382
|
.
gi 806638593 1340 S 1340
Cdd:COG3206 383 L 383
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1018-1152 |
1.10e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 53.71 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1018 LAKLKNKHEAmiTDLEERLRREEKQRQELEKTRRKLEgdstDLSDQIAELQAQIAELKMQLAKKE---EELQAALARVEE 1094
Cdd:COG2433 382 LEELIEKELP--EEEPEAEREKEHEERELTEEEEEIR----RLEEQVERLEAEVEELEAELEEKDeriERLERELSEARS 455
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 806638593 1095 EAAQKNMALKKIRELETQISELQEDLESEracRNKAEKQKRDLGEELEALKTELEDTL 1152
Cdd:COG2433 456 EERREIRKDREISRLDREIERLERELEEE---RERIEELKRKLERLKELWKLEHSGEL 510
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
899-1287 |
1.29e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 53.36 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 899 AEELRARLTAKKQELEEICHDLEARVEEEEERCQYLQAEKKKMQqniqeleEQLEEEESARQKLQLEKVTTEAKLKKLEE 978
Cdd:pfam07888 29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE-------RQRRELESRVAELKEELRQSREKHEELEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 979 DQIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDST 1058
Cdd:pfam07888 102 KYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1059 DLSDQIAELQAQIAELKMQLAKKEEELQaalaRVEEEAAQKNMALKKIRELETQISELQEDLESERACRNKAEKQKRDLG 1138
Cdd:pfam07888 182 QTEEELRSLSKEFQELRNSLAQRDTQVL----QLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1139 EELEALKTELEDTldstaaQQELRSKREQ--EVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEqtkRVKATLE 1216
Cdd:pfam07888 258 EELSSMAAQRDRT------QAELHQARLQaaQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIE---KLSAELQ 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 806638593 1217 KAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQE----LQVKFSEGERVRT---ELADKVSKLQVELDSVTG 1287
Cdd:pfam07888 329 RLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQElkasLRVAQKEKEQLQAekqELLEYIRQLEQRLETVAD 406
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1102-1922 |
1.44e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 53.51 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1102 ALKKIRELETQISELQEDLESERACRNKAEKQKRDLGEELEALKT------ELEDTLDSTAAQQElrskREQEVSILKKT 1175
Cdd:TIGR00606 170 ALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQykekacEIRDQITSKEAQLE----SSREIVKSYEN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1176 LEDEAKTHEAQIQEMRQKhsqaVEELAEQLEQTKRVKATLEKAKQTLENER-------GELANEVKALLQGKGDS-EHKR 1247
Cdd:TIGR00606 246 ELDPLKNRLKEIEHNLSK----IMKLDNEIKALKSRKKQMEKDNSELELKMekvfqgtDEQLNDLYHNHQRTVREkEREL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1248 KKVEAQLQELQVKFSEGERVRTELADKVSKLQVELDSVtgllnQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSL 1327
Cdd:TIGR00606 322 VDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRH-----QEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFH 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1328 STKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEA---KRRLQKDLEGLSQRLEEK 1404
Cdd:TIGR00606 397 TLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEElkfVIKELQQLEGSSDRILEL 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1405 VAAYDKLEKTKTRLQQElddllvdldhqrqsvSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKET--KALSLA 1482
Cdd:TIGR00606 477 DQELRKAERELSKAEKN---------------SLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTrtQMEMLT 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1483 RALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEdelqatedaklrlevnl 1562
Cdd:TIGR00606 542 KDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLE----------------- 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1563 qAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERkqrsiamaARKKLEMDLKDLeAHIDTANKNREEAIKQLRK 1642
Cdd:TIGR00606 605 -QNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLER--------LKEEIEKSSKQR-AMLAGATAVYSQFITQLTD 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1643 lqaQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALE 1722
Cdd:TIGR00606 675 ---ENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRN 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1723 EKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTdlnLERSHAQKNEN----ARQQLERQNKELKAKLQEME 1798
Cdd:TIGR00606 752 KLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTI---MERFQMELKDVerkiAQQAAKLQGSDLDRTVQQVN 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1799 SAVKSKYKASiaaleAKIAQLEEQLDNETKERQAASKQVRRAEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQ 1878
Cdd:TIGR00606 829 QEKQEKQHEL-----DTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIRE 903
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 806638593 1879 LEEAEEEAQRANASRRKLQRELEDATETADAMNR----EVSSLKNKLR 1922
Cdd:TIGR00606 904 IKDAKEQDSPLETFLEKDQQEKEELISSKETSNKkaqdKVNDIKEKVK 951
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
898-1512 |
1.46e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 53.69 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 898 EAEELRARLTAKKQELEEICH------DLEARVEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTT-E 970
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHlhfgykSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKdR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 971 AKLKKLEEDQIIMEDQNCKLAK-----------EKKLLEDRVAEFTTNLMEEEEKSKSL-AKLKNKHEAMITDLEERL-- 1036
Cdd:pfam12128 322 SELEALEDQHGAFLDADIETAAadqeqlpswqsELENLEERLKALTGKHQDVTAKYNRRrSKIKEQNNRDIAGIKDKLak 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1037 RREEKQRQeLEKTRRKLEGDSTDLSDQI--AELQAQIAELKMQLAKKEEELQAALARVEEEA----AQKNMALKKIRELE 1110
Cdd:pfam12128 402 IREARDRQ-LAVAEDDLQALESELREQLeaGKLEFNEEEYRLKSRLGELKLRLNQATATPELllqlENFDERIERAREEQ 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1111 TQISELQEDLESE-RACRNKAEKQKRDLGE----------ELEALK---------------------------------- 1145
Cdd:pfam12128 481 EAANAEVERLQSElRQARKRRDQASEALRQasrrleerqsALDELElqlfpqagtllhflrkeapdweqsigkvispell 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1146 --TELEDTLDSTAAQQE-------LRSKREQ--EVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKAT 1214
Cdd:pfam12128 561 hrTDLDPEVWDGSVGGElnlygvkLDLKRIDvpEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASRE 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1215 LEKAKQTLENER---GELANEV--------KALLQGKGDSEHKRKKVEAQLQELQVKFSEG-ERVRTELADKVSKLQVEL 1282
Cdd:pfam12128 641 ETFARTALKNARldlRRLFDEKqsekdkknKALAERKDSANERLNSLEAQLKQLDKKHQAWlEEQKEQKREARTEKQAYW 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1283 DSVTGLLnqsDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSlstklKQMEDEKNSFReqleeeeeakrnLEKQIATL 1362
Cdd:pfam12128 721 QVVEGAL---DAQLALLKAAIAARRSGAKAELKALETWYKRDLA-----SLGVDPDVIAK------------LKREIRTL 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1363 HAQVTDMKKKMEDG----VGCLETAEEAKRRLQKDLEGLSQRLEEkvaaydkLEKTKTRLQQELDDLLVDLDHQRQSvsn 1438
Cdd:pfam12128 781 ERKIERIAVRRQEVlryfDWYQETWLQRRPRLATQLSNIERAISE-------LQQQLARLIADTKLRRAKLEMERKA--- 850
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 806638593 1439 LEKKQKKFDQLLAEEKTISAKYAEER-----DRAEAEAREKETKALSLARALEEAMEQkaeLERLNKQFRTEMEDLMSS 1512
Cdd:pfam12128 851 SEKQQVRLSENLRGLRCEMSKLATLKedansEQAQGSIGERLAQLEDLKLKRDYLSES---VKKYVEHFKNVIADHSGS 926
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
842-1693 |
1.48e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.80 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 842 RHEDELLAKEAELTKVREKHLAAENRLTEMetmqsqlmAEKLQLQEQLQA--ETELCAEAEELRARLTAKKQ-------- 911
Cdd:COG3096 282 ELSERALELRRELFGARRQLAEEQYRLVEM--------ARELEELSARESdlEQDYQAASDHLNLVQTALRQqekieryq 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 912 -ELEEICHDLEAR---VEEEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMedQN 987
Cdd:COG3096 354 eDLEELTERLEEQeevVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALC--GL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 988 CKLAKEKklLEDRVAEFTtnlmeeeekskslAKLKNKHEAMItDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAEL 1067
Cdd:COG3096 432 PDLTPEN--AEDYLAAFR-------------AKEQQATEEVL-ELEQKLSVADAARRQFEKAYELVCKIAGEVERSQAWQ 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1068 QAQiaelkmQLAKKEEELQAALARVEEEAAQknmalkkIRELEtQISELQEDLESERACRNKAEKQKRDLGEELEALKTE 1147
Cdd:COG3096 496 TAR------ELLRRYRSQQALAQRLQQLRAQ-------LAELE-QRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1148 LEDTLDStaAQQELRSKREQevsilKKTLEDEAKTHEAQIQEMRQKH------SQAVEELAEQLEQT-KRVKATLEKAKQ 1220
Cdd:COG3096 562 LEAQLEE--LEEQAAEAVEQ-----RSELRQQLEQLRARIKELAARApawlaaQDALERLREQSGEAlADSQEVTAAMQQ 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1221 TLENERG-------------ELANEVKALLQGKG--DSEHKRKK------------------------------------ 1249
Cdd:COG3096 635 LLEREREatverdelaarkqALESQIERLSQPGGaeDPRLLALAerlggvllseiyddvtledapyfsalygparhaivv 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1250 -----VEAQLQELQ-----VKFSEGE--------RVRTELADKV-----------------------------SKLQVEL 1282
Cdd:COG3096 715 pdlsaVKEQLAGLEdcpedLYLIEGDpdsfddsvFDAEELEDAVvvklsdrqwrysrfpevplfgraarekrlEELRAER 794
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1283 DSVTGLLNQSD---SKSSKLTKDFSALESQ------LQDTQELLQEENRQklslstkLKQMEDEKNSFREQLEEEEEAKR 1353
Cdd:COG3096 795 DELAEQYAKASfdvQKLQRLHQAFSQFVGGhlavafAPDPEAELAALRQR-------RSELERELAQHRAQEQQLRQQLD 867
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1354 NLEKQIATLHAQV--------TDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQrLEEKVAAYDKLEKTKTRLQQELDDL 1425
Cdd:COG3096 868 QLKEQLQLLNKLLpqanlladETLADRLEELREELDAAQEAQAFIQQHGKALAQ-LEPLVAVLQSDPEQFEQLQADYLQA 946
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1426 LVDLDHQRQSVSNLEkkqkkfdqllaeektisakyaEERDRAEAEAREKETKALSLARALEEAMEQK---AELERLnkQF 1502
Cdd:COG3096 947 KEQQRRLKQQIFALS---------------------EVVQRRPHFSYEDAVGLLGENSDLNEKLRARleqAEEARR--EA 1003
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1503 RTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEdeLQATEDAKLRLEVNLQAMKAQFERDLQGRDE---- 1578
Cdd:COG3096 1004 REQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELG--VQADAEAEERARIRRDELHEELSQNRSRRSQlekq 1081
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1579 --QSEEKKKQLVRQVREMEAELEDERKQ---------RSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQ--- 1644
Cdd:COG3096 1082 ltRCEAEMDSLQKRLRKAERDYKQEREQvvqakagwcAVLRLARDNDVERRLHRRELAYLSADELRSMSDKALGALRlav 1161
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 806638593 1645 ---AQMKDCMRELDDTRAS--------------REEILAQAKENE---KKLKSMEAEMIQLQEELAAAE 1693
Cdd:COG3096 1162 adnEHLRDALRLSEDPRRPerkvqfyiavyqhlRERIRQDIIRTDdpvEAIEQMEIELARLTEELTSRE 1230
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1538-1844 |
1.79e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 53.03 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1538 KTQLEELEDELQATEDAKLRLEvnlqAMKAQFERDLQGRdeqsEEKKKQLVRQVRemeAELEDERkQRSIAMAARKKLEM 1617
Cdd:PRK05035 435 KAEIRAIEQEKKKAEEAKARFE----ARQARLEREKAAR----EARHKKAAEARA---AKDKDAV-AAALARVKAKKAAA 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1618 DLKDLEAHIDTANKNREEAIKQLRKLQAqmkdcmrelddtRASREEILAQAKENEKKLKsmeaemIQlqeelAAAERAK- 1696
Cdd:PRK05035 503 TQPIVIKAGARPDNSAVIAAREARKAQA------------RARQAEKQAAAAADPKKAA------VA-----AAIARAKa 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1697 RQAQQERDELADEIANSSGKGALAlEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIdqintdlnlershaqkn 1776
Cdd:PRK05035 560 KKAAQQAANAEAEEEVDPKKAAVA-AAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAI----------------- 621
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 806638593 1777 enARQQLERQNKELKAKLQEMESAVKSKYKASIAALEAKIAQLEEQLDNET------KERQAASkqVRRAEKKL 1844
Cdd:PRK05035 622 --ARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEeaedpkKAAVAAA--IARAKAKK 691
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
958-1170 |
1.89e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 958 ARQKLQlekvTTEAKLKKLEEDQIIMEdqnckLAKEKKLLEDRVAEFTT-------NLMEEEEKSKSLAKLKNKHEAMIT 1030
Cdd:COG3206 187 LRKELE----EAEAALEEFRQKNGLVD-----LSEEAKLLLQQLSELESqlaearaELAEAEARLAALRAQLGSGPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1031 DLEE--RLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLakkEEELQAALARVEEEAAQknmALKKIRE 1108
Cdd:COG3206 258 ELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL---QQEAQRILASLEAELEA---LQAREAS 331
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 806638593 1109 LETQISELQEDLESEracrNKAEKQKRDLGEELEALKTELEDTLdstAAQQELRSKREQEVS 1170
Cdd:COG3206 332 LQAQLAQLEARLAEL----PELEAELRRLEREVEVARELYESLL---QRLEEARLAEALTVG 386
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1065-1362 |
1.95e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.99 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1065 AELQAQIAELKMQlaKKEEELQAALARVEEEAAQknmALKKIRELETQISELQEDLEseracrnKAEKQKRDLGEELEAL 1144
Cdd:PRK11281 39 ADVQAQLDALNKQ--KLLEAEDKLVQQDLEQTLA---LLDKIDRQKEETEQLKQQLA-------QAPAKLRQAQAELEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1145 KTELEDTLDSTAAQQELRskreqevsilkkTLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQTLEn 1224
Cdd:PRK11281 107 KDDNDEETRETLSTLSLR------------QLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQ- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1225 ergELANEVKALLQGKGDSEHKRK-KVEAQLQ--ELQVKFSE------------GERVRTELADKVSKLQVELDSVTGLL 1289
Cdd:PRK11281 174 ---QIRNLLKGGKVGGKALRPSQRvLLQAEQAllNAQNDLQRkslegntqlqdlLQKQRDYLTARIQRLEHQLQLLQEAI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1290 NQSDSKSS--KLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSF-------REQLEEEEEAKRNLEKQIA 1360
Cdd:PRK11281 251 NSKRLTLSekTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLLKATEKLNTLtqqnlrvKNWLDRLTQSERNIKEQIS 330
|
..
gi 806638593 1361 TL 1362
Cdd:PRK11281 331 VL 332
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1491-1920 |
2.15e-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: 52.72 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1491 QKAELERLNKQFRTEMEDLMSSKD---DVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKA 1567
Cdd:TIGR04523 31 QDTEEKQLEKKLKTIKNELKNKEKelkNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1568 QFERDLQGRDEQSEEKKKqlvrqvreMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQM 1647
Cdd:TIGR04523 111 EIKNDKEQKNKLEVELNK--------LEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1648 KDCMRELDDTRASR---EEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEK 1724
Cdd:TIGR04523 183 LNIQKNIDKIKNKLlklELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1725 RRLEARIAQLeeeleeeQGNTELINDRLKKANLQIDQINTDLnlERSHAQKNENARQQLERQNKELKAKLQEMESAVkSK 1804
Cdd:TIGR04523 263 NKIKKQLSEK-------QKELEQNNKKIKELEKQLNQLKSEI--SDLNNQKEQDWNKELKSELKNQEKKLEEIQNQI-SQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1805 YKASIAALEAKIAQLEEQLDNETKERQAASKQVRRAEKKLKDVL--------------LQVEDERRNAEQFKDQADKAST 1870
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKkenqsykqeiknleSQINDLESKIQNQEKLNQQKDE 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 806638593 1871 RLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNK 1920
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNT 462
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1337-1733 |
2.24e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.03 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1337 EKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGvgcletaEEAKRRLQKDLEglsqrleekvAAYDKLEKTKT 1416
Cdd:COG3096 279 ERRELSERALELRRELFGARRQLAEEQYRLVEMARELEEL-------SARESDLEQDYQ----------AASDHLNLVQT 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1417 RLQQELDDLlvdldHQRQSVSNLEKKqkkfdqlLAEEKTISAKYAEERDRAEAEAREKETKALSLARALeeAMEQKA--E 1494
Cdd:COG3096 342 ALRQQEKIE-----RYQEDLEELTER-------LEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL--ADYQQAldV 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1495 LERLNKQFRtemedlmsskddvgKSVHELEKSKRALEQ---QVEEMKTQLEELEDELQATEDAKLRLEVNL---QAMKAQ 1568
Cdd:COG3096 408 QQTRAIQYQ--------------QAVQALEKARALCGLpdlTPENAEDYLAAFRAKEQQATEEVLELEQKLsvaDAARRQ 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1569 FERDLQ------GRDEQSE--EKKKQLVRQVRE----------MEAELEDERKQRSIAMAARKKLE----------MDLK 1620
Cdd:COG3096 474 FEKAYElvckiaGEVERSQawQTARELLRRYRSqqalaqrlqqLRAQLAELEQRLRQQQNAERLLEefcqrigqqlDAAE 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1621 DLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAE------- 1693
Cdd:COG3096 554 ELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQevtaamq 633
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 806638593 1694 ---RAKRQAQQERDELAdeianssgkgalalEEKRRLEARIAQ 1733
Cdd:COG3096 634 qllEREREATVERDELA--------------ARKQALESQIER 662
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
993-1218 |
2.43e-06 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 53.01 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 993 EKKLLEDRvaeftTNLMEEEEKSKSLAklknkhEAMITDLEERLRREEKQRQELEKTRR-----------KLEGDSTDLs 1061
Cdd:PLN03188 1046 EKKLEQER-----LRWTEAESKWISLA------EELRTELDASRALAEKQKHELDTEKRcaeelkeamqmAMEGHARML- 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1062 DQIAELQaqiaELKMQLAKKEEELQAALARVEEEAAQ---KNMALKKIRELETQISELQedleSERacrnkaEKQKRDLG 1138
Cdd:PLN03188 1114 EQYADLE----EKHIQLLARHRRIQEGIDDVKKAAARagvRGAESKFINALAAEISALK----VER------EKERRYLR 1179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1139 EELEALKTELEDTLDSTAAQQEL--RSKREQEVSIL--KKTLEDEAKTHEA--QIQEMRQKHSQAVEELAEQLEQTKRVK 1212
Cdd:PLN03188 1180 DENKSLQAQLRDTAEAVQAAGELlvRLKEAEEALTVaqKRAMDAEQEAAEAykQIDKLKRKHENEISTLNQLVAESRLPK 1259
|
....*.
gi 806638593 1213 ATLEKA 1218
Cdd:PLN03188 1260 EAIRPA 1265
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1462-1704 |
2.68e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.45 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1462 EERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQL 1541
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1542 EELEDELQATEDAKLRLEvNLQAMKAQFERDLQGRDeQSEEKKKQLVRQVREMEAELEDERKQRSIAMAARKKLEmDLKD 1621
Cdd:COG1340 95 DELRKELAELNKAGGSID-KLRKEIERLEWRQQTEV-LSPEEEKELVEKIKELEKELEKAKKALEKNEKLKELRA-ELKE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1622 LEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEEL------------ 1689
Cdd:COG1340 172 LRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELrelrkelkklrk 251
|
250
....*....|....*..
gi 806638593 1690 --AAAERAKRQAQQERD 1704
Cdd:COG1340 252 kqRALKREKEKEELEEK 268
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1466-1879 |
2.76e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.65 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1466 RAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDD------------------------VGKSVH 1521
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDleqdyqaasdhlnlvqtalrqqekIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1522 ELEKSKRALEQQ---VEEMKTQLEELEDELQATEDAKLRLEVNL----QAMKAQFERDLQGRDE-QSEEKKKQL------ 1587
Cdd:PRK04863 356 DLEELEERLEEQnevVEEADEQQEENEARAEAAEEEVDELKSQLadyqQALDVQQTRAIQYQQAvQALERAKQLcglpdl 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1588 -VRQVREMEAELEDERKQrsiAMAARKKLEMDLKDLEAhidtANKNREEAIKQLRKLQAQMkdcmrelddtraSREEILA 1666
Cdd:PRK04863 436 tADNAEDWLEEFQAKEQE---ATEELLSLEQKLSVAQA----AHSQFEQAYQLVRKIAGEV------------SRSEAWD 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1667 QAKENEKKLKSMEAEMIQLQE---ELAAAERAKRQaQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEeleeeqg 1743
Cdd:PRK04863 497 VARELLRRLREQRHLAEQLQQlrmRLSELEQRLRQ-QQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLE------- 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1744 ntelindrlkkanlqidqintDLNLERSHAQKNenaRQQLERQNKELKAKLQEMEsavkSKYKASIAALEAkIAQLEEQL 1823
Cdd:PRK04863 569 ---------------------SLSESVSEARER---RMALRQQLEQLQARIQRLA----ARAPAWLAAQDA-LARLREQS 619
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 806638593 1824 DNETKERQAASKQVRRAEKKLKDVLLQVEDERRNAEQFKDQADKAS-------TRLKQLKRQL 1879
Cdd:PRK04863 620 GEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSqpggsedPRLNALAERF 682
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1432-1800 |
2.77e-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: 52.43 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1432 QRQSVSNLEKKQKKFDqllaeektisaKYAEERDRAEAEAREKEtkalslaraleeaMEQKAELERLNKQFRTEMEDlms 1511
Cdd:pfam17380 279 QHQKAVSERQQQEKFE-----------KMEQERLRQEKEEKARE-------------VERRRKLEEAEKARQAEMDR--- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1512 skddvgKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLrlevnlqAMKAQFERDLQgRDEQSEEKKKQLVRQv 1591
Cdd:pfam17380 332 ------QAAIYAEQERMAMERERELERIRQEERKRELERIRQEEI-------AMEISRMRELE-RLQMERQQKNERVRQ- 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1592 remeaELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKEN 1671
Cdd:pfam17380 397 -----ELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1672 EKKLKSmeaemiqlqeELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRR-LEARIAQLEEELEEEQGNTELIND 1750
Cdd:pfam17380 472 RKRKKL----------ELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKlLEKEMEERQKAIYEEERRREAEEE 541
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 806638593 1751 RLKKANL----QIDQINTDLNLERSHAQKNENARQQLeRQNKELKAKLQEMESA 1800
Cdd:pfam17380 542 RRKQQEMeerrRIQEQMRKATEERSRLEAMEREREMM-RQIVESEKARAEYEAT 594
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1026-1160 |
3.28e-06 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 51.39 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1026 EAMITDLEERLRRE--EKQRQELEKTRRKLEGDSTDLSD------------QIAELQAQIAELKMQLAKKEEELQAALAR 1091
Cdd:COG3524 164 EELVNQLSERAREDavRFAEEEVERAEERLRDAREALLAfrnrngildpeaTAEALLQLIATLEGQLAELEAELAALRSY 243
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 806638593 1092 VEEEAAQKNMALKKIRELETQISELQEDLESERACRNKAEKQkrdlgEELEALKTEL---EDTLDSTAAQQE 1160
Cdd:COG3524 244 LSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSLASLL-----AEYERLELERefaEKAYTSALAALE 310
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1107-1918 |
4.51e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.88 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1107 RELETQISELQEDLESERACRNKAEKQKRDLGEELEALK---TELEDTLDS---------TAAQQELRSKREQEvsilkk 1174
Cdd:COG3096 281 RELSERALELRRELFGARRQLAEEQYRLVEMARELEELSareSDLEQDYQAasdhlnlvqTALRQQEKIERYQE------ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1175 tlEDEAKTHEAQIQEMrqkhsqAVEELAEQLEqtkRVKATLEKAKQTLENERGELANEVKALlqgkgDSEHKRKkveaqL 1254
Cdd:COG3096 355 --DLEELTERLEEQEE------VVEEAAEQLA---EAEARLEAAEEEVDSLKSQLADYQQAL-----DVQQTRA-----I 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1255 QELQ-VKFSEGERVRTELADkvsklqVELDSVTGLLNQSDSKSSKLTKDFSALESQLQDTQELlQEENRQKLSLSTKLKQ 1333
Cdd:COG3096 414 QYQQaVQALEKARALCGLPD------LTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAA-RRQFEKAYELVCKIAG 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1334 MEDEKNSFRE--QLEEEEEAKRNLEKQIATLHAQVTDmkkkmedgvgcLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKL 1411
Cdd:COG3096 487 EVERSQAWQTarELLRRYRSQQALAQRLQQLRAQLAE-----------LEQRLRQQQNAERLLEEFCQRIGQQLDAAEEL 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1412 EKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQkkfDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLA--RALEEAM 1489
Cdd:COG3096 556 EELLAELEAQLEELEEQAAEAVEQRSELRQQL---EQLRARIKELAARAPAWLAAQDALERLREQSGEALAdsQEVTAAM 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1490 EQKAELERLNKQfrtemedlmsSKDdvgksvhELEKSKRALEQQVEEMK-------TQLEELEDELQATEDAKLRLEVNL 1562
Cdd:COG3096 633 QQLLEREREATV----------ERD-------ELAARKQALESQIERLSqpggaedPRLLALAERLGGVLLSEIYDDVTL 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1563 Q-----------AMKAQFERDLQGrdeqseekkkqlvrqVREMEAELED--------ERKQRSIAMAARKKLEMDLKDL- 1622
Cdd:COG3096 696 EdapyfsalygpARHAIVVPDLSA---------------VKEQLAGLEDcpedlyliEGDPDSFDDSVFDAEELEDAVVv 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1623 -----------------------EAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKklksmE 1679
Cdd:COG3096 761 klsdrqwrysrfpevplfgraarEKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPDP-----E 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1680 AEMiqlqeelaaaerakRQAQQERDELADEIANssgkgalaleekrrLEARIAQLEEELEEEQGNTELINDRLKKANLQI 1759
Cdd:COG3096 836 AEL--------------AALRQRRSELERELAQ--------------HRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLA 887
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1760 DQintdlnlerSHAQKNENARQQLErqnkelkaKLQEMESAVKSKYKAsIAALEAKIAQL------EEQLDNETKERQAA 1833
Cdd:COG3096 888 DE---------TLADRLEELREELD--------AAQEAQAFIQQHGKA-LAQLEPLVAVLqsdpeqFEQLQADYLQAKEQ 949
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1834 SKQVRRAEKKLKDVLlqvedERRNAEQFKD---QADKASTRLKQLKRQLEeaeeeaqRANASRRKLQRELEDATETADAM 1910
Cdd:COG3096 950 QRRLKQQIFALSEVV-----QRRPHFSYEDavgLLGENSDLNEKLRARLE-------QAEEARREAREQLRQAQAQYSQY 1017
|
....*...
gi 806638593 1911 NREVSSLK 1918
Cdd:COG3096 1018 NQVLASLK 1025
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
864-1277 |
4.66e-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: 51.94 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 864 AENRLTEMETMQSQLMAEKLQLQEQLQAETElcaeaEELRARLTAKKQELEEICHDL---EARVEEEEERCQYLQAEKKK 940
Cdd:TIGR04523 279 NNKKIKELEKQLNQLKSEISDLNNQKEQDWN-----KELKSELKNQEKKLEEIQNQIsqnNKIISQLNEQISQLKKELTN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 941 MQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAK 1020
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKE 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1021 LKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELqaalarvEEEAAQKN 1100
Cdd:TIGR04523 434 TIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL-------KKLNEEKK 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1101 MALKKIRELETQISELQEDLESERACRNKAEKQKRDLGEELEalktELEDTLDSTAAQQELRSKrEQEVSILKKTLEDEA 1180
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN----KDDFELKKENLEKEIDEK-NKEIEELKQTQKSLK 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1181 KTHEaQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVK 1260
Cdd:TIGR04523 582 KKQE-EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
|
410
....*....|....*..
gi 806638593 1261 FSEGERVRTELADKVSK 1277
Cdd:TIGR04523 661 WPEIIKKIKESKTKIDD 677
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1522-1683 |
5.00e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.92 E-value: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1522 ELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDlqgrdeqseEKKKQLVRQVREMEAelede 1601
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY---------EEQLGNVRNNKEYEA----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1602 rKQRSIAMAARKKlemdlKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAE 1681
Cdd:COG1579 94 -LQKEIESLKRRI-----SDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
..
gi 806638593 1682 MI 1683
Cdd:COG1579 168 LA 169
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1466-1874 |
5.34e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.88 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1466 RAEAEAREKETKALSLARALEEAMEQKAElerlnKQFRTEmedlmsskddvgksvhelekskrALEQQVEEMKTQLEELE 1545
Cdd:COG3096 275 RHANERRELSERALELRRELFGARRQLAE-----EQYRLV-----------------------EMARELEELSARESDLE 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1546 DELQATEDaklRLEVNLQAMKAQ-----FERDLqgrdEQSEEKKKQLVRQVREMEAELEDERKQRSIAMAARKKLEMDLK 1620
Cdd:COG3096 327 QDYQAASD---HLNLVQTALRQQekierYQEDL----EELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1621 DLEAHIDtANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKEnekKLKSMEAEMIQLQEELAAAERAKRQ-- 1698
Cdd:COG3096 400 DYQQALD-VQQTRAIQYQQAVQALEKARALCGLPDLTPENAEDYLAAFRA---KEQQATEEVLELEQKLSVADAARRQfe 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1699 -AQQERDELADEIANSS--GKGALALEEKRRLEArIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQK 1775
Cdd:COG3096 476 kAYELVCKIAGEVERSQawQTARELLRRYRSQQA-LAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1776 NENARQQLERQNKELKAKLQEmESAVKSKYKASIAALEAKIAQLE-------------EQLDNETKERQAASKQVRRAEK 1842
Cdd:COG3096 555 LEELLAELEAQLEELEEQAAE-AVEQRSELRQQLEQLRARIKELAarapawlaaqdalERLREQSGEALADSQEVTAAMQ 633
|
410 420 430
....*....|....*....|....*....|..
gi 806638593 1843 KLKDVLLQVEDERRNAEQFKDQADKASTRLKQ 1874
Cdd:COG3096 634 QLLEREREATVERDELAARKQALESQIERLSQ 665
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1456-1657 |
6.16e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.40 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1456 ISAKYAEERDRAEAEAREkeTKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSkddvgksvhELEKSKRALEQQVE 1535
Cdd:COG2433 355 VEKKVPPDVDRDEVKARV--IRGLSIEEALEELIEKELPEEEPEAEREKEHEERELT---------EEEEEIRRLEEQVE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1536 EMKTQLEELEDELQATEDAKLRLEvnlqaMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKqrsiamaARKKL 1615
Cdd:COG2433 424 RLEAEVEELEAELEEKDERIERLE-----RELSEARSEERREIRKDREISRLDREIERLERELEEERE-------RIEEL 491
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 806638593 1616 EMDLKDLEAHIDTANKNREEAIKQLRKLQaqmKDCMRELDDT 1657
Cdd:COG2433 492 KRKLERLKELWKLEHSGELVPVKVVEKFT---KEAIRRLEEE 530
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1522-1706 |
6.16e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1522 ELEKSKRALEQQVEEMKTQLEELEDELQA----------TEDAKLRLE--VNLQAMKAQFERDLQGRDEQSEEKKKQLVR 1589
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdlSEEAKLLLQqlSELESQLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1590 QVREMEAELEDERKQR---SIAMAARKKLEMDLKDLEAH--IDTANKNREEAIKQLRKLQAQMKDCMR-ELDDTRASREE 1663
Cdd:COG3206 252 GPDALPELLQSPVIQQlraQLAELEAELAELSARYTPNHpdVIALRAQIAALRAQLQQEAQRILASLEaELEALQAREAS 331
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 806638593 1664 ILAQAKENEKKLKSM---EAEMIQLQEELAAAERAKRQAQQERDEL 1706
Cdd:COG3206 332 LQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1142-1524 |
6.21e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.05 E-value: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1142 EALKTELEDTLDSTAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKhsqaVEELAEQLEQTKRVKATLEKAKQT 1221
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESR----VAELKEELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1222 LENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVSKL-------QVELDSVTGLLNQSDS 1294
Cdd:pfam07888 106 LSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAgaqrkeeEAERKQLQAKLQQTEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1295 KSSKLTKDFSALESQL--QDTQEL-LQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKK 1371
Cdd:pfam07888 186 ELRSLSKEFQELRNSLaqRDTQVLqLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1372 KMEDGVgcletAEEAKRRLQkdLEGLSQRLEEKVAAydkLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLA 1451
Cdd:pfam07888 266 QRDRTQ-----AELHQARLQ--AAQLTLQLADASLA---LREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQ 335
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 806638593 1452 EEKTisakyaeERDRAEAE-AREKETKALSLARALEEAMEQKAELERLNKqfrtEMEDLMSSKDDVGKSVHELE 1524
Cdd:pfam07888 336 EERM-------EREKLEVElGREKDCNRVQLSESRRELQELKASLRVAQK----EKEQLQAEKQELLEYIRQLE 398
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
934-1110 |
7.09e-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: 7.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 934 LQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDqiiMEDQNCKLAKEKKLLEDRVAEF-----TTNL 1008
Cdd:COG3883 28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE---IAEAEAEIEERREELGERARALyrsggSVSY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1009 MEEEEKSKSLA----------KLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQL 1078
Cdd:COG3883 105 LDVLLGSESFSdfldrlsalsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALL 184
|
170 180 190
....*....|....*....|....*....|..
gi 806638593 1079 AKKEEELQAALARVEEEAAQKNMALKKIRELE 1110
Cdd:COG3883 185 AQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1433-1755 |
7.12e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 50.45 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1433 RQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLN---KQFRTEMEDL 1509
Cdd:pfam19220 44 PQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRielRDKTAQAEAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1510 MSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFER------DLQGRDEQSEEK 1583
Cdd:pfam19220 124 ERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEqaaelaELTRRLAELETQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1584 KKQLVRQVREMEAELEDERKQRSIAMAA-----------RKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMR 1652
Cdd:pfam19220 204 LDATRARLRALEGQLAAEQAERERAEAQleeaveahraeRASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAER 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1653 ELDDTRASReeilaqaKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIA 1732
Cdd:pfam19220 284 RLKEASIER-------DTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIA 356
|
330 340
....*....|....*....|...
gi 806638593 1733 QLEEELEEEQGNTELINDRLKKA 1755
Cdd:pfam19220 357 ELTKRFEVERAALEQANRRLKEE 379
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1618-1712 |
7.13e-06 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 50.84 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1618 DLKDLEAHIDT-----ANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEI---LAQAKENEKKLKSMEAEMIQLQEEL 1689
Cdd:PRK05431 3 DIKLIRENPEAvkealAKRGFPLDVDELLELDEERRELQTELEELQAERNALskeIGQAKRKGEDAEALIAEVKELKEEI 82
|
90 100
....*....|....*....|...
gi 806638593 1690 AAAERAKRQAQQERDELADEIAN 1712
Cdd:PRK05431 83 KALEAELDELEAELEELLLRIPN 105
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1251-1918 |
8.01e-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: 50.98 E-value: 8.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1251 EAQLQELQvkfSEGERVRTELADKVSKLQVELDSVTGLLNQSDSKSSKLTKDFSALESQLQDTQELLQEENRQklsLSTK 1330
Cdd:pfam10174 2 QAQLRDLQ---RENELLRRELDIKESKLGSSMNSIKTFWSPELKKERALRKEEAARISVLKEQYRVTQEENQH---LQLT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1331 LKQMEDEKnsfreqleeeeEAKRNLEKqiaTLHAQVTDMKKKMEDGVGCLETAEEAKRRLQ-------KDLEGLSQRLEE 1403
Cdd:pfam10174 76 IQALQDEL-----------RAQRDLNQ---LLQQDFTTSPVDGEDKFSTPELTEENFRRLQseherqaKELFLLRKTLEE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1404 K-----------VAAYDKLEKTKTRLQQELDDLLVDLDHQ--RQSVSNLEKKQKKFDQLLAEEKTISAKYAEE-RDRAEA 1469
Cdd:pfam10174 142 MelrietqkqtlGARDESIKKLLEMLQSKGLPKKSGEEDWerTRRIAEAEMQLGHLEVLLDQKEKENIHLREElHRRNQL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1470 EAREKETKALslaRALEEAMEQK-AELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDEL 1548
Cdd:pfam10174 222 QPDPAKTKAL---QTVIEMKDTKiSSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQEL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1549 QATEDAKLRLEVNLQAMKAQFERDLQGRD--EQSEEKKKQ-----------LVRQVREMEAELEDERKQRSIAMAARKKL 1615
Cdd:pfam10174 299 SKKESELLALQTKLETLTNQNSDCKQHIEvlKESLTAKEQraailqtevdaLRLRLEEKESFLNKKTKQLQDLTEEKSTL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1616 EMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAemiQLQEELAAAERA 1695
Cdd:pfam10174 379 AGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEE---ALSEKERIIERL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1696 KRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQK 1775
Cdd:pfam10174 456 KEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1776 NENARQqlerqnkelKAKLQEMESAVKSKYKASIAALEAKIAQLEEqldnetkERQAASKQVRRaekkLKDVLLQVEDER 1855
Cdd:pfam10174 536 LENQLK---------KAHNAEEAVRTNPEINDRIRLLEQEVARYKE-------ESGKAQAEVER----LLGILREVENEK 595
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 806638593 1856 RNAEqfKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLK 1918
Cdd:pfam10174 596 NDKD--KKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQ 656
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1009-1339 |
8.24e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 8.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1009 MEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAA 1088
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1089 LARVEEEAAQKNMALKKIRELETQISELQEDLESERACRNKAEKQKRDLGEELEALKTELedtldsTAAQQELRSKREQE 1168
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI------AEREEELKELEEQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1169 VSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRK 1248
Cdd:COG4372 160 ESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1249 -KVEAQLQELQVKFSEGERVRTELADKVSKLQVELDSVTGLLNQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSL 1327
Cdd:COG4372 240 dALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLA 319
|
330
....*....|..
gi 806638593 1328 STKLKQMEDEKN 1339
Cdd:COG4372 320 ALLELAKKLELA 331
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1578-1733 |
9.92e-06 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 48.67 E-value: 9.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1578 EQSEEKKKQLVRQVREMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQ-----LRKLQAQMKDCMR 1652
Cdd:COG1842 19 DKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgredlAREALERKAELEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1653 ELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAeRAKRQAQQERDELADEIANSSGKGALALEEkrRLEARIA 1732
Cdd:COG1842 99 QAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTL-KARAKAAKAQEKVNEALSGIDSDDATSALE--RMEEKIE 175
|
.
gi 806638593 1733 Q 1733
Cdd:COG1842 176 E 176
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1010-1225 |
1.10e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1010 EEEEKSKSLAKLKNKheamITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAAL 1089
Cdd:COG3883 17 QIQAKQKELSELQAE----LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1090 ARVEE------------------EAAQKNMALKKIRELETQ-ISELQEDLESERACRNKAEKQKrdlgEELEALKTELED 1150
Cdd:COG3883 93 RALYRsggsvsyldvllgsesfsDFLDRLSALSKIADADADlLEELKADKAELEAKKAELEAKL----AELEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 806638593 1151 TLDSTAAQQElrskreqEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQTLENE 1225
Cdd:COG3883 169 AKAELEAQQA-------EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1304-1494 |
1.29e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1304 SALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMED-------- 1375
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraralyrs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1376 --GVGCLETAEEAK---------RRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQK 1444
Cdd:COG3883 99 ggSVSYLDVLLGSEsfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 806638593 1445 KFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAE 1494
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
960-1419 |
1.38e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 50.44 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 960 QKLQLEKVTTEAKLKKLE---EDQIIMEDQNCKLAKEKKLLEDRVAEFTTnLMEEEEKSKSLAKLKNKHEAMITDLEERL 1036
Cdd:TIGR01612 1229 EKIDEEKKKSEHMIKAMEayiEDLDEIKEKSPEIENEMGIEMDIKAEMET-FNISHDDDKDHHIISKKHDENISDIREKS 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1037 RR------EEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAE----LKMQLAKKE-EELQAALARVEEEAAQKNMALKK 1105
Cdd:TIGR01612 1308 LKiiedfsEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANiyniLKLNKIKKIiDEVKEYTKEIEENNKNIKDELDK 1387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1106 IrelETQISELQEDLeSERACRNKAEK--QKRDLGEELEALkTELEDTLDSTAAQQELRSKREQE----VSILKKTLE-- 1177
Cdd:TIGR01612 1388 S---EKLIKKIKDDI-NLEECKSKIEStlDDKDIDECIKKI-KELKNHILSEESNIDTYFKNADEnnenVLLLFKNIEma 1462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1178 DEAKTHEAQIQE--MRQKHSQAVEELAEQLEQTKRVKATLEK-AKQTLEN---------ERGELANEVKALL------QG 1239
Cdd:TIGR01612 1463 DNKSQHILKIKKdnATNDHDFNINELKEHIDKSKGCKDEADKnAKAIEKNkelfeqykkDVTELLNKYSALAiknkfaKT 1542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1240 KGDSE---------HKRKKVEAQLQELQVKFSEGERVRTElaDKVSKLQVELDSVTGLLNQSDSKSSKLTKdFSALESQL 1310
Cdd:TIGR01612 1543 KKDSEiiikeikdaHKKFILEAEKSEQKIKEIKKEKFRIE--DDAAKNDKSNKAAIDIQLSLENFENKFLK-ISDIKKKI 1619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1311 QDTQELLQEENRQKLSLS-----TKLKQMEDEKNSFREQLEEEEEAKRNLEkqiatlhaqvtDMKKKMEDGVGCLETAEE 1385
Cdd:TIGR01612 1620 NDCLKETESIEKKISSFSidsqdTELKENGDNLNSLQEFLESLKDQKKNIE-----------DKKKELDELDSEIEKIEI 1688
|
490 500 510
....*....|....*....|....*....|....*.
gi 806638593 1386 AKRRLQKDLE-GLSQRLEE-KVAAYDKLEKTKTRLQ 1419
Cdd:TIGR01612 1689 DVDQHKKNYEiGIIEKIKEiAIANKEEIESIKELIE 1724
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
961-1526 |
1.45e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 50.44 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 961 KLQLEKVTTEAKLKKLEEDQIIMEDQNC----KLAKEKKLLeDRVAEFTTNLmeeEEKSKSLAKLKNKHEAMITDLeerl 1036
Cdd:TIGR01612 1324 KKELQKNLLDAQKHNSDINLYLNEIANIynilKLNKIKKII-DEVKEYTKEI---EENNKNIKDELDKSEKLIKKI---- 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1037 rreeKQRQELEKTRRKLEgdSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEE-------------AAQKNMAL 1103
Cdd:TIGR01612 1396 ----KDDINLEECKSKIE--STLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENnenvlllfkniemADNKSQHI 1469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1104 KKIR------ELETQISELQEDLESERACRNKAEKQKRdlgeelealkteledtldSTAAQQELRSKREQEVSIL----- 1172
Cdd:TIGR01612 1470 LKIKkdnatnDHDFNINELKEHIDKSKGCKDEADKNAK------------------AIEKNKELFEQYKKDVTELlnkys 1531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1173 ----KKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKatleKAKQTLENERGELANEVKALLQgkgdsehkrk 1248
Cdd:TIGR01612 1532 alaiKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIK----KEKFRIEDDAAKNDKSNKAAID---------- 1597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1249 kVEAQLQELQVKFSEGERVRTELADkvsklqveldsvtgLLNQSDSksskLTKDFSALESQLQDTQelLQEENRQKLSLS 1328
Cdd:TIGR01612 1598 -IQLSLENFENKFLKISDIKKKIND--------------CLKETES----IEKKISSFSIDSQDTE--LKENGDNLNSLQ 1656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1329 TKLKQMEDEKNSFREQLEEEEeakrNLEKQIATLHAQVTDMKKKMEDGV--GCLETAEEAKRRLQKDLEGLSQRLEEKVA 1406
Cdd:TIGR01612 1657 EFLESLKDQKKNIEDKKKELD----ELDSEIEKIEIDVDQHKKNYEIGIieKIKEIAIANKEEIESIKELIEPTIENLIS 1732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1407 AY-----------DKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLlaEEKTISAKyAEERDRAEAEAREKE 1475
Cdd:TIGR01612 1733 SFntndlegidpnEKLEEYNTEIGDIYEEFIELYNIIAGCLETVSKEPITYDEI--KNTRINAQ-NEFLKIIEIEKKSKS 1809
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 806638593 1476 TKALSLARALEEAMEQ-KAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKS 1526
Cdd:TIGR01612 1810 YLDDIEAKEFDRIINHfKKKLDHVNDKFTKEYSKINEGFDDISKSIENVKNS 1861
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1450-1607 |
1.92e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.39 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1450 LAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEM-----------EDLMSSKDDVGK 1518
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELqklekrllqkeENLDRKLELLEK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1519 SVHELEKSKRALEQQVEEMKTQLEELEdELQATEDAKLRLEVNLQAMKAQfERDLQGRDEQSEEKKKQLVRQVrEMEAEL 1598
Cdd:PRK12704 108 REEELEKKEKELEQKQQELEKKEEELE-ELIEEQLQELERISGLTAEEAK-EILLEKVEEEARHEAAVLIKEI-EEEAKE 184
|
....*....
gi 806638593 1599 EDERKQRSI 1607
Cdd:PRK12704 185 EADKKAKEI 193
|
|
| Gp58 |
pfam07902 |
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage ... |
1055-1318 |
2.03e-05 |
|
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage and prophage proteins. They are similar to gp58, a minor structural protein of Lactococcus delbrueckii bacteriophage LL-H.
Pssm-ID: 369586 [Multi-domain] Cd Length: 594 Bit Score: 49.57 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1055 GDSTDLSDQIAELQAQIAELKMQLAK-KEEELQAALARVE----EEAAQKNMA---LKKIRELETQISElqedleserac 1126
Cdd:pfam07902 71 GESTGLFKSLEEMLSQLKELNLELTDtKNSNLWSKIKLNNngmlREYHNDTIKteiVESAEGIATRISE----------- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1127 rnKAEKQKRDLGEELEALKTELEDtldstaAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQLE 1206
Cdd:pfam07902 140 --DTDKKLALINETISGIRREYQD------ADRQLSSSYQAGIEGLKATMASDKIGLQAEIQASAQGLSQRYDNEIRKLS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1207 Q--TKRVKATLEKAKQTLENERGELANEvkallqgkgdSEHKRKKVEAQLQELQ-VKFSEGERVRTELADK---VSKLQV 1280
Cdd:pfam07902 212 AkiTTTSSGTTEAYESKLDDLRAEFTRS----------NQGMRTELESKISGLQsTQQSTAYQISQEISNRegaVSRVQQ 281
|
250 260 270
....*....|....*....|....*....|....*...
gi 806638593 1281 ELDSVTGLLNQSDSKSSKLTKDFSALESQLQDTQELLQ 1318
Cdd:pfam07902 282 DLDSYQRRLQDAEKNYSSLTQTVKGLQSTVSDPNSKLE 319
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1184-1421 |
2.07e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1184 EAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQTLENERGELAnevkallqgkgDSEHKRKKVEAQLQELQVKFse 1263
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE-----------ALQAEIDKLQAEIAEAEAEI-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1264 gERVRTELADKVSKLQVELDSVTGLLNQSDSKS-SKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFR 1342
Cdd:COG3883 82 -EERREELGERARALYRSGGSVSYLDVLLGSESfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 806638593 1343 EQLEEEEEAKRNLEKQIATLHAQVTDMKKKmedgvgcLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQE 1421
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAE-------EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1155-1921 |
2.16e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1155 TAAQQELRSKREQEVSILKKTLE--DEAKTHEAQIQEMRQKHSQAVEELA------EQLEQTKRVKATLEKAkqtleNER 1226
Cdd:PRK04863 289 LELRRELYTSRRQLAAEQYRLVEmaRELAELNEAESDLEQDYQAASDHLNlvqtalRQQEKIERYQADLEEL-----EER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1227 GELANEVKALLQGKGDsEHKRKKVEAQLqelqvkfsEGERVRTELADKVSKLQVE-------------LDSVTGLLNQSD 1293
Cdd:PRK04863 364 LEEQNEVVEEADEQQE-ENEARAEAAEE--------EVDELKSQLADYQQALDVQqtraiqyqqavqaLERAKQLCGLPD 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1294 SKSSKLTKDFSALESQLQD-TQELLQEEnrQKLSLSTKLKQM-----------------EDEKNSFREQLeeeeeakRNL 1355
Cdd:PRK04863 435 LTADNAEDWLEEFQAKEQEaTEELLSLE--QKLSVAQAAHSQfeqayqlvrkiagevsrSEAWDVARELL-------RRL 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1356 EKQIAtLHAQVTDMKKKMEDgvgcLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQS 1435
Cdd:PRK04863 506 REQRH-LAEQLQQLRMRLSE----LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARER 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1436 VSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAeAREKETKALSLARALEEAMEQKAELERlnkQFRTEMEdlmsskdd 1515
Cdd:PRK04863 581 RMALRQQLEQLQARIQRLAARAPAWLAAQDALAR-LREQSGEEFEDSQDVTEYMQQLLERER---ELTVERD-------- 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1516 vgksvhELEKSKRALEQQVEEMK-------TQLEELEDELQATEDAKLRLEVNLQ-----------AMKAQFERDLQGrd 1577
Cdd:PRK04863 649 ------ELAARKQALDEEIERLSqpggsedPRLNALAERFGGVLLSEIYDDVSLEdapyfsalygpARHAIVVPDLSD-- 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1578 eqseekkkqlvrqVREMEAELEDerkqrsiamaarkkLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDcmRELddt 1657
Cdd:PRK04863 721 -------------AAEQLAGLED--------------CPEDLYLIEGDPDSFDDSVFSVEELEKAVVVKIAD--RQW--- 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1658 RASR--EEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSgkgALALE-----EKRRLEAR 1730
Cdd:PRK04863 769 RYSRfpEVPLFGRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHL---AVAFEadpeaELRQLNRR 845
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1731 IAQLEEELEEEQGNTELINDRLKKANLQIDQIN-----TDLNLERSHAQKNENARQQLERqnkelkakLQEMESAVKsKY 1805
Cdd:PRK04863 846 RVELERALADHESQEQQQRSQLEQAKEGLSALNrllprLNLLADETLADRVEEIREQLDE--------AEEAKRFVQ-QH 916
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1806 KASIAALEAKIAQL---EEQLDNETKERQAASKQVRRAEKK---LKDVL-----LQVEDERRNAEQFKDQADKASTRLKQ 1874
Cdd:PRK04863 917 GNALAQLEPIVSVLqsdPEQFEQLKQDYQQAQQTQRDAKQQafaLTEVVqrrahFSYEDAAEMLAKNSDLNEKLRQRLEQ 996
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 806638593 1875 LKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKL 1921
Cdd:PRK04863 997 AEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQEL 1043
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1026-1709 |
2.36e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 49.82 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1026 EAMITDLEERLRREEKQRQE-LEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLakKEEELQAALARvEEEAAQKNMALK 1104
Cdd:NF041483 505 ERVRTEAIERATTLRRQAEEtLERTRAEAERLRAEAEEQAEEVRAAAERAAREL--REETERAIAAR-QAEAAEELTRLH 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1105 KirELETQISELQEDLESERAcrnKAEKQKRDLGEELEALKTELEDTLDSTAAQQE------------------------ 1160
Cdd:NF041483 582 T--EAEERLTAAEEALADARA---EAERIRREAAEETERLRTEAAERIRTLQAQAEqeaerlrteaaadasaaraegenv 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1161 ---LRSKREQEVSILKKTLEDEAKTHEAQIQEMRQK-HSQAVEELAEQLEQTKR----VKATLEKAKQTLENERGELANE 1232
Cdd:NF041483 657 avrLRSEAAAEAERLKSEAQESADRVRAEAAAAAERvGTEAAEALAAAQEEAARrrreAEETLGSARAEADQERERAREQ 736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1233 VKALLQGkgdsehKRKKVEAQLQELQVKFSEGERVRTEL--ADKVSKLQVElDSVTGLLNQSDSKSSKLTkdfSALESQL 1310
Cdd:NF041483 737 SEELLAS------ARKRVEEAQAEAQRLVEEADRRATELvsAAEQTAQQVR-DSVAGLQEQAEEEIAGLR---SAAEHAA 806
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1311 QDTQELLQEE-NRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIAT--------LHAQVTDMKKKME-DGVGCL 1380
Cdd:NF041483 807 ERTRTEAQEEaDRVRSDAYAERERASEDANRLRREAQEETEAAKALAERTVSeaiaeaerLRSDASEYAQRVRtEASDTL 886
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1381 ETAEEAKRRLQKDLEGLSQRLEEKVAAY-DKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAK 1459
Cdd:NF041483 887 ASAEQDAARTRADAREDANRIRSDAAAQaDRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEA 966
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1460 YAE-ERDRAEAeareketkALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVheLEKSKRALEQQVEEMK 1538
Cdd:NF041483 967 TGEaERLRAEA--------AETVGSAQQHAERIRTEAERVKAEAAAEAERLRTEAREEADRT--LDEARKDANKRRSEAA 1036
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1539 TQLEELEDElQATEDAKLRLEVNLQAMKAQFERDLQGrDEQSEEKKKQLVRQVREMEAE----LEDERKQ--------RS 1606
Cdd:NF041483 1037 EQADTLITE-AAAEADQLTAKAQEEALRTTTEAEAQA-DTMVGAARKEAERIVAEATVEgnslVEKARTDadellvgaRR 1114
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1607 IAMAARKKLEMDLKDLEAHIDTAN-KNREEAIKQLR----KLQAQMKDCMRELDDTRASREEILAQA------------K 1669
Cdd:NF041483 1115 DATAIRERAEELRDRITGEIEELHeRARRESAEQMKsageRCDALVKAAEEQLAEAEAKAKELVSDAnseaskvriaavK 1194
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 806638593 1670 ENEKKLKSMEAEMIQLQEElaaAERAKRQAQQERDELADE 1709
Cdd:NF041483 1195 KAEGLLKEAEQKKAELVRE---AEKIKAEAEAEAKRTVEE 1231
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1088-1297 |
2.80e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1088 ALARVEEEAAQKNMALKKIRELETQISELQEDLESERACRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKR-- 1165
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1166 -----EQEVSILKKTLE----DEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQTLENERGELANEVKAL 1236
Cdd:COG3883 94 alyrsGGSVSYLDVLLGsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 806638593 1237 LQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVSKLQVELDSVTGLLNQSDSKSS 1297
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1381-1664 |
3.14e-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: 48.87 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1381 ETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTR----LQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLA--EEK 1454
Cdd:pfam05667 215 ELAAAQEWEEEWNSQGLASRLTPEEYRKRKRTKLLKRiaeqLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTtdTGL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1455 TISAKYAEERDRAEAEAREKETKALSLARALEEAMEQK--AELERLNKQFrtemEDLMSSKDDVGKSVHELEKSKRALEQ 1532
Cdd:pfam05667 295 TKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQreEELEELQEQL----EDLESSIQELEKEIKKLESSIKQVEE 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1533 QVEEMKTQLEELEDELQATE-------DAKLRLEvNLQAMKAQFERDLQGRDEQSEEKKKQLV---RQVREMEAELEDER 1602
Cdd:pfam05667 371 ELEELKEQNEELEKQYKVKKktldllpDAEENIA-KLQALVDASAQRLVELAGQWEKHRVPLIeeyRALKEAKSNKEDES 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1603 KQ------------RSIAMAARKKLEMdLKDLEAHIDTANK--NRE-------EAIKQLRKlqaQMKDCMRELDDTRASR 1661
Cdd:pfam05667 450 QRkleeikelrekiKEVAEEAKQKEEL-YKQLVAEYERLPKdvSRSaytrrilEIVKNIKK---QKEEITKILSDTKSLQ 525
|
...
gi 806638593 1662 EEI 1664
Cdd:pfam05667 526 KEI 528
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
872-1238 |
3.67e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.74 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 872 ETMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQYLQAEKKKMQQNIQELEEQ 951
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 952 LEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLaklknkhEAMITD 1031
Cdd:pfam07888 110 SEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQL-------QAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1032 LEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKmqlaKKEEELQAALARVEEEAAQKNMALKKIRELET 1111
Cdd:pfam07888 183 TEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH----RKEAENEALLEELRSLQERLNASERKVEGLGE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1112 QISELQEDLESERACRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQE--LRSKREQEVSILKktLEDEAKTHEAQIQE 1189
Cdd:pfam07888 259 ELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQEREtlQQSAEADKDRIEK--LSAELQRLEERLQE 336
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 806638593 1190 MRQKHSQAVEELAE-------QLEQTKRVKATLEKAKQTLENERGELANEVKALLQ 1238
Cdd:pfam07888 337 ERMEREKLEVELGRekdcnrvQLSESRRELQELKASLRVAQKEKEQLQAEKQELLE 392
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1177-1367 |
4.10e-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: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1177 EDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQE 1256
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1257 LQVKFSEGERVR--------TELADKVSKLQVELDSVTGLLNQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLS 1328
Cdd:COG3883 95 LYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 806638593 1329 TKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVT 1367
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1025-1176 |
4.18e-05 |
|
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: 47.83 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1025 HEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAqknmalk 1104
Cdd:pfam09787 42 STALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEA------- 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 806638593 1105 kirELETQISELQEDLESERACRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQ--EVSILKKTL 1176
Cdd:pfam09787 115 ---ELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSSSSQSELENRLHQltETLIQKQTM 185
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
650-674 |
4.32e-05 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 45.80 E-value: 4.32e-05
10 20
....*....|....*....|....*
gi 806638593 650 YKEQLAKLMATLRNTNPNFVRCIIP 674
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
857-1593 |
4.44e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 48.64 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 857 VREKHLAAEnrlTEMETMQSQLMAEKLQLQEQLQAETE-LCAEAEELRARLTAKKQELEEIchdlearveEEEERCQYLQ 935
Cdd:PRK10246 189 VFEQHKSAR---TELEKLQAQASGVALLTPEQVQSLTAsLQVLTDEEKQLLTAQQQQQQSL---------NWLTRLDELQ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 936 AEKKKMQQniQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQiimEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKS 1015
Cdd:PRK10246 257 QEASRRQQ--ALQQALAAEEKAQPQLAALSLAQPARQLRPHWERI---QEQSAALAHTRQQIEEVNTRLQSTMALRARIR 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1016 KSLAKLKNKHEAMITDLEERLRREEKQR---QELEKTRRKLEGDSTDlSDQIAELQAQIAELKMQLAKKEEelqAALARV 1092
Cdd:PRK10246 332 HHAAKQSAELQAQQQSLNTWLAEHDRFRqwnNELAGWRAQFSQQTSD-REQLRQWQQQLTHAEQKLNALPA---ITLTLT 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1093 EEEAAQKNMALKKIRELETQISELQEDLESERacrnkaeKQKRDLGEELEALKTELEDtLDSTAAQQELRSK-REQEVSI 1171
Cdd:PRK10246 408 ADEVAAALAQHAEQRPLRQRLVALHGQIVPQQ-------KRLAQLQVAIQNVTQEQTQ-RNAALNEMRQRYKeKTQQLAD 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1172 LKKTLEDEAKTHEAQIQEMRQKHSQ-----------AVEEL-AEQLEQTKRVKATLEKAKQTLENERGELANEVKALLQg 1239
Cdd:PRK10246 480 VKTICEQEARIKDLEAQRAQLQAGQpcplcgstshpAVEAYqALEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTK- 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1240 kgdsEHKRKKVEAQ--LQELQVKFSEGERVrteladkVSKLQVEL---DSVTGLLNQSDSKSSKLTkdfsaLESQLQDTQ 1314
Cdd:PRK10246 559 ----QLQRDESEAQslRQEEQALTQQWQAV-------CASLNITLqpqDDIQPWLDAQEEHERQLR-----LLSQRHELQ 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1315 ELLQEENRQKLSLStklKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQvtdmkkkmedgvgcletAEEAKRRLQKDL 1394
Cdd:PRK10246 623 GQIAAHNQQIIQYQ---QQIEQRQQQLLTALAGYALTLPQEDEEASWLATR-----------------QQEAQSWQQRQN 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1395 EglSQRLEEKVAAYDKLEKTktrLQQELDDLLVDldhQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAeAEAREK 1474
Cdd:PRK10246 683 E--LTALQNRIQQLTPLLET---LPQSDDLPHSE---ETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRL-QKAQAQ 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1475 ETKALSLARALEEAMEQKAELerlnkqfrtemedlmsskDDvgKSVHELEKSKRALEQQVEEMKTQLEELEDELQAteda 1554
Cdd:PRK10246 754 FDTALQASVFDDQQAFLAALL------------------DE--ETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQ---- 809
|
730 740 750
....*....|....*....|....*....|....*....
gi 806638593 1555 klrlevNLQAMKAQFerDLQGRDEQSEEKKKQLVRQVRE 1593
Cdd:PRK10246 810 ------HQQHRPDGL--DLTVTVEQIQQELAQLAQQLRE 840
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1063-1239 |
4.57e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1063 QIAELQAQIAELKMQLakkeEELQAALARVEEEaaqknmalkkIRELETQISELQEDLESERACRNKAEKQKrdlgEELE 1142
Cdd:COG1579 11 DLQELDSELDRLEHRL----KELPAELAELEDE----------LAALEARLEAAKTELEDLEKEIKRLELEI----EEVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1143 ALKTELEDTLDSTAAQQELRSkREQEVSILKK---TLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAK 1219
Cdd:COG1579 73 ARIKKYEEQLGNVRNNKEYEA-LQKEIESLKRrisDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170 180
....*....|....*....|
gi 806638593 1220 QTLENERGELANEVKALLQG 1239
Cdd:COG1579 152 AELEAELEELEAEREELAAK 171
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1335-1536 |
4.80e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1335 EDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLekt 1414
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1415 kTRLQQELDDLLVDLDH--QRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQK 1492
Cdd:COG3883 92 -ARALYRSGGSVSYLDVllGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 806638593 1493 AELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEE 1536
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1019-1153 |
5.49e-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: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1019 AKLKNKHEAM---ITDLEERLRREEKQRQELEKtrrklegdstdlsDQIAELQAQIAELKMQLAKKEEELQAALARVEEE 1095
Cdd:COG0542 400 ARVRMEIDSKpeeLDELERRLEQLEIEKEALKK-------------EQDEASFERLAELRDELAELEEELEALKARWEAE 466
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 806638593 1096 aaqknmalkkiRELETQISELQEDLESERACRNKAEKQKRDLGEELEALKTELEDTLD 1153
Cdd:COG0542 467 -----------KELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVT 513
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1386-1622 |
5.92e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.09 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1386 AKRRLQKDLeglsqrLEEKV-AAYDKLEKTKTR-LQQELDDLLVDLDHQRQSV---------------SNLEKKQKKFDQ 1448
Cdd:PHA02562 151 ARRKLVEDL------LDISVlSEMDKLNKDKIReLNQQIQTLDMKIDHIQQQIktynknieeqrkkngENIARKQNKYDE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1449 LLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKqfrtemEDLMSSKDDV----GKSVHELE 1524
Cdd:PHA02562 225 LVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQK------VIKMYEKGGVcptcTQQISEGP 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1525 KSKRALEQQVEEMKTQLEELEDELQatEDAKLRLEVNLQAMKAqfeRDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQ 1604
Cdd:PHA02562 299 DRITKIKDKLKELQHSLEKLDTAID--ELEEIMDEFNEQSKKL---LELKNKISTNKQSLITLVDKAKKVKAAIEELQAE 373
|
250
....*....|....*...
gi 806638593 1605 RSIAMAARKKLEMDLKDL 1622
Cdd:PHA02562 374 FVDNAEELAKLQDELDKI 391
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
905-1469 |
6.18e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.36 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 905 RLTAKKQELEEICHDLEARVEEEeercQYLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIME 984
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRAEISNI----DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLK 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 985 D---QNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDL----EERLRREEKQRQELEKTRRKLEGDS 1057
Cdd:PRK01156 239 SalnELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPvyknRNYINDYFKYKNDIENKKQILSNID 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1058 TDLSD------QIAELQAQIAE-LKMQlaKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERACRNKA 1130
Cdd:PRK01156 319 AEINKyhaiikKLSVLQKDYNDyIKKK--SRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEI 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1131 EKQKRDLGEELEALKTELEDTLDSTAA-----QQELRSKREQEVSILKKT--LEDEAK-----TH--EAQIQEMRQKHSQ 1196
Cdd:PRK01156 397 LKIQEIDPDAIKKELNEINVKLQDISSkvsslNQRIRALRENLDELSRNMemLNGQSVcpvcgTTlgEEKSNHIINHYNE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1197 AVEELAEQLEQTKR-VKATLEKAKQTLENE---RGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELA 1272
Cdd:PRK01156 477 KKSRLEEKIREIEIeVKDIDEKIVDLKKRKeylESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1273 D-KVSKLQVELDSVTGLLNQSDSKS-SKLTKDFSALESQLQD----TQELLQEENRQKLSLSTKLKQMEDEKNSFREQLE 1346
Cdd:PRK01156 557 SlKLEDLDSKRTSWLNALAVISLIDiETNRSRSNEIKKQLNDlesrLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYN 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1347 EEEEAKRnlekQIATLHAQVTDMKKKMEDgvgcletaeeaKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLL 1426
Cdd:PRK01156 637 EIQENKI----LIEKLRGKIDNYKKQIAE-----------IDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLE 701
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 806638593 1427 VDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEA 1469
Cdd:PRK01156 702 STIEILRTRINELSDRINDINETLESMKKIKKAIGDLKRLREA 744
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1462-1704 |
6.65e-05 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 46.56 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1462 EERDRAEAEAREKETKalsLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTql 1541
Cdd:pfam00261 8 EELDEAEERLKEAMKK---LEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKV-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1542 eeLEDELQATEDAKLRLEVNLQAMKaqferdlqGRDEQSEEKKKQLVRQVREMEAELE--DERKQRSIAMAARKKLEM-- 1617
Cdd:pfam00261 83 --LENRALKDEEKMEILEAQLKEAK--------EIAEEADRKYEEVARKLVVVEGDLEraEERAELAESKIVELEEELkv 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1618 ---DLKDLEAHIDTANKNREEAIKQLRKLQAQMKdcmrelddtrasreEILAQAKENEKKLKSMEAEMIQLQEELAAAER 1694
Cdd:pfam00261 153 vgnNLKSLEASEEKASEREDKYEEQIRFLTEKLK--------------EAETRAEFAERSVQKLEKEVDRLEDELEAEKE 218
|
250
....*....|
gi 806638593 1695 AKRQAQQERD 1704
Cdd:pfam00261 219 KYKAISEELD 228
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
851-1131 |
7.06e-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: 47.37 E-value: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 851 EAELTKVREKHLAAENRLTEMETMQSQLmAEKLQLQEQ----LQAETElcAEAEELrARLTAKKQELEEICHDLEARVEE 926
Cdd:pfam19220 138 EEENKALREEAQAAEKALQRAEGELATA-RERLALLEQenrrLQALSE--EQAAEL-AELTRRLAELETQLDATRARLRA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 927 EEERCQYLQAEKKKMQQNIQELEEQLEEEESArQKLQLEKVTTEAklkkLEEDQIIMEDQNcklakekkLLEDRVAEFTt 1006
Cdd:pfam19220 214 LEGQLAAEQAERERAEAQLEEAVEAHRAERAS-LRMKLEALTARA----AATEQLLAEARN--------QLRDRDEAIR- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1007 nlmEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQ 1086
Cdd:pfam19220 280 ---AAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIA 356
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 806638593 1087 AALARVEEEAAqknmalkkirELETQISELQEDLESERACRNKAE 1131
Cdd:pfam19220 357 ELTKRFEVERA----------ALEQANRRLKEELQRERAERALAQ 391
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
842-1374 |
7.16e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.81 E-value: 7.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 842 RHEDELLAKEAELTKVREKHLAAENRLTEM----------ETMQSQLMAEKLQLQEQL-QAETELCAEAEELRARLTAKK 910
Cdd:pfam05557 45 RESDRNQELQKRIRLLEKREAEAEEALREQaelnrlkkkyLEALNKKLNEKESQLADArEVISCLKNELSELRRQIQRAE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 911 QELEEICHDLEArveeEEERCQYLQAEKKKMQQNIQELEEQLEEEESARQKLQlekvTTEAKLKKLEEDQIIMEDQNCKL 990
Cdd:pfam05557 125 LELQSTNSELEE----LQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIK----ELEFEIQSQEQDSEIVKNSKSEL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 991 AkekklledRVAEFTTNLMEEEEKSKSLAKLKNKHEAM---ITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAEL 1067
Cdd:pfam05557 197 A--------RIPELEKELERLREHNKHLNENIENKLLLkeeVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1068 QAQIAELK--MQLAKKEEELQAA-LARVEE-----------EAAQKNMAlKKIRELETQISELQEDLESERACRNKAEKQ 1133
Cdd:pfam05557 269 QDTGLNLRspEDLSRRIEQLQQReIVLKEEnssltssarqlEKARRELE-QELAQYLKKIEDLNKKLKRHKALVRRLQRR 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1134 KRDLGEELEALKTELEdTLDSTAAQQELRSKREQEVsilkKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKA 1213
Cdd:pfam05557 348 VLLLTKERDGYRAILE-SYDKELTMSNYSPQLLERI----EEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLER 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1214 TLEKAK-QTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQvkfsegervrteladkvskLQVELDSVTGLLNQS 1292
Cdd:pfam05557 423 ELQALRqQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELE-------------------MELERRCLQGDYDPK 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1293 DSKSSKLTKDFSAL-ESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEeakrnlEKQIATLHAQVTDMKK 1371
Cdd:pfam05557 484 KTKVLHLSMNPAAEaYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMN------FKEVLDLRKELESAEL 557
|
...
gi 806638593 1372 KME 1374
Cdd:pfam05557 558 KNQ 560
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1653-1909 |
7.73e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1653 ELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIAnssgkgalALEEK-RRLEARI 1731
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA--------EAEAEiEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1732 AQLEEELEEEQGNTELINDRLKKANLQ--IDQINTDLNLERSHAQKNE---NARQQLERQNKELKAKLQEMESAvkskyk 1806
Cdd:COG3883 89 GERARALYRSGGSVSYLDVLLGSESFSdfLDRLSALSKIADADADLLEelkADKAELEAKKAELEAKLAELEAL------ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1807 asIAALEAKIAQLEEQLDNETKERQAASKQVRRAEKKLKDVLLQVEDERRNAEQfKDQADKASTRLKQLKRQLEEAEEEA 1886
Cdd:COG3883 163 --KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA-AAAAAAAAAAAAAAAAAAAAAAAAA 239
|
250 260
....*....|....*....|...
gi 806638593 1887 QRANASRRKLQRELEDATETADA 1909
Cdd:COG3883 240 AAAAASAAGAGAAGAAGAAAGSA 262
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
965-1503 |
7.86e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.81 E-value: 7.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 965 EKVTTEAKLKKLEEDQIIMEDQNcklAKEKKLLEDRVAEFTTNLMEEEEKSKSLaklknkhEAMITDLEERL-RREEKQR 1043
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEH---KRARIELEKKASALKRQLDRESDRNQEL-------QKRIRLLEKREaEAEEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1044 QELEKTRRKLEGDST-------------DLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELE 1110
Cdd:pfam05557 73 EQAELNRLKKKYLEAlnkklnekesqlaDAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1111 TQISELQEDLESERACRNKAEKQKRDL------GEELEALKTELEDTLDSTAAQQELRSKREQ-------------EVSI 1171
Cdd:pfam05557 153 QLRQNLEKQQSSLAEAEQRIKELEFEIqsqeqdSEIVKNSKSELARIPELEKELERLREHNKHlnenienklllkeEVED 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1172 LKKTLEDEAKTHEAQIQ-EMRQKHSQAVEELAEQLEQT-----------KRVKATLEKAKQTLENERGELANEVKALLQG 1239
Cdd:pfam05557 233 LKRKLEREEKYREEAATlELEKEKLEQELQSWVKLAQDtglnlrspedlSRRIEQLQQREIVLKEENSSLTSSARQLEKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1240 KGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVSKLQVELDSVTGLLNQSDSK------SSKLTKDFSALESQLQDT 1313
Cdd:pfam05557 313 RRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKEltmsnySPQLLERIEEAEDMTQKM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1314 QELLQEenrqklsLSTKLKQMEDEKNSFREQLeeeeeakrnlekqiATLHAQVTDMKKK--MEDGVGCLETAEEAKRRLQ 1391
Cdd:pfam05557 393 QAHNEE-------MEAQLSVAEEELGGYKQQA--------------QTLERELQALRQQesLADPSYSKEEVDSLRRKLE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1392 kDLEGLSQRLEEKVAAYDkLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKK--FDQLLAEEKTISAKYAEERDRAEA 1469
Cdd:pfam05557 452 -TLELERQRLREQKNELE-MELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKnqLEKLQAEIERLKRLLKKLEDDLEQ 529
|
570 580 590
....*....|....*....|....*....|....
gi 806638593 1470 EAREKETkalSLARALEEAMEQKAELERLNKQFR 1503
Cdd:pfam05557 530 VLRLPET---TSTMNFKEVLDLRKELESAELKNQ 560
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1041-1276 |
8.02e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 47.38 E-value: 8.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1041 KQRQELEKTRRKLEGDSTDLSDQIAELQAQIAEL-KMQLAKKE-EELQAA---LARVEEEAAQKNMALKKIRELE----T 1111
Cdd:COG0497 165 RAWRALKKELEELRADEAERARELDLLRFQLEELeAAALQPGEeEELEEErrrLSNAEKLREALQEALEALSGGEggalD 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1112 QISELQEDLESeracRNKAEKQKRDLGEELEALKTELEDtldstaAQQELRSKREQevsilkktLE-DEAKTHE-----A 1185
Cdd:COG0497 245 LLGQALRALER----LAEYDPSLAELAERLESALIELEE------AASELRRYLDS--------LEfDPERLEEveerlA 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1186 QIQEMRQKHSQAVEEL-------AEQLEQTKRVKATLEKAKQTLENERGELANEVKALlqgkgdSEhKRKK--------V 1250
Cdd:COG0497 307 LLRRLARKYGVTVEELlayaeelRAELAELENSDERLEELEAELAEAEAELLEAAEKL------SA-ARKKaakklekaV 379
|
250 260 270
....*....|....*....|....*....|...
gi 806638593 1251 EAQLQEL-------QVKFSEGERVRTELADKVS 1276
Cdd:COG0497 380 TAELADLgmpnarfEVEVTPLEEPGPNGADQVE 412
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1051-1339 |
8.40e-05 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 47.54 E-value: 8.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1051 RKLEGDSTDlsdqIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKnmaLKKirELETQISE------LQEDLESER 1124
Cdd:PLN03229 422 KKREAVKTP----VRELEGEVEKLKEQILKAKESSSKPSELALNEMIEK---LKK--EIDLEYTEaviamgLQERLENLR 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1125 ACRNKAEKQK----RDLGEELEALKTELEDTLDSTAAQQELRSKRE--QEVSILKKTLEDEAKTheaqiQEMRQKHSQAV 1198
Cdd:PLN03229 493 EEFSKANSQDqlmhPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDmlNEFSRAKALSEKKSKA-----EKLKAEINKKF 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1199 EELAEQLEQTKRVKATLEKAKQTLENERGELANEVK-ALLQGKGDSEHKRKKVEAQLqELQVKFSEGERVRT-------E 1270
Cdd:PLN03229 568 KEVMDRPEIKEKMEALKAEVASSGASSGDELDDDLKeKVEKMKKEIELELAGVLKSM-GLEVIGVTKKNKDTaeqtpppN 646
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 806638593 1271 LADKVSKLQVELDS-VTGLLNQSDSKS------SKLTKDFSALESQLQDTQELLQEENRQKLSL---STKLKQMEDEKN 1339
Cdd:PLN03229 647 LQEKIESLNEEINKkIERVIRSSDLKSkiellkLEVAKASKTPDVTEKEKIEALEQQIKQKIAEalnSSELKEKFEELE 725
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
1480-1587 |
9.34e-05 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 44.61 E-value: 9.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1480 SLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLE 1559
Cdd:pfam11559 42 ELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLK 121
|
90 100
....*....|....*....|....*...
gi 806638593 1560 VNLQAMKAQFERDLQGRDEQSEEKKKQL 1587
Cdd:pfam11559 122 NALQQIKTQFAHEVKKRDREIEKLKERL 149
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1056-1167 |
9.48e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 46.58 E-value: 9.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1056 DSTDLSDQIAELQAQIAELKMQLAKKE---------EELQAALARVEEEAAQKNMALKKIRELETQ--ISelQEDLESER 1124
Cdd:COG1566 77 DPTDLQAALAQAEAQLAAAEAQLARLEaelgaeaeiAAAEAQLAAAQAQLDLAQRELERYQALYKKgaVS--QQELDEAR 154
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 806638593 1125 ACRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQ 1167
Cdd:COG1566 155 AALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAA 197
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1026-1281 |
9.76e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.44 E-value: 9.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1026 EAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKK 1105
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1106 IRELETQISELQEdlesERACRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQEL--RSKR-EQEVSILKKTLEDEAKT 1182
Cdd:COG1340 87 LNELREELDELRK----ELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELveKIKElEKELEKAKKALEKNEKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1183 HE--AQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQTLENERGElANEVKALLQGKGDsehKRKKVEAQLQELQVK 1260
Cdd:COG1340 163 KElrAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKE-ADELHKEIVEAQE---KADELHEEIIELQKE 238
|
250 260
....*....|....*....|.
gi 806638593 1261 FSEGERVRTELADKVSKLQVE 1281
Cdd:COG1340 239 LRELRKELKKLRKKQRALKRE 259
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1460-1640 |
9.98e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 47.01 E-value: 9.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1460 YAEERDRAEAEAREKEtkalslARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKT 1539
Cdd:PRK12705 26 KKRQRLAKEAERILQE------AQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1540 qLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVrqVREMEAELEDERKQRSIAMAARKKLEMDL 1619
Cdd:PRK12705 100 -LDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLL--LKLLDAELEEEKAQRVKKIEEEADLEAER 176
|
170 180
....*....|....*....|.
gi 806638593 1620 KDLEAHIDTANKNREEAIKQL 1640
Cdd:PRK12705 177 KAQNILAQAMQRIASETASDL 197
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1631-1913 |
1.05e-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: 47.43 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1631 KNREEAIKQLRKLQAQMKDCMRELDDTRASRE-EILAQAK---ENEKKLKSMEAEMIQLQEElaaaERAKRQAQQERDEL 1706
Cdd:pfam17380 295 KMEQERLRQEKEEKAREVERRRKLEEAEKARQaEMDRQAAiyaEQERMAMERERELERIRQE----ERKRELERIRQEEI 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1707 ADEIANSSGKGALALEEKRRLEaRIAQLEEELEEEQGNTELINDRLKKANLQIDQINTdlnlERSHAQKNENARQQLERQ 1786
Cdd:pfam17380 371 AMEISRMRELERLQMERQQKNE-RVRQELEAARKVKILEEERQRKIQQQKVEMEQIRA----EQEEARQREVRRLEEERA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1787 NKELKAKLQEMEsavKSKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRA-EKKLKDVLLQ-VEDERRNAEQFKDQ 1864
Cdd:pfam17380 446 REMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAmIEEERKRKLLEKEM 522
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 806638593 1865 ADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETA---DAMNRE 1913
Cdd:pfam17380 523 EERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERsrlEAMERE 574
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1663-1858 |
1.30e-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: 45.69 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1663 EILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIanssgkgalaleekRRLEARIAQleeeleeeq 1742
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI--------------KRLELEIEE--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1743 gntelINDRLKKANLQIDQINT-----DLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSKYKASIAALEAKIA 1817
Cdd:COG1579 71 -----VEARIKKYEEQLGNVRNnkeyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 806638593 1818 QLEEQLDNETKERQAASKQVRRAEKKLKDVLLQVEDERRNA 1858
Cdd:COG1579 146 ELDEELAELEAELEELEAEREELAAKIPPELLALYERIRKR 186
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1071-1221 |
1.43e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1071 IAELKMQLAKKEEELQAALARVEEEAAQKnmalKKIRELETQISELQEDLESE-RACRNKAEKQKRDLGEELEALKTELE 1149
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKK----EALLEAKEEIHKLRNEFEKElRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1150 DTLDSTA---AQQELRSKREQEVSILKKTLEdeaKTHEAQIQEMRQ----KHSQAVEELAEQLEQ------TKRVKATLE 1216
Cdd:PRK12704 104 LLEKREEeleKKEKELEQKQQELEKKEEELE---ELIEEQLQELERisglTAEEAKEILLEKVEEearheaAVLIKEIEE 180
|
....*
gi 806638593 1217 KAKQT 1221
Cdd:PRK12704 181 EAKEE 185
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
995-1283 |
1.46e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 46.07 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 995 KLLEDRVAEFTtnlmeeeEKSKSLAKLKNKHEAMITDLEERLRREEKQRQEL-EKTRRklegdstDLSDQIAELQAQIAE 1073
Cdd:pfam00038 7 QELNDRLASYI-------DKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLyEKEIE-------DLRRQLDTLTVERAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1074 LKMQLAKKEEELQAALARVEEEAAQKnmalkkiRELETQISELQEDLESERACRNKAEKQKRDLGEELEALKTELED--- 1150
Cdd:pfam00038 73 LQLELDNLRLAAEDFRQKYEDELNLR-------TSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEevr 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1151 -------------------TLDSTAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRV 1211
Cdd:pfam00038 146 elqaqvsdtqvnvemdaarKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRT 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 806638593 1212 KATLEkakQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQvkfSEGERVRTELADKVSKLQVELD 1283
Cdd:pfam00038 226 IQSLE---IELQSLKKQKASLERQLAETEERYELQLADYQELISELE---AELQETRQEMARQLREYQELLN 291
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1467-1715 |
1.47e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1467 AEAEAREKETKALSLARALEEAMEQKAELERlnkqfrtEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELED 1546
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQA-------ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1547 EL-------QATEDAKLRLEVNLQA-------MKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQrsiAMAAR 1612
Cdd:COG3883 87 ELgeraralYRSGGSVSYLDVLLGSesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE---LEALK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1613 KKLEMDLKDLEAHIDTAnknrEEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAA 1692
Cdd:COG3883 164 AELEAAKAELEAQQAEQ----EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
250 260
....*....|....*....|...
gi 806638593 1693 ERAKRQAQQERDELADEIANSSG 1715
Cdd:COG3883 240 AAAAASAAGAGAAGAAGAAAGSA 262
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1024-1364 |
1.51e-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: 46.43 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1024 KHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEA------- 1096
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEekykels 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1097 --------------AQKNMALKKIRELETQISEL-QEDLESERACRNKAEKQKRDLGE--ELEALKTELEDTLDSTAAQQ 1159
Cdd:pfam07888 108 asseelseekdallAQRAAHEARIRELEEDIKTLtQRVLERETELERMKERAKKAGAQrkEEEAERKQLQAKLQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1160 ELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQ---LEQTKRVKATLEKAKQTLENERGELANEVKAl 1236
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENealLEELRSLQERLNASERKVEGLGEELSSMAAQ- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1237 lQGKGDSEHKRKKVEA-----QLQELQVKFSEGErvrteladkvSKLQVELdsvTGLLNQSDSKSSKLTKdfsaLESQLQ 1311
Cdd:pfam07888 267 -RDRTQAELHQARLQAaqltlQLADASLALREGR----------ARWAQER---ETLQQSAEADKDRIEK----LSAELQ 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 806638593 1312 DTQELLQEENRQKLSLSTKLKQmedEKNSFREQLeeeEEAKRNLEKQIATLHA 1364
Cdd:pfam07888 329 RLEERLQEERMEREKLEVELGR---EKDCNRVQL---SESRRELQELKASLRV 375
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1679-1846 |
1.66e-04 |
|
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: 45.88 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1679 EAEMIQLQEELAAAERAKRQAQQERDELadeianssgkgalaleekRRLEARIAQLEEELEEEQGNTELINDRLKKANLQ 1758
Cdd:pfam00529 57 QAALDSAEAQLAKAQAQVARLQAELDRL------------------QALESELAISRQDYDGATAQLRAAQAAVKAAQAQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1759 IDQINTDLNLERSHAQKN-------ENARQQLERQNKELKAKLQEMESAvkskYKASIAALEAKIAQLEEQLDNETKERQ 1831
Cdd:pfam00529 119 LAQAQIDLARRRVLAPIGgisreslVTAGALVAQAQANLLATVAQLDQI----YVQITQSAAENQAEVRSELSGAQLQIA 194
|
170
....*....|....*
gi 806638593 1832 AASKQVRRAEKKLKD 1846
Cdd:pfam00529 195 EAEAELKLAKLDLER 209
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
990-1115 |
1.77e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.11 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 990 LAKEKKL-LEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLrreekqrQELEKTRRKLEGDSTDLSDQIAELQ 1068
Cdd:PRK09039 71 LERQGNQdLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRA-------GELAQELDSEKQVSARALAQVELLN 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 806638593 1069 AQIAELKMQLAKKEEELQAALARVEEEAAQ-------KNMAL-KKIRELETQISE 1115
Cdd:PRK09039 144 QQIAALRRQLAALEAALDASEKRDRESQAKiadlgrrLNVALaQRVQELNRYRSE 198
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1455-1909 |
1.77e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 46.44 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1455 TISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQV 1534
Cdd:COG5278 72 TGDESFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALM 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1535 EEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSIAMAARKK 1614
Cdd:COG5278 152 DEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1615 LEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAER 1694
Cdd:COG5278 232 LELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1695 AKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQ 1774
Cdd:COG5278 312 AAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELE 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1775 KNENARQQLERQNKELKAKLQEMESAVKSKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRAEKKLKDVLLQVEDE 1854
Cdd:COG5278 392 VLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAV 471
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 806638593 1855 RRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADA 1909
Cdd:COG5278 472 AALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALA 526
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1102-1263 |
1.81e-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: 45.30 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1102 ALKKIRELETQISELQEDLESERACRNKAEKQKRDLGEELEALKTELEDT-LDSTAAQQELRSKREQEVSILKK----TL 1176
Cdd:COG1579 8 ALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLeKEIKRLELEIEEVEARIKKYEEQlgnvRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1177 EDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQE 1256
Cdd:COG1579 88 NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
....*..
gi 806638593 1257 LQVKFSE 1263
Cdd:COG1579 168 LAAKIPP 174
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
983-1151 |
1.84e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 983 MEDQNCKLAKEKKLLEDRVAEFTTNL-MEEEEKSKSLAKLKNKHEAMITDLEeRLRREEKQRQElektrrklEGDSTDLS 1061
Cdd:PHA02562 221 KYDELVEEAKTIKAEIEELTDELLNLvMDIEDPSAALNKLNTAAAKIKSKIE-QFQKVIKMYEK--------GGVCPTCT 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1062 DQIAELQAQIAELK---MQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERACRNKAEK------ 1132
Cdd:PHA02562 292 QQISEGPDRITKIKdklKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAaieelq 371
|
170 180
....*....|....*....|
gi 806638593 1133 -QKRDLGEELEALKTELEDT 1151
Cdd:PHA02562 372 aEFVDNAEELAKLQDELDKI 391
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1036-1167 |
1.90e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.73 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1036 LRRE-EKQRQELEKTRRKLegdsTDLSDQIA-------ELQAQIAELKMQLAKKEEE---LQAALARVEEEAAqknmalk 1104
Cdd:PRK09039 44 LSREiSGKDSALDRLNSQI----AELADLLSlerqgnqDLQDSVANLRASLSAAEAErsrLQALLAELAGAGA------- 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 806638593 1105 kirELETQISELQEDLESERACRNKAEKQKRDLGEELEALKTEL---EDTLDstAAQQELRSKREQ 1167
Cdd:PRK09039 113 ---AAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLaalEAALD--ASEKRDRESQAK 173
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1619-1873 |
2.04e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.84 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1619 LKDLEAHIDTANKNREEAIKQLRKLQAQMKD-------CMRELDDTRASREEIlaqakenEKKLKSMEAEMIQLQeelaa 1691
Cdd:PRK11637 49 LKSIQQDIAAKEKSVRQQQQQRASLLAQLKKqeeaisqASRKLRETQNTLNQL-------NKQIDELNASIAKLE----- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1692 aeraKRQAQQERDeLADEIANSSGKG---ALAL----EEKRRLEaRIaqleeeleeeQGNTELINDRLKKANLQIDQINT 1764
Cdd:PRK11637 117 ----QQQAAQERL-LAAQLDAAFRQGehtGLQLilsgEESQRGE-RI----------LAYFGYLNQARQETIAELKQTRE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1765 DLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSKYKASIAALEAKIAQLEEQLDNETKERQaaskQVRRAEKKL 1844
Cdd:PRK11637 181 ELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRD----SIARAEREA 256
|
250 260 270
....*....|....*....|....*....|..
gi 806638593 1845 KdvlLQVEDERRNAEQFKD---QADKASTRLK 1873
Cdd:PRK11637 257 K---ARAEREAREAARVRDkqkQAKRKGSTYK 285
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1075-1221 |
2.16e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.39 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1075 KMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEdleseracrnkaekQKRDLGEELEALK---TELEDT 1151
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA--------------EVEELEAELEEKDeriERLERE 449
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1152 LDSTAAQQELRSKREQEVSILKKtledEAKTHEAQIQEMRQKhsqaVEELAEQLEQTKRVKATLEKAKQT 1221
Cdd:COG2433 450 LSEARSEERREIRKDREISRLDR----EIERLERELEEERER----IEELKRKLERLKELWKLEHSGELV 511
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
999-1270 |
2.16e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.01 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 999 DRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERL-RREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQ 1077
Cdd:pfam02029 34 ESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKReERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1078 LAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERACRNKAEKQKRD--LGEELEALKTELEDTLDST 1155
Cdd:pfam02029 114 SWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTEnfAKEEVKDEKIKKEKKVKYE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1156 AAQQELRSKREQEVsilkKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQlEQTKRVKAtlEKAKQTLENERGELANEVKA 1235
Cdd:pfam02029 194 SKVFLDQKRGHPEV----KSQNGEEEVTKLKVTTKRRQGGLSQSQEREE-EAEVFLEA--EQKLEELRRRRQEKESEEFE 266
|
250 260 270
....*....|....*....|....*....|....*
gi 806638593 1236 LLQgkgdseHKRKKVEAQLQELQVKFSEGERVRTE 1270
Cdd:pfam02029 267 KLR------QKQQEAELELEELKKKREERRKLLEE 295
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1382-1611 |
2.25e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1382 TAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDllvdldhQRQSVSNLEKKQKKFDQLLAE-EKTISAKY 1460
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE-------LQAELEALQAEIDKLQAEIAEaEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1461 AEERDRAEAEAREKET----KALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDdvgksvhELEKSKRALEQQVEE 1536
Cdd:COG3883 86 EELGERARALYRSGGSvsylDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKA-------ELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 806638593 1537 MKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSIAMAA 1611
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| BicD |
pfam09730 |
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ... |
1079-1548 |
2.60e-04 |
|
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled domains and are involved in dynein-mediated minus end-directed transport from the Golgi apparatus to the endoplasmic reticulum (ER). For full functioning they bind with GSK-3beta pfam05350 to maintain the anchoring of microtubules to the centromere. It appears that amino-acid residues 437-617 of BicD and the kinase activity of GSK-3 are necessary for the formation of a complex between BicD and GSK-3beta in intact cells.
Pssm-ID: 462863 [Multi-domain] Cd Length: 717 Bit Score: 46.01 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1079 AKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERACrnkAEKQKRDLGEELEALKTELEDTLDSTAAQ 1158
Cdd:pfam09730 26 ASKEAYYAQRILELQNELKQARAVLSNTQAENERLASLSQELKEECEC---VELQRGRMRDEIKEYKVREARLLQDYSEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1159 QELRSKREQEVSILKKT-LEDEAKTHEAQIQEMRQkhsqavEELAEQLEQTKRVKA----TLEKAKQTLENERgELANEV 1233
Cdd:pfam09730 103 EEENISLQKQVSVLKQNqVEFEGLKHEITRKEEET------ELLNSQLEEAIRLREiaerQLDEALETLKTER-EQKNSL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1234 KALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVSKLQVELDSVTGLLNQSDSKSSKLTKDFSALESQLQDT 1313
Cdd:pfam09730 176 RKELSHYMTLNDFDYVSHLSISLDGLKFSEDEGAGTEPNNDGEAMDGGENGGGGLKNSGLDNRTSTPRKSEVFPPAPSLV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1314 QELLQEENrqkLSLSTKLKQmedeknsfreQLEEeeeakrnLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKD 1393
Cdd:pfam09730 256 SDLLSELN---ISEIQKLKQ----------QLIQ-------VEREKVSLLSTLQESQKQLEQAKGALSEQQEKVNRLTEN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1394 LEGLsQRLEEKVAAYDKLEKTKTRLQQELDD--------LLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERD 1465
Cdd:pfam09730 316 LEAM-RGLQASKERQDALDSEKDRDSHEDGDyyevdingPEILECKYRVAVEEAGELREELKALKARYNTLEERYKEEKT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1466 RAEAEAreketkalslaralEEAMEQKAELERLNKQFRTEMEdlmsskddvgksvhELEKSKRALEQQVEEMKTQLEELE 1545
Cdd:pfam09730 395 RWEAEA--------------QDLAEKIRQLEKASHQDQERIA--------------HLEKELGKTRKVAGESEGSLSVAQ 446
|
...
gi 806638593 1546 DEL 1548
Cdd:pfam09730 447 DEL 449
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
994-1145 |
2.61e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 45.39 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 994 KKLLEDRVAEFTTNLM----EEEEKSKSLAKLKNKHEAmITDLEERLRREEKQRQELEKTRRKLEGDSTD-LSDQIAELQ 1068
Cdd:smart00787 139 MKLLEGLKEGLDENLEglkeDYKLLMKELELLNSIKPK-LRDRKDALEEELRQLKQLEDELEDCDPTELDrAKEKLKKLL 217
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 806638593 1069 AQIAELKMQLAKKEEELQAALARVEEEAAQKNmalkkirELETQISELQEDLESERACRNKAEKQKRDLGEELEALK 1145
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKS-------ELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1611-1924 |
2.63e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1611 ARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELa 1690
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1691 aaeRAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQleeeleeeqgntelindrlkkanLQIDQINTDLNLER 1770
Cdd:COG1340 81 ---DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIER-----------------------LEWRQQTEVLSPEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1771 shaqknenaRQQLERQNKELKAKLQEMESAVKSKYKasIAALEAKIAQLEEQLDNETKERQAASKQVRRAEKKLKDVLLQ 1850
Cdd:COG1340 135 ---------EKELVEKIKELEKELEKAKKALEKNEK--LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKE 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 806638593 1851 VEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDA--TETADAMNREVSSLKNKLRRG 1924
Cdd:COG1340 204 ADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALkrEKEKEELEEKAEEIFEKLKKG 279
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1520-1907 |
2.77e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 45.79 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1520 VHELEKSKRAleqqVEEMKTQLEELE-DELQATED---AKLRLEvnlqamkaqfERDLQGRDEQSEEKKKQLvrqvreme 1595
Cdd:pfam05701 69 LEELESTKRL----IEELKLNLERAQtEEAQAKQDselAKLRVE----------EMEQGIADEASVAAKAQL-------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1596 aELEDERKQRSIA--MAARKKLEMDLKDLEAHI---DTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREeiLAQAKE 1670
Cdd:pfam05701 127 -EVAKARHAAAVAelKSVKEELESLRKEYASLVserDIAIKRAEEAVSASKEIEKTVEELTIELIATKESLE--SAHAAH 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1671 NEKKLKSMEAEMIQLQEELAAaERAKRQAQQERDELADEIANS-------SGKGALALEEKRRLEARIAQLEEELEEEQG 1743
Cdd:pfam05701 204 LEAEEHRIGAALAREQDKLNW-EKELKQAEEELQRLNQQLLSAkdlksklETASALLLDLKAELAAYMESKLKEEADGEG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1744 NTELINDRLKKA-----------NLQIDQINTDLNLERSHAqknENARQQLERQNKELkAKLQEMESavkskyKASIAal 1812
Cdd:pfam05701 283 NEKKTSTSIQAAlasakkeleevKANIEKAKDEVNCLRVAA---ASLRSELEKEKAEL-ASLRQREG------MASIA-- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1813 eakIAQLEEQLDNETKERQAASKQVRRAEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANAS 1892
Cdd:pfam05701 351 ---VSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESR 427
|
410
....*....|....*
gi 806638593 1893 RRKLQRELEDATETA 1907
Cdd:pfam05701 428 LEAVLKEIEAAKASE 442
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
850-1192 |
2.79e-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: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 850 KEAELTKVREKHLAAENRLTEMETMQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEeee 929
Cdd:pfam07888 57 REKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRE--- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 930 rcqyLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTTNLM 1009
Cdd:pfam07888 134 ----LEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1010 EEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSD-------QIAEL---QAQIAELKMQLA 1079
Cdd:pfam07888 210 QLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSmaaqrdrTQAELhqaRLQAAQLTLQLA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1080 KKEEELQAALAR--VEEEAAQKNMALKK--IRELETQISELQEDLESERACRNKaekqkrdlgeeleaLKTELEDTLDST 1155
Cdd:pfam07888 290 DASLALREGRARwaQERETLQQSAEADKdrIEKLSAELQRLEERLQEERMEREK--------------LEVELGREKDCN 355
|
330 340 350
....*....|....*....|....*....|....*..
gi 806638593 1156 AAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQ 1192
Cdd:pfam07888 356 RVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLE 392
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1033-1212 |
2.82e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 45.63 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1033 EERLRREEKQRQ-ELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQlAKKEEELQAALARVEEEAAQKNMalkkirELET 1111
Cdd:COG2268 211 ETEIAIAQANREaEEAELEQEREIETARIAEAEAELAKKKAEERRE-AETARAEAEAAYEIAEANAEREV------QRQL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1112 QISELQEDLESERACRNKAEKQ-KRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVsiLKKTLEDEAKTHEAQIQEM 1190
Cdd:COG2268 284 EIAEREREIELQEKEAEREEAElEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEG--KRALAEAWNKLGDAAILLM 361
|
170 180
....*....|....*....|...
gi 806638593 1191 R-QKHSQAVEELAEQLEQTKRVK 1212
Cdd:COG2268 362 LiEKLPEIAEAAAKPLEKIDKIT 384
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1375-1604 |
2.83e-04 |
|
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: 46.37 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1375 DGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKL------EKTKTRLQQELDDllvdldhQRQSVSNLEKKQKKFDQ 1448
Cdd:NF012221 1525 DGLGYILDNVVATSESSQQADAVSKHAKQDDAAQNALadkeraEADRQRLEQEKQQ-------QLAAISGSQSQLESTDQ 1597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1449 LLAEEKTISakyaeERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTE-----MEDLMSSKDDVGKSVHE- 1522
Cdd:NF012221 1598 NALETNGQA-----QRDAILEESRAVTKELTTLAQGLDALDSQATYAGESGDQWRNPfagglLDRVQEQLDDAKKISGKq 1672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1523 LEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFER-----DLQGRDEQSEEKKKQLVRQvremEAE 1597
Cdd:NF012221 1673 LADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKrkddaLAKQNEAQQAESDANAAAN----DAQ 1748
|
....*..
gi 806638593 1598 LEDERKQ 1604
Cdd:NF012221 1749 SRGEQDA 1755
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1056-1240 |
2.84e-04 |
|
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: 45.11 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1056 DSTDLSDQIAELQAQIAelkmqlakkeeELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERACRNKAEkqkr 1135
Cdd:pfam00529 52 DPTDYQAALDSAEAQLA-----------KAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQ---- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1136 dlgEELEALKTELEDTlDSTAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTK-RVKAT 1214
Cdd:pfam00529 117 ---AQLAQAQIDLARR-RVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELsGAQLQ 192
|
170 180
....*....|....*....|....*..
gi 806638593 1215 LEKAKQTLENERGELAN-EVKALLQGK 1240
Cdd:pfam00529 193 IAEAEAELKLAKLDLERtEIRAPVDGT 219
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1564-1731 |
3.09e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1564 AMKAQFER--DLQGRDEQSEEKKKQLvrqvREMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLR 1641
Cdd:COG1579 1 AMPEDLRAllDLQELDSELDRLEHRL----KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1642 KLQAQM---------KDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIAN 1712
Cdd:COG1579 77 KYEEQLgnvrnnkeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
170
....*....|....*....
gi 806638593 1713 ssgKGALALEEKRRLEARI 1731
Cdd:COG1579 157 ---ELEELEAEREELAAKI 172
|
|
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
1618-1712 |
3.16e-04 |
|
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439942 [Multi-domain] Cd Length: 421 Bit Score: 45.38 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1618 DLKDLEAHIDT-----ANKNREEAIKQLRKLQAQMKDCMRELDDTRASR----EEIlAQAKENEKKLKSMEAEMIQLQEE 1688
Cdd:COG0172 3 DIKLIRENPEAvkealAKRGFDLDVDELLELDEERRELQTEVEELRAERnalsKEI-GKAKKKGEEAEALIAEVKELKEE 81
|
90 100
....*....|....*....|....
gi 806638593 1689 LAAAERAKRQAQQERDELADEIAN 1712
Cdd:COG0172 82 IKELEEELKELEEELDELLLSIPN 105
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1616-1822 |
3.35e-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: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1616 EMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAaaERA 1695
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG--ERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1696 KRQAQQER-----------DELADEIANSSGKGALA----------LEEKRRLEARIAQLEEELEEEQGNTELINDRLKK 1754
Cdd:COG3883 93 RALYRSGGsvsyldvllgsESFSDFLDRLSALSKIAdadadlleelKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 806638593 1755 ANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSKYKASIAALEAKIAQLEEQ 1822
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1656-1927 |
3.64e-04 |
|
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: 45.98 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1656 DTRASREEILAQAKENEKKLKSMEAEMIQLQEElAAAERAKRQAQQERDELADEIANSSGKgaLALEEKRRLEAriaQLE 1735
Cdd:NF012221 1532 DNVVATSESSQQADAVSKHAKQDDAAQNALADK-ERAEADRQRLEQEKQQQLAAISGSQSQ--LESTDQNALET---NGQ 1605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1736 EELEEEQGNTELINDRLKKANLQIDQINTDLNlershaQKNENARQQLERQNKELKAKLQEMESAVKSKYKASIAALEAK 1815
Cdd:NF012221 1606 AQRDAILEESRAVTKELTTLAQGLDALDSQAT------YAGESGDQWRNPFAGGLLDRVQEQLDDAKKISGKQLADAKQR 1679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1816 IAQLEEQLDNETKERQAAskqVRRAEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAeeeaqrANASRRK 1895
Cdd:NF012221 1680 HVDNQQKVKDAVAKSEAG---VAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAA------ANDAQSR 1750
|
250 260 270
....*....|....*....|....*....|..
gi 806638593 1896 LQRELEDATETADAMNREVSSLknKLRRGDMP 1927
Cdd:NF012221 1751 GEQDASAAENKANQAQADAKGA--KQDESDKP 1780
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1727-1926 |
3.74e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1727 LEARIAQLEEELEEEQGNTELIN-DRLKKANLQIDQI---NTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVK 1802
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNlKELKELEEELKEAeekEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1803 -SKYKASIAALEAKIAQLEEQLDnETKERQAASKQVRRAEKKLKDVLLQVEDERRNAEQFKDQADKAstRLKQLKRQLee 1881
Cdd:COG4717 127 lLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE--ELQDLAEEL-- 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 806638593 1882 aeeeaQRANASRRKLQRELEDATETADAMNREVSSLKNKLRRGDM 1926
Cdd:COG4717 202 -----EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
863-1100 |
4.05e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 863 AAENRLTEMETMQSQLMAEKLQLQEQLQAETElcaEAEELRARLTAKKQELEEichdlearveeeeercqyLQAEKKKMQ 942
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNE---EYNELQAELEALQAEIDK------------------LQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 943 QNIQELEEQLEEEESARQKlqlekvtTEAKLKKLEedqIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEeeksksLAKLK 1022
Cdd:COG3883 79 AEIEERREELGERARALYR-------SGGSVSYLD---VLLGSESFSDFLDRLSALSKIADADADLLEE------LKADK 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 806638593 1023 NKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKN 1100
Cdd:COG3883 143 AELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1527-1699 |
4.13e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1527 KRALEQQVEEMKTQ----LEELEDELQATEDAKLrLEVN--LQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELED 1600
Cdd:PRK12704 26 KKIAEAKIKEAEEEakriLEEAKKEAEAIKKEAL-LEAKeeIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1601 ERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDcmrelddtrASREEILAQAKEnekKLKSMEA 1680
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE---------EAKEILLEKVEE---EARHEAA 172
|
170
....*....|....*....
gi 806638593 1681 EMIQLQEELAAAErAKRQA 1699
Cdd:PRK12704 173 VLIKEIEEEAKEE-ADKKA 190
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1384-1591 |
4.27e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1384 EEAKRRLQKDleglSQRLEEKVAaydKLEKTKTRLQQElddllvdldhqRQSVSNLEKKQKKFDQLLAEEKtisAKYAEE 1463
Cdd:PRK00409 505 EEAKKLIGED----KEKLNELIA---SLEELERELEQK-----------AEEAEALLKEAEKLKEELEEKK---EKLQEE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1464 RDRAEAEAREKETKALSLARalEEAMEQKAELERLNKQFRTEMEDlmsskddvgksvHELEKSKRALEQQVEEMKTQL-- 1541
Cdd:PRK00409 564 EDKLLEEAEKEAQQAIKEAK--KEADEIIKELRQLQKGGYASVKA------------HELIEARKRLNKANEKKEKKKkk 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 806638593 1542 -EELEDELQATEDAKLR--------------LEVNLQA----MKAQfERDLQGRDEQSEEKKKQLVRQV 1591
Cdd:PRK00409 630 qKEKQEELKVGDEVKYLslgqkgevlsipddKEAIVQAgimkMKVP-LSDLEKIQKPKKKKKKKPKTVK 697
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1154-1403 |
4.88e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 45.02 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1154 STAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEelaeqleQTKRVKATLEK--AKQTLENERGELAN 1231
Cdd:pfam05667 155 GSRALRPFHTQTLVLPGRKGKTLKNSKELKEFYSEYLPPVTAQPSS-------RASVVPSLLERnaAELAAAQEWEEEWN 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1232 EVKALLQG------KGDSEHKRKKVEAQLQELQVKFSEGE----RVRTELADKVSKLQVELDSVTGLLNQS---DSKSSK 1298
Cdd:pfam05667 228 SQGLASRLtpeeyrKRKRTKLLKRIAEQLRSAALAGTEATsgasRSAQDLAELLSSFSGSSTTDTGLTKGSrftHTEKLQ 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1299 LTKDFSALESQL---QDTQELLQEENRQKLS--------LSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVt 1367
Cdd:pfam05667 308 FTNEAPAATSSPptkVETEEELQQQREEELEelqeqledLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQY- 386
|
250 260 270
....*....|....*....|....*....|....*.
gi 806638593 1368 DMKKKMedgVGCLETAEEAKRRLQKDLEGLSQRLEE 1403
Cdd:pfam05667 387 KVKKKT---LDLLPDAEENIAKLQALVDASAQRLVE 419
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1450-1923 |
5.71e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.04 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1450 LAEEKTISAKYAEERDRAEAEAREKE---TKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKD------------ 1514
Cdd:TIGR00606 233 LESSREIVKSYENELDPLKNRLKEIEhnlSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDeqlndlyhnhqr 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1515 ----------DVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKK 1584
Cdd:TIGR00606 313 tvrekerelvDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1585 K---QLVRQVREMEAEL---------EDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREE---AIKQLRKLQAQMKD 1649
Cdd:TIGR00606 393 KnfhTLVIERQEDEAKTaaqlcadlqSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEElkfVIKELQQLEGSSDR 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1650 CMrELDDTRASREEILAQAKENeKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANS------SGKGALALEE 1723
Cdd:TIGR00606 473 IL-ELDQELRKAERELSKAEKN-SLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRtqmemlTKDKMDKDEQ 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1724 KRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKS 1803
Cdd:TIGR00606 551 IRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1804 KykASIAALEAKIAQLEEQLDNETKERQAASKqvrrAEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAE 1883
Cdd:TIGR00606 631 V--CGSQDEESDLERLKEEIEKSSKQRAMLAG----ATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKL 704
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 806638593 1884 EEAQRANASRRKLQRELEDATETA-----------DAMNREVSSLKNKLRR 1923
Cdd:TIGR00606 705 RLAPDKLKSTESELKKKEKRRDEMlglapgrqsiiDLKEKEIPELRNKLQK 755
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
962-1181 |
6.13e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.89 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 962 LQLEKVTTEAKLKKLEEDQI---IMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEE--KSKSLAkLKNKHEAM------IT 1030
Cdd:PLN02939 175 LEMRLSETDARIKLAAQEKIhveILEEQLEKLRNELLIRGATEGLCVHSLSKELDvlKEENML-LKDDIQFLkaelieVA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1031 DLEERLRREEKQRQELEKTRRKLEgdSTDLSDQiaELQAQIAELKMQ-LAKKEEELQAALARVEEEAAQKNMALKKIREL 1109
Cdd:PLN02939 254 ETEERVFKLEKERSLLDASLRELE--SKFIVAQ--EDVSKLSPLQYDcWWEKVENLQDLLDRATNQVEKAALVLDQNQDL 329
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 806638593 1110 ETQISELQEDLESERACRNKAEKQKRdLGEELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLEDEAK 1181
Cdd:PLN02939 330 RDKVDKLEASLKEANVSKFSSYKVEL-LQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEESK 400
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1057-1236 |
6.86e-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: 44.75 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1057 STDLSDQIAELQAQIAELKMQLA--KKEEELQAALARVEEEAAQKNMALKKIRELETQIS--ELQEDLESERACRNKAEK 1132
Cdd:pfam09731 282 NDDLNSLIAHAHREIDQLSKKLAelKKREEKHIERALEKQKEELDKLAEELSARLEEVRAadEAQLRLEFEREREEIRES 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1133 QKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEvSILKKTLEDEAKTHEAQIQEMRQK---HSQAVEELAEQLEQTK 1209
Cdd:pfam09731 362 YEEKLRTELERQAEAHEEHLKDVLVEQEIELQREFL-QDIKEKVEEERAGRLLKLNELLANlkgLEKATSSHSEVEDENR 440
|
170 180 190
....*....|....*....|....*....|....*..
gi 806638593 1210 R----------VKATLEKAKQTLenERGELANEVKAL 1236
Cdd:pfam09731 441 KaqqlwlaveaLRSTLEDGSADS--RPRPLVRELKAL 475
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1757-1909 |
7.31e-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: 43.37 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1757 LQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKsKYKASIAALEAKIAQLEEQLDNETKERQ----- 1831
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIK-RLELEIEEVEARIKKYEEQLGNVRNNKEyealq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1832 ----AASKQVRRAEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLeeaEEEAQRANASRRKLQRELEDATETA 1907
Cdd:COG1579 96 keieSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL---DEELAELEAELEELEAEREELAAKI 172
|
..
gi 806638593 1908 DA 1909
Cdd:COG1579 173 PP 174
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1012-1901 |
9.22e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.43 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1012 EEKSKSLAKLKNKHEAMITDLEERLRREEKQ-RQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAK----KEEELQ 1086
Cdd:NF041483 360 EDTAAQLAKAARTAEEVLTKASEDAKATTRAaAEEAERIRREAEAEADRLRGEAADQAEQLKGAAKDDTKeyraKTVELQ 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1087 AALARVEEEAAQ----------------KNMALKKIRELETQISEL-----QEDLESERACRNKAEKQKRDLGEELEALK 1145
Cdd:NF041483 440 EEARRLRGEAEQlraeavaegerirgeaRREAVQQIEEAARTAEELltkakADADELRSTATAESERVRTEAIERATTLR 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1146 TELEDTLDSTAAQQE-LRSKREQEVSILKKTLEDEAK-THEAQIQEMRQKHSQAVEELAE-QLEQTKRVKA---TLEKAK 1219
Cdd:NF041483 520 RQAEETLERTRAEAErLRAEAEEQAEEVRAAAERAAReLREETERAIAARQAEAAEELTRlHTEAEERLTAaeeALADAR 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1220 QTLENERGELANEVKAL----------LQGKGDSEHKRKKVEAQLQELQVKfSEGE----RVRTELADKVSKLQVEL-DS 1284
Cdd:NF041483 600 AEAERIRREAAEETERLrteaaerirtLQAQAEQEAERLRTEAAADASAAR-AEGEnvavRLRSEAAAEAERLKSEAqES 678
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1285 VTGLLNQSDSKSSKLTKDfsALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRN-LEKQIATLH 1363
Cdd:NF041483 679 ADRVRAEAAAAAERVGTE--AAEALAAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLASARKrVEEAQAEAQ 756
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1364 AQVTDMKKKMEDGVGcleTAEEAKRRLQKDLEGLSQRLEEKV-----AAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSN 1438
Cdd:NF041483 757 RLVEEADRRATELVS---AAEQTAQQVRDSVAGLQEQAEEEIaglrsAAEHAAERTRTEAQEEADRVRSDAYAERERASE 833
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1439 LEKKQKKfdqlLAEEKTISAKYAEERDRAEA--EAREKETKALSLA-RALEEAMEQKAELERLNKQFRTEM-EDLMSSKD 1514
Cdd:NF041483 834 DANRLRR----EAQEETEAAKALAERTVSEAiaEAERLRSDASEYAqRVRTEASDTLASAEQDAARTRADArEDANRIRS 909
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1515 DVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMK------AQFER------DLQGRDEQSEE 1582
Cdd:NF041483 910 DAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQliaeatGEAERlraeaaETVGSAQQHAE 989
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1583 KKKQLVRQVREmEAELEDERKQRSIAMAARKKLEMDLKDleahidtANKNREEAIKQLRKLQAQMKDCMRELddTRASRE 1662
Cdd:NF041483 990 RIRTEAERVKA-EAAAEAERLRTEAREEADRTLDEARKD-------ANKRRSEAAEQADTLITEAAAEADQL--TAKAQE 1059
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1663 EILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDEL-ADEIANSSGKGALALEEKrrleariaqleeeleee 1741
Cdd:NF041483 1060 EALRTTTEAEAQADTMVGAARKEAERIVAEATVEGNSLVEKARTdADELLVGARRDATAIRER----------------- 1122
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1742 qgnTELINDRLKKanlQIDQINtdlnlERSHAQKNENARQQLERQNKELKAKLQEMESAvkskykasiaalEAKIAQLEE 1821
Cdd:NF041483 1123 ---AEELRDRITG---EIEELH-----ERARRESAEQMKSAGERCDALVKAAEEQLAEA------------EAKAKELVS 1179
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1822 QLDNE-TKERQAAskqVRRAEKKLKDVLLQVEDERRNAEQFKDQADKASTRL-KQLKRQLEEAEEEAQRANASRRKLQRE 1899
Cdd:NF041483 1180 DANSEaSKVRIAA---VKKAEGLLKEAEQKKAELVREAEKIKAEAEAEAKRTvEEGKRELDVLVRRREDINAEISRVQDV 1256
|
..
gi 806638593 1900 LE 1901
Cdd:NF041483 1257 LE 1258
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1505-1925 |
9.86e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.91 E-value: 9.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1505 EMEDLMSSKDDVGKSVHELEKS-------KRALEQQVEEMKTQLEELED-ELQATEDAK--LRLEVNLQAMKAQFERDLQ 1574
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQvsllqeeKNSLQQENKKLQERLDQLESgDDSGTPGGKkyLLLQKQLEQLQEENFRLET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1575 GRDE---QSEEKKKQLVrqvremEAELEDERKQRSIAMAARKKLEMDLkdleahidtanknREEAIKQLRKLQAQMKDCM 1651
Cdd:pfam05622 81 ARDDyriKCEELEKEVL------ELQHRNEELTSLAEEAQALKDEMDI-------------LRESSDKVKKLEATVETYK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1652 RELDDTRASREEILAQAKENEKKLKsmeaEMIQLQEEL--AAAERA-----KRQAQQERDELADEiansSGKGALALEEK 1724
Cdd:pfam05622 142 KKLEDLGDLRRQVKLLEERNAEYMQ----RTLQLEEELkkANALRGqletyKRQVQELHGKLSEE----SKKADKLEFEY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1725 RRLEARIA---QLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENArqQLERQNKELKAKLQEMESAV 1801
Cdd:pfam05622 214 KKLEEKLEalqKEKERLIIERDTLRETNEELRCAQLQQAELSQADALLSPSSDPGDNL--AAEIMPAEIREKLIRLQHEN 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1802 KSKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRAEKKLKDVLLQVEDERRNAEQFKDQADKASTrlkqLKRQLEE 1881
Cdd:pfam05622 292 KMLRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSL----LKQKLEE 367
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 806638593 1882 AEEEAQRANASRRKLQRELEDATETADA-MNREVSSLKNKLRRGD 1925
Cdd:pfam05622 368 HLEKLHEAQSELQKKKEQIEELEPKQDSnLAQKIDELQEALRKKD 412
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
842-1631 |
1.00e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 842 RHEDELLAKEAELTKVREKHLAAENRLTEME-------------TMQSQLMAEKLQ---------------------LQE 887
Cdd:PRK04863 283 VHLEEALELRRELYTSRRQLAAEQYRLVEMArelaelneaesdlEQDYQAASDHLNlvqtalrqqekieryqadleeLEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 888 QLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEER--------CQYLQA----EKKKMQQNIQELEEQLEEE 955
Cdd:PRK04863 363 RLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQAldvqqtraIQYQQAvqalERAKQLCGLPDLTADNAED 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 956 ESARQKLQLEKVTTEakLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTTN--------LMEEEEKSKSLAKLKNKHEA 1027
Cdd:PRK04863 443 WLEEFQAKEQEATEE--LLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSeawdvareLLRRLREQRHLAEQLQQLRM 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1028 MITDLEERLRreekQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELqaalarveEEAAQKNMALKKIR 1107
Cdd:PRK04863 521 RLSELEQRLR----QQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESV--------SEARERRMALRQQL 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1108 E-LETQISELQedleseracrnKAEKQKRDLGEELEALKTELEDTLDSTAA-----QQELRSKREQEVSilkktlEDEAK 1181
Cdd:PRK04863 589 EqLQARIQRLA-----------ARAPAWLAAQDALARLREQSGEEFEDSQDvteymQQLLERERELTVE------RDELA 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1182 THEAQIQEMRQKHSQAVEELAEQLEQTKR---------------------------------VKATLEKAKQTLENERGE 1228
Cdd:PRK04863 652 ARKQALDEEIERLSQPGGSEDPRLNALAErfggvllseiyddvsledapyfsalygparhaiVVPDLSDAAEQLAGLEDC 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1229 LAN------EVKALLQGKGDSEHKRKKVEAQLQELQVKFSE-------GERVRTELADkvsKLQVELDSVTGLLNQSDSK 1295
Cdd:PRK04863 732 PEDlyliegDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRfpevplfGRAAREKRIE---QLRAEREELAERYATLSFD 808
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1296 SSKLTKDFSALESQL---------QDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHA-Q 1365
Cdd:PRK04863 809 VQKLQRLHQAFSRFIgshlavafeADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLlA 888
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1366 VTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQrleekvaaydkLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKK 1445
Cdd:PRK04863 889 DETLADRVEEIREQLDEAEEAKRFVQQHGNALAQ-----------LEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQ 957
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1446 FDQLlaeektisakyAEERDRAEAEAREKETKALSLARALEEAMEQK-AELERLNKQFRTEMEDLMSSKDDVGKSVHELE 1524
Cdd:PRK04863 958 AFAL-----------TEVVQRRAHFSYEDAAEMLAKNSDLNEKLRQRlEQAEQERTRAREQLRQAQAQLAQYNQVLASLK 1026
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1525 KSKRALEQQVEEMKTQLEELedELQATEDAKLRLevnlqamkAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQ 1604
Cdd:PRK04863 1027 SSYDAKRQMLQELKQELQDL--GVPADSGAEERA--------RARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKK 1096
|
890 900
....*....|....*....|....*..
gi 806638593 1605 rsiamaaRKKLEMDLKDLEAHIDTANK 1631
Cdd:PRK04863 1097 -------LRKLERDYHEMREQVVNAKA 1116
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1496-1854 |
1.03e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1496 ERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFE----- 1570
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEqleee 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1571 -RDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKD 1649
Cdd:COG4372 82 lEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1650 CMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEA 1729
Cdd:COG4372 162 LQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1730 RIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSKYKASI 1809
Cdd:COG4372 242 LELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAAL 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 806638593 1810 AALEAKIAQLEEQLDNETKERQAASKQVRRAEKKLKDVLLQVEDE 1854
Cdd:COG4372 322 LELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAG 366
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1139-1859 |
1.05e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.02 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1139 EELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLEDEAKTHEAQiQEMRQKHSQAVEELAEQLEQTKRVKATLEKA 1218
Cdd:PRK10246 191 EQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLLTA-QQQQQQSLNWLTRLDELQQEASRRQQALQQA 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1219 KQTLENERGELANEVKALlqgkgdsehkrkkVEAQLQELQVKFSEGERVRTELADKVSKLQVELDSVTGLlnQSDSKSSK 1298
Cdd:PRK10246 270 LAAEEKAQPQLAALSLAQ-------------PARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMAL--RARIRHHA 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1299 LtKDFSALESQLQDTQELLQEENRQKLslstklkqMEDEKNSFREQLEEEEEAKrnleKQIATLHAQVTDMKKKMED--G 1376
Cdd:PRK10246 335 A-KQSAELQAQQQSLNTWLAEHDRFRQ--------WNNELAGWRAQFSQQTSDR----EQLRQWQQQLTHAEQKLNAlpA 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1377 VGCLETAEE--AKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEK 1454
Cdd:PRK10246 402 ITLTLTADEvaAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVK 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1455 TISAKYAEERDRAEAEAREKETKALSLARALEE-AMEQKAELERLNKQFRtemedlmssKDDVGKSVHELEKSKRALEQQ 1533
Cdd:PRK10246 482 TICEQEARIKDLEAQRAQLQAGQPCPLCGSTSHpAVEAYQALEPGVNQSR---------LDALEKEVKKLGEEGAALRGQ 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1534 VEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDE------QSEEKKKQL--VRQVREMEAELEDERKQR 1605
Cdd:PRK10246 553 LDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDiqpwldAQEEHERQLrlLSQRHELQGQIAAHNQQI 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1606 SIAMAA----RKKLEMDLKDLEAHIDTANK------NREEAIK-------QLRKLQAQMKDCMRELDDTRASREEILAQA 1668
Cdd:PRK10246 633 IQYQQQieqrQQQLLTALAGYALTLPQEDEeaswlaTRQQEAQswqqrqnELTALQNRIQQLTPLLETLPQSDDLPHSEE 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1669 KENEKKLKSMEAEMIQLQEELAAAERakrQAQQERDELADEIANSSGkgALALEEKRRLEARIAQleeeleeeqgnteLI 1748
Cdd:PRK10246 713 TVALDNWRQVHEQCLSLHSQLQTLQQ---QDVLEAQRLQKAQAQFDT--ALQASVFDDQQAFLAA-------------LL 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1749 NDrlkKANLQIDQINTDLNLERSHAQK-NENARQQLERQNKELKAKLQEmesavkskyKASIAALEAKIAQLEEQLDNET 1827
Cdd:PRK10246 775 DE---ETLTQLEQLKQNLENQRQQAQTlVTQTAQALAQHQQHRPDGLDL---------TVTVEQIQQELAQLAQQLRENT 842
|
730 740 750
....*....|....*....|....*....|....*
gi 806638593 1828 KERQAASKQVRRAE---KKLKDVLLQVEDERRNAE 1859
Cdd:PRK10246 843 TRQGEIRQQLKQDAdnrQQQQALMQQIAQATQQVE 877
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1718-1923 |
1.08e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1718 ALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLnlERSHAQKnENARQQLERQNKELKAKLQEM 1797
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL--EALQAEI-DKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1798 ESAVKSKYKASIAA------LEAKiaQLEEQLDnetkeRQAASKQVRRAEKKLkdvLLQVEDERRNAEQFKDQADKASTR 1871
Cdd:COG3883 89 GERARALYRSGGSVsyldvlLGSE--SFSDFLD-----RLSALSKIADADADL---LEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 806638593 1872 LKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKLRR 1923
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1603-1903 |
1.27e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1603 KQRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEM 1682
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1683 IQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDR---------LK 1753
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAeaeqaldelLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1754 KANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSKYKASIAALEAKIAQLEEQLDNETKERQAA 1833
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1834 SKQVRRAEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDA 1903
Cdd:COG4372 271 KDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1495-1879 |
1.28e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 43.74 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1495 LERLNKqfrtEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDElqatedaKLRLEVNLQAMKAQFERDlq 1574
Cdd:pfam15964 302 IERLTK----ERDDLMSALVSVRSSLAEAQQRESSAYEQVKQAVQMTEEANFE-------KTKALIQCEQLKSELERQ-- 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1575 gRDEQSEEKKKQLVRQVREMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMkdCMREL 1654
Cdd:pfam15964 369 -KERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQL--ASQEM 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1655 DDTRASREeilAQAKENEKKLKSMEAEMiQLQEELAAAERAKRQAQQERDELADEIANSSGKgalaLEEKRRLEARIAQL 1734
Cdd:pfam15964 446 DVTKVCGE---MRYQLNQTKMKKDEAEK-EHREYRTKTGRQLEIKDQEIEKLGLELSESKQR----LEQAQQDAARAREE 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1735 EEELEEEQGNTE--LINDRLKKANLQidqintdlnleRSHAQKNENARQQLERQNKELKAKLQEMES----------AVK 1802
Cdd:pfam15964 518 CLKLTELLGESEhqLHLTRLEKESIQ-----------QSFSNEAKAQALQAQQREQELTQKMQQMEAqhdktvneqySLL 586
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 806638593 1803 SKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRAEKKLKDVLLQVEDERRNAEQFKDQADKASTRLKQLKRQL 1879
Cdd:pfam15964 587 TSQNTFIAKLKEECCTLAKKLEEITQKSRSEVEQLSQEKEYLQDRLEKLQKRNEELEEQCVQHGRMHERMKQRLRQL 663
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1432-1728 |
1.30e-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: 43.79 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1432 QRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSlaRALEEAMEQKAELERLN-KQFRTEMEDLM 1510
Cdd:COG5185 204 VNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTS--DKLEKLVEQNTDLRLEKlGENAESSKRLN 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1511 SSKDDVGKSVHELEKSKRALEQQVEeMKTQLEELEDELQATE------DAKLRLEVNLQAMKAQFERDLQGRDEQSEEKK 1584
Cdd:COG5185 282 ENANNLIKQFENTKEKIAEYTKSID-IKKATESLEEQLAAAEaeqeleESKRETETGIQNLTAEIEQGQESLTENLEAIK 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1585 KQL-----VRQVREMEAELEDERKQRS--------IAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCM 1651
Cdd:COG5185 361 EEIenivgEVELSKSSEELDSFKDTIEstkesldeIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVS 440
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 806638593 1652 RELDDTRASREEILAQAKENEKKLKSMEAEMIQ--LQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLE 1728
Cdd:COG5185 441 KLLNELISELNKVMREADEESQSRLEEAYDEINrsVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKL 519
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1052-1206 |
1.42e-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: 41.48 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1052 KLEGDSTDLSDQIAELQAQIA----ELKMQLAKKEEELQAALARVEEEAAQK---------NMALKKIRELETQISELQE 1118
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGpvaqELVDRLEKETEALRERLQKDLEEVRAKlepyleelqAKLGQNVEELRQRLEPYTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1119 DLESerACRNKAEKQKRDLGEELEALKTELEDTLDSTAAQ-----QELRSKREQEVSILKKTLEDEAKTHEAQ----IQE 1189
Cdd:pfam01442 81 ELRK--RLNADAEELQEKLAPYGEELRERLEQNVDALRARlapyaEELRQKLAERLEELKESLAPYAEEVQAQlsqrLQE 158
|
170
....*....|....*..
gi 806638593 1190 MRQKHSQAVEELAEQLE 1206
Cdd:pfam01442 159 LREKLEPQAEDLREKLD 175
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1662-1806 |
1.52e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1662 EEILAQAKEN--EKKLK------SMEAEMIQLQEELAAAERAKRQAQQERDELADEIAnssgkgalALEEKRRLEARIAQ 1733
Cdd:PRK00409 501 ENIIEEAKKLigEDKEKlneliaSLEELERELEQKAEEAEALLKEAEKLKEELEEKKE--------KLQEEEDKLLEEAE 572
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 806638593 1734 LEeeleeeqgntelINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQnKELKAKLQEMESAVKSKYK 1806
Cdd:PRK00409 573 KE------------AQQAIKEAKKEADEIIKELRQLQKGGYASVKAHELIEAR-KRLNKANEKKEKKKKKQKE 632
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
844-1219 |
1.53e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 844 EDELLAKEAELTKVREKHLAAENRLTEMETmQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEI---CHDL 920
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEA-ELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLdasSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 921 EArveeeeercqyLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEkkLLEDR 1000
Cdd:COG4913 688 AA-----------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--LLEER 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1001 VAefttnlmeEEEKSKSLAKLKNKHEAMITDLEERLRREEKQ-RQELEKTRRKLEGDSTDLSDQIAELQAQIAELkmqla 1079
Cdd:COG4913 755 FA--------AALGDAVERELRENLEERIDALRARLNRAEEElERAMRAFNREWPAETADLDADLESLPEYLALL----- 821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1080 kkeEELQA-ALARVEEEAAQknmALKkiRELETQISELQEDLESEracRNKAEKQKRDLGEELEALKTELEDTLdstaaQ 1158
Cdd:COG4913 822 ---DRLEEdGLPEYEERFKE---LLN--ENSIEFVADLLSKLRRA---IREIKERIDPLNDSLKRIPFGPGRYL-----R 885
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 806638593 1159 QELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAK 1219
Cdd:COG4913 886 LEARPRPDPEVREFRQELRAVTSGASLFDEELSEARFAALKRLIERLRSEEEESDRRWRAR 946
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1017-1148 |
1.58e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.03 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1017 SLAKLKNkheamiTDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEea 1096
Cdd:PRK09039 70 SLERQGN------QDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVEL-- 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 806638593 1097 aqknmalkkireLETQISELQEDLESERACRNKAEKQKRDLGEELEALKTEL 1148
Cdd:PRK09039 142 ------------LNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRL 181
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1442-1607 |
1.66e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1442 KQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVH 1521
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1522 ELEKSKRALEQQVEEMKTQLEELEDELQatEDAKLRLEVNLQAMKAQFERDLqgrdeqsEEKKKQLVRQVREmEAELEDE 1601
Cdd:PRK12705 106 QLEEREKALSARELELEELEKQLDNELY--RVAGLTPEQARKLLLKLLDAEL-------EEEKAQRVKKIEE-EADLEAE 175
|
....*.
gi 806638593 1602 RKQRSI 1607
Cdd:PRK12705 176 RKAQNI 181
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1638-1796 |
1.68e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.03 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1638 KQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKG 1717
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVS 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 806638593 1718 ALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLerSHAQKNenarQQLERQNKELKAKLQE 1796
Cdd:PRK09039 133 ARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNV--ALAQRV----QELNRYRSEFFGRLRE 205
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1026-1420 |
1.71e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.29 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1026 EAMITDLEERLR--REEKQRQELEKTRRKLEgdstDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEeaAQKNMAL 1103
Cdd:PRK04778 85 EEQLFEAEELNDkfRFRKAKHEINEIESLLD----LIEEDIEQILEELQELLESEEKNREEVEQLKDLYRE--LRKSLLA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1104 KK------IRELETQISELQEDLE-----SERACRNKAEKQKRDLGEELEALKTELED--TLDSTAaQQELRSKREQEVS 1170
Cdd:PRK04778 159 NRfsfgpaLDELEKQLENLEEEFSqfvelTESGDYVEAREILDQLEEELAALEQIMEEipELLKEL-QTELPDQLQELKA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1171 ILKKTLED----EAKTHEAQIQEMRQKHSQAVEELAEqLEqTKRVKATLEKAKQTLENERGELANEVKAllqgKGDSEHK 1246
Cdd:PRK04778 238 GYRELVEEgyhlDHLDIEKEIQDLKEQIDENLALLEE-LD-LDEAEEKNEEIQERIDQLYDILEREVKA----RKYVEKN 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1247 RKKVEAQLQELQVKFS----EGERVR------TELADKVSKLQVELDSVTGLLNQSDSKSSKLTKDFSALESQLQDTQEL 1316
Cdd:PRK04778 312 SDTLPDFLEHAKEQNKelkeEIDRVKqsytlnESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQ 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1317 LQEENRQKLSLSTKLKQMEDEKNSFREQLEEeeeakrnlekqiatlhaqvtdMKKKMedgvgcletaEEAKRRLQK-DLE 1395
Cdd:PRK04778 392 LEEIEKEQEKLSEMLQGLRKDELEAREKLER---------------------YRNKL----------HEIKRYLEKsNLP 440
|
410 420
....*....|....*....|....*.
gi 806638593 1396 GLSQR-LEEKVAAYDKLEKTKTRLQQ 1420
Cdd:PRK04778 441 GLPEDyLEMFFEVSDEIEALAEELEE 466
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1635-1876 |
1.76e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.14 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1635 EAIKQLRKLQAQMKDCMRELDDTRASREEI-LAQAKENEkklksmEAEMIQLQEELAAAERAKRQAQQERDELADE---I 1710
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLEELeAAALQPGE------EEELEEERRRLSNAEKLREALQEALEALSGGeggA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1711 ANSSGKGALALEEKRRLEARIAQleeeleeeqgntelINDRLKKANLQIDQINTDLnleRSHAQKNENARQQLErqnkEL 1790
Cdd:COG0497 243 LDLLGQALRALERLAEYDPSLAE--------------LAERLESALIELEEAASEL---RRYLDSLEFDPERLE----EV 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1791 KAKLQEMESAvKSKYKASIAALEAKIAQLEEQL---DNETKERQAASKQVRRAEKKLKDVLLQVEDERRN-AEQFkdqAD 1866
Cdd:COG0497 302 EERLALLRRL-ARKYGVTVEELLAYAEELRAELaelENSDERLEELEAELAEAEAELLEAAEKLSAARKKaAKKL---EK 377
|
250
....*....|
gi 806638593 1867 KASTRLKQLK 1876
Cdd:COG0497 378 AVTAELADLG 387
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1184-1421 |
1.82e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1184 EAQIQEMRQKHSQAVEELAEQLEQtkrVKATLEKAKQTLENERGElanevkallQGKGDSEHKRKKVEAQLQELQVKFSE 1263
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPE---LRKELEEAEAALEEFRQK---------NGLVDLSEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1264 gerVRTELADkvskLQVELDSVTGLLNQSDSKSSKLTKD--FSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSF 1341
Cdd:COG3206 231 ---ARAELAE----AEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAAL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1342 REQLeeeeeaKRNLEKQIATLHAQVtdmkkkmedgvgcletaEEAKRRLQkDLEGLSQRLEEKVAAYDKLEKTKTRLQQE 1421
Cdd:COG3206 304 RAQL------QQEAQRILASLEAEL-----------------EALQAREA-SLQAQLAQLEARLAELPELEAELRRLERE 359
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1658-1858 |
2.01e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.01 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1658 RASREEILAQAKENEK----KLKsMEAEMIQL-QEELAAAERAKRQAQQERDELADEIAnssgkGALAleekrRLEARIA 1732
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKaeeaKAR-FEARQARLeREKAAREARHKKAAEARAAKDKDAVA-----AALA-----RVKAKKA 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1733 QLEEELEEEQG----NTELINDR-LKKANLQIDQINTDLN-------------LERSHAQKNENARQQLERQNKEL--KA 1792
Cdd:PRK05035 501 AATQPIVIKAGarpdNSAVIAAReARKAQARARQAEKQAAaaadpkkaavaaaIARAKAKKAAQQAANAEAEEEVDpkKA 580
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 806638593 1793 KLQEMESAVKSKyKASIAALEAKIAQLEEQLDNETKERQAASKQV--RRAEKKLKDVLLQVEDERRNA 1858
Cdd:PRK05035 581 AVAAAIARAKAK-KAAQQAASAEPEEQVAEVDPKKAAVAAAIARAkaKKAEQQANAEPEEPVDPRKAA 647
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1037-1416 |
2.06e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1037 RREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISEL 1116
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1117 QEDLESERACRNKAEKQKRDLGEELEALKTELEdtldstaaqqELRSKREQevsilkktLEDEAKTHEAQIQEMRQKHSQ 1196
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELE----------ELQKERQD--------LEQQRKQLEAQIAELQSEIAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1197 AVEELAEQLEQTKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKFSEGERVRTELADKVS 1276
Cdd:COG4372 148 REEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1277 KLQVELDSVTGLLNQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLE 1356
Cdd:COG4372 228 EAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAAL 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1357 KQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKT 1416
Cdd:COG4372 308 SLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
971-1160 |
2.08e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 41.59 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 971 AKLKKLEEDQIIME----DQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQR-QE 1045
Cdd:pfam04012 15 EGLDKAEDPEKMLEqairDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEELAREALAEkKS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1046 LEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARveEEAAQKNMALKK----------IRELEtQISE 1115
Cdd:pfam04012 95 LEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKAR--LKAAKAQEAVQTslgslstssaTDSFE-RIEE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 806638593 1116 LQEDLESERACRNKAEkQKRDLGEELEALKTELEDTLDSTAAQQE 1160
Cdd:pfam04012 172 KIEEREARADAAAELA-SAVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1579-1746 |
2.23e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1579 QSEEKKKQLVRQVREMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDD-- 1656
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1657 --------------------------TRASR------------EEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQ 1698
Cdd:COG3883 93 ralyrsggsvsyldvllgsesfsdflDRLSAlskiadadadllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 806638593 1699 AQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTE 1746
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1110-1447 |
2.31e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1110 ETQISELQEDLESERACRNKAEK-----QKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVSILKktLEDEAKTHE 1184
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKareveRRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIR--QEERKRELE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1185 AQIQEMRQKHSQAVEELA----EQLEQTKRVKATLEKAKQT--LENERGELANEVKALLQG-KGDSEHKRKKVEAQLQEL 1257
Cdd:pfam17380 364 RIRQEEIAMEISRMRELErlqmERQQKNERVRQELEAARKVkiLEEERQRKIQQQKVEMEQiRAEQEEARQREVRRLEEE 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1258 QVKfsEGERVRTELADKVSKLQVELDsvtgllNQSDSKSSKLTKDfsalesQLQDTQELLQEENRQKLSlstklKQMEDE 1337
Cdd:pfam17380 444 RAR--EMERVRLEEQERQQQVERLRQ------QEEERKRKKLELE------KEKRDRKRAEEQRRKILE-----KELEER 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1338 KNSFREQleeeEEAKRNLEKQIATLHAQVTDMKKKMEdgvgcletAEEaKRRLQKDLEGlSQRLEEKVAaydKLEKTKTR 1417
Cdd:pfam17380 505 KQAMIEE----ERKRKLLEKEMEERQKAIYEEERRRE--------AEE-ERRKQQEMEE-RRRIQEQMR---KATEERSR 567
|
330 340 350
....*....|....*....|....*....|
gi 806638593 1418 LQqeldDLLVDLDHQRQSVSNlEKKQKKFD 1447
Cdd:pfam17380 568 LE----AMEREREMMRQIVES-EKARAEYE 592
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1467-1733 |
2.32e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.01 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1467 AEAEAREKETKALSLARALEEA----MEQKaELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLE 1542
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEArqarLERE-KAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARP 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1543 EledelqatedaklrlevNLQAMKAQFERDLQGRDEQSEEKkkqlvrqvremEAELEDERK---QRSIAMAARKKLEMDL 1619
Cdd:PRK05035 515 D-----------------NSAVIAAREARKAQARARQAEKQ-----------AAAAADPKKaavAAAIARAKAKKAAQQA 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1620 KDLEAHIDTANK----NREEAIKQLRKLQAQMKD-----CMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELA 1690
Cdd:PRK05035 567 ANAEAEEEVDPKkaavAAAIARAKAKKAAQQAASaepeeQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKA 646
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 806638593 1691 AAE----RAK-RQAQQERDELADEIANSSGKGALAlEEKRRLEARIAQ 1733
Cdd:PRK05035 647 AVAaaiaRAKaRKAAQQQANAEPEEAEDPKKAAVA-AAIARAKAKKAA 693
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1035-1167 |
2.38e-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: 42.41 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1035 RLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKkeeeLQAALARVEEEAAQKNMALKKIRELETQIS 1114
Cdd:pfam00529 76 RLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQ----AQIDLARRRVLAPIGGISRESLVTAGALVA 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 806638593 1115 ELQEDLESERACRNKAEKQKRDLGEELEAL--KTELEDTLDSTAAQQELRSKREQ 1167
Cdd:pfam00529 152 QAQANLLATVAQLDQIYVQITQSAAENQAEvrSELSGAQLQIAEAEAELKLAKLD 206
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1765-1923 |
2.39e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1765 DLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSKYKASIAALEAKIAQ------LEEQLDNETKERQAAS---- 1834
Cdd:COG3206 102 KLNLDEDPLGEEASREAAIERLRKNLTVEPVKGSNVIEISYTSPDPELAAAVANalaeayLEQNLELRREEARKALefle 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1835 KQVRRAEKKLKDVLLQVED--ERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAM-- 1910
Cdd:COG3206 182 EQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELlq 261
|
170
....*....|...
gi 806638593 1911 NREVSSLKNKLRR 1923
Cdd:COG3206 262 SPVIQQLRAQLAE 274
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1453-1603 |
2.46e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 42.18 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1453 EKTISAKYAEERDRAEAEAREKETKAL-SLARALEEAMEQ------------KAELERLNKQFRTEM----------EDL 1509
Cdd:cd16269 96 MEQLEEKKEEFCKQNEEASSKRCQALLqELSAPLEEKISQgsysvpggyqlyLEDREKLVEKYRQVPrkgvkaeevlQEF 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1510 MSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDL-QGRDEQSEEKKKQLV 1588
Cdd:cd16269 176 LQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLrQLKEKMEEERENLLK 255
|
170
....*....|....*
gi 806638593 1589 RQVREMEAELEDERK 1603
Cdd:cd16269 256 EQERALESKLKEQEA 270
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1196-1331 |
2.48e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1196 QAVEELAEQLEQTKRVKATLEKAKQTLENERGELANEVKAllqgkgdSEHKRKKVEAQLqelqvkfSEGERVRTELADKV 1275
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-------AEAERSRLQALL-------AELAGAGAAAEGRA 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 806638593 1276 SKLQVELDSVTGLLNQSDSKSSKLTKDFSALESQLQDTQELL-------QEENRQKLSLSTKL 1331
Cdd:PRK09039 119 GELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALdasekrdRESQAKIADLGRRL 181
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1247-1578 |
2.63e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1247 RKKVEAQLQELQVKFSEGERVRTELADKVSKLQVELDSVTGLLNQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLS 1326
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1327 LSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVA 1406
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1407 AydKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALE 1486
Cdd:COG4372 179 A--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1487 EAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMK 1566
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330
....*....|..
gi 806638593 1567 AQFERDLQGRDE 1578
Cdd:COG4372 337 AELADLLQLLLV 348
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1029-1173 |
2.67e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 41.52 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1029 ITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALK-KIR 1107
Cdd:pfam12795 80 LEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQaELA 159
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 806638593 1108 ELETQISELQEDLES-------ERACRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVSILK 1173
Cdd:pfam12795 160 ALKAQIDMLEQELLSnnnrqdlLKARRDLLTLRIQRLEQQLQALQELLNEKRLQEAEQAVAQTEQLAEEAAGD 232
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1050-1179 |
2.74e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1050 RRKLEGDSTdlSDQIAELQAQIAELKMQlakkeeelQAALARVEEEAAQKnmalkKIRELETQISELQEDLESERAcRNK 1129
Cdd:COG0542 401 RVRMEIDSK--PEELDELERRLEQLEIE--------KEALKKEQDEASFE-----RLAELRDELAELEEELEALKA-RWE 464
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 806638593 1130 AEKQkrdLGEELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLEDE 1179
Cdd:COG0542 465 AEKE---LIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
964-1115 |
2.75e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 964 LEKVTTEAKLKKLEE--DQIIMEDQN-CKLAKEKKLLE--DRVAEFTTNLMEE-EEKSKSLAKLKNK---HEAMITDLEE 1034
Cdd:PRK12704 24 VRKKIAEAKIKEAEEeaKRILEEAKKeAEAIKKEALLEakEEIHKLRNEFEKElRERRNELQKLEKRllqKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1035 RLRREEkqrQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAK-----KEEELQAALARVEEEAAQKNMALkkIREL 1109
Cdd:PRK12704 104 LLEKRE---EELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisgltAEEAKEILLEKVEEEARHEAAVL--IKEI 178
|
....*.
gi 806638593 1110 ETQISE 1115
Cdd:PRK12704 179 EEEAKE 184
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
958-1095 |
2.78e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 958 ARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLK---------NKHEAM 1028
Cdd:COG1579 25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyealqkeiESLKRR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 806638593 1029 ITDLEERLR----REEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEE 1095
Cdd:COG1579 105 ISDLEDEILelmeRIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1050-1297 |
2.87e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1050 RRKLEGDSTDLS----------DQIAELQAQIAELKMQL----------AKKEEELQA-ALARVEEEAAQKNMALKKIRE 1108
Cdd:PHA02562 152 RRKLVEDLLDISvlsemdklnkDKIRELNQQIQTLDMKIdhiqqqiktyNKNIEEQRKkNGENIARKQNKYDELVEEAKT 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1109 LETQISELQEDL-------ESERACRNKAEKQKRDLGEELEALKTEL----EDTLDSTAAQQ-----ELRSKREQEVSIL 1172
Cdd:PHA02562 232 IKAEIEELTDELlnlvmdiEDPSAALNKLNTAAAKIKSKIEQFQKVIkmyeKGGVCPTCTQQisegpDRITKIKDKLKEL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1173 KKTLEDeaktheaqIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQTLENERGELanevkallqgkgdsehkrKKVEA 1252
Cdd:PHA02562 312 QHSLEK--------LDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKA------------------KKVKA 365
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 806638593 1253 QLQELQVKF----SEGERVRTELADKVSKLQ------VELDSVTGLLNQSDSKSS 1297
Cdd:PHA02562 366 AIEELQAEFvdnaEELAKLQDELDKIVKTKSelvkekYHRGIVTDLLKDSGIKAS 420
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
1047-1337 |
3.04e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 41.97 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1047 EKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQI----------SEL 1116
Cdd:pfam15742 33 EKELRYERGKNLDLKQHNSLLQEENIKIKAELKQAQQKLLDSTKMCSSLTAEWKHCQQKIRELELEVlkqaqsiksqNSL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1117 QEDLESERACRNKAEKQKRDLGEELE-ALKTELEDTLDSTAAQQELRSKREQevsilkktlEDEAKThEAQIQEmrqkhs 1195
Cdd:pfam15742 113 QEKLAQEKSRVADAEEKILELQQKLEhAHKVCLTDTCILEKKQLEERIKEAS---------ENEAKL-KQQYQE------ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1196 qaveelaeqlEQTKRvkATLEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQ---VKFSEGERVRTELA 1272
Cdd:pfam15742 177 ----------EQQKR--KLLDQNVNELQQQVRSLQDKEAQLEMTNSQQQLRIQQQEAQLKQLEnekRKSDEHLKSNQELS 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 806638593 1273 DKVSKLQVELDSVTG----LLNQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKlslSTKLKQMEDE 1337
Cdd:pfam15742 245 EKLSSLQQEKEALQEelqqVLKQLDVHVRKYNEKHHHHKAKLRRAKDRLVHEVEQR---DERIKQLENE 310
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
844-1088 |
3.17e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 844 EDELLAKEAELTKVREKHLAAENRLTEMETMQSQLMAEKLQLQEQLQaetELCAEAEELRARLTAKKQELEEICHDLEAR 923
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE---ALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 924 VEEeeercqylqaekkkMQQNIQELEEQLEEEES-----ARQKLQLEKVTTEAKLKKLEEdqiIMEDQNcKLAKEKKLLE 998
Cdd:COG3883 92 ARA--------------LYRSGGSVSYLDVLLGSesfsdFLDRLSALSKIADADADLLEE---LKADKA-ELEAKKAELE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 999 DRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQL 1078
Cdd:COG3883 154 AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
250
....*....|
gi 806638593 1079 AKKEEELQAA 1088
Cdd:COG3883 234 AAAAAAAAAA 243
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1578-1714 |
3.40e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 41.20 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1578 EQSEEKKKQLVRQVREMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNRE------------EAIKQLRKLQA 1645
Cdd:pfam04012 18 DKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQaaltkgneelarEALAEKKSLEK 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 806638593 1646 QMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAeRAKRQAQQERDELADEIANSS 1714
Cdd:pfam04012 98 QAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAA-KAQEAVQTSLGSLSTSSATDS 165
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1058-1135 |
3.45e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 3.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 806638593 1058 TDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLESERACRNKAEKQKR 1135
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERK 215
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1408-1841 |
3.55e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.20 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1408 YDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQLLaeEKTISAKYAEERDRAEAEAREKETKALS---LARA 1484
Cdd:COG5278 81 YEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAEL--EQVIALRRAGGLEAALALVRSGEGKALMdeiRARL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1485 LEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQA 1564
Cdd:COG5278 159 LLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAAL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1565 MKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQ 1644
Cdd:COG5278 239 ALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1645 AQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEK 1724
Cdd:COG5278 319 AAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAA 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1725 RRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKSK 1804
Cdd:COG5278 399 AAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALA 478
|
410 420 430
....*....|....*....|....*....|....*..
gi 806638593 1805 YKASIAALEAKIAQLEEQLDNETKERQAASKQVRRAE 1841
Cdd:COG5278 479 AAAAALAEAEAAAALAAAAALSLALALAALLLAAAEA 515
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1034-1373 |
3.73e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 42.36 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1034 ERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKK-----EEELQAALARVEEEAAQKNMALKKIRE 1108
Cdd:pfam13166 93 EIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLDECWKKikrkkNSALSEALNGFKYEANFKSRLLREIEK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1109 LETQISELQEDLESERACRNKAEKQKRDLGE------ELEALKTELEDTLDSTAAQQELrsKREQEVSILKKTLEDEAKT 1182
Cdd:pfam13166 173 DNFNAGVLLSDEDRKAALATVFSDNKPEIAPltfnviDFDALEKAEILIQKVIGKSSAI--EELIKNPDLADWVEQGLEL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1183 HEAQIQEMRQKHSQAVEELAEQLE---------QTKRVKATLEKAKQTLENERGELaNEVKALLQGKGDSEHKRKKVEAQ 1253
Cdd:pfam13166 251 HKAHLDTCPFCGQPLPAERKAALEahfddefteFQNRLQKLIEKVESAISSLLAQL-PAVSDLASLLSAFELDVEDIESE 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1254 LQELQVKFSEGERVRTELADKVSKlQVELDSVTG----------LLNQSDSKSSKLTKDFSALESQLQDTQEL------- 1316
Cdd:pfam13166 330 AEVLNSQLDGLRRALEAKRKDPFK-SIELDSVDAkiesindlvaSINELIAKHNEITDNFEEEKNKAKKKLRLhlveefk 408
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 806638593 1317 --LQEENRQKLSLSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKM 1373
Cdd:pfam13166 409 seIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQLRDHKPGADEINKLL 467
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
989-1238 |
3.77e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 989 KLAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQ 1068
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1069 AQIAELKMQLAKK------EEELQAALARVEEEAAQKNMALKKIRELETQISELQEDLEsERACRNKAEKQKRDLGEELE 1142
Cdd:COG1340 92 EELDELRKELAELnkaggsIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELE-KAKKALEKNEKLKELRAELK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1143 ALKTELEDTLDSTAAQQELRSKREQEVSILKKTLED----------EAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVK 1212
Cdd:COG1340 171 ELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADElrkeadelhkEIVEAQEKADELHEEIIELQKELRELRKELKKLR 250
|
250 260
....*....|....*....|....*.
gi 806638593 1213 ATLEKAKqtLENERGELANEVKALLQ 1238
Cdd:COG1340 251 KKQRALK--REKEKEELEEKAEEIFE 274
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
1032-1160 |
3.86e-03 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 41.76 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1032 LEERLRREEKQR--QELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQlakKEEELQAALARVEEEAAQKNMALKKIREL 1109
Cdd:PRK00247 288 AEQRAQYREKQKekKAFLWTLRRNRLRMIITPWRAPELHAENAEIKKT---RTAEKNEAKARKKEIAQKRRAAEREINRE 364
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 806638593 1110 ETQisELQEDLESERACRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQE 1160
Cdd:PRK00247 365 ARQ--ERAAAMARARARRAAVKAKKKGLIDASPNEDTPSENEESKGSPPQV 413
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1719-1853 |
3.89e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.57 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1719 LALEEKR-RLEARIAQLEEELEEEQGNTElindrLKKANLQIDQINTDLNLershAQKNENARQQLERQNKELKAKLQEM 1797
Cdd:COG1566 83 AALAQAEaQLAAAEAQLARLEAELGAEAE-----IAAAEAQLAAAQAQLDL----AQRELERYQALYKKGAVSQQELDEA 153
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 806638593 1798 ESAVKSKyKASIAALEAKIAQLEEQLDNETkERQAASKQVRRAEKKLKDVLLQVED 1853
Cdd:COG1566 154 RAALDAA-QAQLEAAQAQLAQAQAGLREEE-ELAAAQAQVAQAEAALAQAELNLAR 207
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
957-1182 |
3.90e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 957 SARQKL--QLEKVTTEAKLKKLEEDQIIMEDQNCK-LAKEKKLLEDRVAEFTTNLMEEEEKSKSLAKlknKHEAMITDLE 1033
Cdd:PHA02562 150 PARRKLveDLLDISVLSEMDKLNKDKIRELNQQIQtLDMKIDHIQQQIKTYNKNIEEQRKKNGENIA---RKQNKYDELV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1034 ERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLA--KKEEE--------------LQAALARVEEEAA 1097
Cdd:PHA02562 227 EEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEqfQKVIKmyekggvcptctqqISEGPDRITKIKD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1098 QKNMALKKIRELETQISELQEDLESERACRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKR---EQEVSILKK 1174
Cdd:PHA02562 307 KLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFvdnAEELAKLQD 386
|
....*...
gi 806638593 1175 TLEDEAKT 1182
Cdd:PHA02562 387 ELDKIVKT 394
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1438-1647 |
4.09e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1438 NLEKKQKKFDQLLAEEKTISAkyAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKddvg 1517
Cdd:COG3206 190 ELEEAEAALEEFRQKNGLVDL--SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP---- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1518 kSVHELEKSKRALEQQVEEMKTQLEELEDELQAtedaklrlevnLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAE 1597
Cdd:COG3206 264 -VIQQLRAQLAELEAELAELSARYTPNHPDVIA-----------LRAQIAALRAQLQQEAQRILASLEAELEALQAREAS 331
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 806638593 1598 LEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQM 1647
Cdd:COG3206 332 LQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAE 381
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1608-1830 |
4.18e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1608 AMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQE 1687
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1688 ELAAAERAKrqaqqERDELADEIANssgkgalaleekrrLEARIaqleeeleeeqgntELINDRLKKANLQIDQINTDLn 1767
Cdd:COG1579 81 QLGNVRNNK-----EYEALQKEIES--------------LKRRI--------------SDLEDEILELMERIEELEEEL- 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 806638593 1768 lershaqknENARQQLERQNKELKAKLQEMESAVKsKYKASIAALEAKIAQLEEQLDNETKER 1830
Cdd:COG1579 127 ---------AELEAELAELEAELEEKKAELDEELA-ELEAELEELEAEREELAAKIPPELLAL 179
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1523-1727 |
4.21e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1523 LEKSK-RALEQQVEEMKTQLEELEDELQATEDaklrLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDE 1601
Cdd:PHA02562 171 LNKDKiRELNQQIQTLDMKIDHIQQQIKTYNK----NIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1602 RKQRSIAMAARKKLEMDLKDLEAHIDTANK----------------NREEAIKQLRKLQAQMKDC---MRELDDTRASRE 1662
Cdd:PHA02562 247 VMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyekggvcptctqQISEGPDRITKIKDKLKELqhsLEKLDTAIDELE 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 806638593 1663 EILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRL 1727
Cdd:PHA02562 327 EIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1107-1707 |
4.31e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.12 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1107 RELETQISELQEDLESERACRNK-AEKQKRDLGEELEALKTELEDTL-------------DSTAAQ------QELRSKRE 1166
Cdd:NF041483 167 RLLDESRAEAEQALAAARAEAERlAEEARQRLGSEAESARAEAEAILrrarkdaerllnaASTQAQeatdhaEQLRSSTA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1167 QEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKATLEKAKQTLENERGELANEVKALLQGKGDSEHK 1246
Cdd:NF041483 247 AESDQARRQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAESANEQRTRTAKEEIARLVGEATKEAE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1247 RKKVEAQlQELQVKFSEGERVRTELADKVSKLQVElDSVTGLLNQSDSKSSKLTKdfsALESQLQDTQELLQEENRQKLS 1326
Cdd:NF041483 327 ALKAEAE-QALADARAEAEKLVAEAAEKARTVAAE-DTAAQLAKAARTAEEVLTK---ASEDAKATTRAAAEEAERIRRE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1327 LSTKLKQMEDEKNSFREQLeeEEEAKRNLEKQIA-TLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKV 1405
Cdd:NF041483 402 AEAEADRLRGEAADQAEQL--KGAAKDDTKEYRAkTVELQEEARRLRGEAEQLRAEAVAEGERIRGEARREAVQQIEEAA 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1406 AAYDKLeKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQKKFDQllAEEKTISAKYAEERDRAEAEAREKETK--ALSLAR 1483
Cdd:NF041483 480 RTAEEL-LTKAKADADELRSTATAESERVRTEAIERATTLRRQ--AEETLERTRAEAERLRAEAEEQAEEVRaaAERAAR 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1484 ALEEAMEQ-----KAELERLNKQFRTEMED-LMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQA---TEDA 1554
Cdd:NF041483 557 ELREETERaiaarQAEAAEELTRLHTEAEErLTAAEEALADARAEAERIRREAAEETERLRTEAAERIRTLQAqaeQEAE 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1555 KLRLEVNLQAMKAQFERD---LQGRDEQSEEKKKQlvrqvrEMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANK 1631
Cdd:NF041483 637 RLRTEAAADASAARAEGEnvaVRLRSEAAAEAERL------KSEAQESADRVRAEAAAAAERVGTEAAEALAAAQEEAAR 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1632 NREEAIKQLRKLQAQMKdcmRELDDTRASREEILAQAKeneKKLKSMEAEMIQLQEE--------LAAAErakRQAQQER 1703
Cdd:NF041483 711 RRREAEETLGSARAEAD---QERERAREQSEELLASAR---KRVEEAQAEAQRLVEEadrratelVSAAE---QTAQQVR 781
|
....
gi 806638593 1704 DELA 1707
Cdd:NF041483 782 DSVA 785
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1526-1721 |
4.65e-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: 41.28 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1526 SKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDlqgrdeqseekkkqlVRQVREMEAELEderKQR 1605
Cdd:pfam09787 41 SSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEE---------------AESSREQLQELE---EQL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1606 SIAMAARKKLEMDLKDLEAHIDtanKNREEAIKQLRKLQAQMKDCMRELDDTRA---SREEILAQAKENEKKLKSMEAEM 1682
Cdd:pfam09787 103 ATERSARREAEAELERLQEELR---YLEEELRRSKATLQSRIKDREAEIEKLRNqltSKSQSSSSQSELENRLHQLTETL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 806638593 1683 IQLQEELAA--AERAKRQAQQERDELADEIANSSGKGALAL 1721
Cdd:pfam09787 180 IQKQTMLEAlsTEKNSLVLQLERMEQQIKELQGEGSNGTSI 220
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1582-1860 |
4.65e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1582 EKKKQLVRQVREMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASR 1661
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1662 EEILAQAKENEKKLKSMEAEMiqlqEELAAAERAKRQAQQERDELADEIANSSgkgaLALEEKRRLEARIAQLEEELEEE 1741
Cdd:COG1340 81 DELNEKLNELREELDELRKEL----AELNKAGGSIDKLRKEIERLEWRQQTEV----LSPEEEKELVEKIKELEKELEKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1742 QgntelindRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKAKLQEMESAVKsKYKASIAALEAKIAQLEE 1821
Cdd:COG1340 153 K--------KALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEAD-ELRKEADELHKEIVEAQE 223
|
250 260 270
....*....|....*....|....*....|....*....
gi 806638593 1822 QLDNETKERQAASKQVRRAEKKLKDVLLQVEDERRNAEQ 1860
Cdd:COG1340 224 KADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK 262
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1533-1921 |
4.72e-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: 42.04 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1533 QVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLvRQVREMEAELEDE-RKQRSIAMAA 1611
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRI-RLLEKREAEAEEAlREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1612 RKKLEMDLKDLEAHIDTANKNRE--EAIKQ-LRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEaemiQLQEE 1688
Cdd:pfam05557 82 KKYLEALNKKLNEKESQLADAREviSCLKNeLSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAE----QLRQN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1689 LAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLeARIAQLEEELeeeqgntelinDRLKKANLQIDQINTDLNL 1768
Cdd:pfam05557 158 LEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSEL-ARIPELEKEL-----------ERLREHNKHLNENIENKLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1769 ershaqknenarqqLERQNKELKAKLQEMEsavksKYKASIAALEAKIAQLEEQLDNETKERQAASKQVRRAEK-KLKDV 1847
Cdd:pfam05557 226 --------------LKEEVEDLKRKLEREE-----KYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDlSRRIE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1848 LLQVEDERRNAEQFKDQADKASTR---------LKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLK 1918
Cdd:pfam05557 287 QLQQREIVLKEENSSLTSSARQLEkarreleqeLAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYD 366
|
...
gi 806638593 1919 NKL 1921
Cdd:pfam05557 367 KEL 369
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1436-1598 |
4.82e-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: 40.68 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1436 VSNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKaELERLNKQfrtemedlmsskdd 1515
Cdd:COG1579 33 LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-EYEALQKE-------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1516 vgksVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREME 1595
Cdd:COG1579 98 ----IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
...
gi 806638593 1596 AEL 1598
Cdd:COG1579 174 PEL 176
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1773-1923 |
4.88e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1773 AQKNENARQQLERQNKELKAKLQEMESAVKSKYKasiaaleakiaQLEEQLDNETKERQaasKQVRRAEKKLKDVLLQVE 1852
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIH-----------KLRNEFEKELRERR---NELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 806638593 1853 DERRNAEQFKDQADKASTRLKQLKRQLEEAEEEAQRAnasRRKLQRELEDATE-TAD-AMNREVSSLKNKLRR 1923
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEEL---IEEQLQELERISGlTAEeAKEILLEKVEEEARH 169
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1047-1277 |
4.98e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1047 EKTRRKLEGDSTDLSDQIAELQAQiaelKMQLAKKEEELQAALARVEEeaaqknmalkkireletqiseLQEDLeserac 1126
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEEL----ERELEQKAEEAEALLKEAEK---------------------LKEEL------ 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1127 rnkaEKQKRDLGEELEALKTELEDtldstAAQQELRSKREQEVSILKKTLEDEAKTHEA----QIQEMRQKHSQAVEELa 1202
Cdd:PRK00409 554 ----EEKKEKLQEEEDKLLEEAEK-----EAQQAIKEAKKEADEIIKELRQLQKGGYASvkahELIEARKRLNKANEKK- 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1203 eqleqtkrVKATLEKAKQTLENERGElanEVKAL-LQGKGDSEHKRKKVEAQLQE----LQVKFSEGERVRTELADKVSK 1277
Cdd:PRK00409 624 --------EKKKKKQKEKQEELKVGD---EVKYLsLGQKGEVLSIPDDKEAIVQAgimkMKVPLSDLEKIQKPKKKKKKK 692
|
|
| RUN_RUNDC1 |
cd17683 |
RUN domain found in RUN domain-containing protein 1 (RUNDC1) and similar proteins; RUN ... |
1531-1625 |
5.02e-03 |
|
RUN domain found in RUN domain-containing protein 1 (RUNDC1) and similar proteins; RUN domain-containing protein 1 (RUNDC1) is thought to a role as p53/TP53 inhibitor and as such may have oncogenic activity. This model contains the RUN domain.
Pssm-ID: 439045 Cd Length: 248 Bit Score: 40.68 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1531 EQQVEEMKTQLEELE---DELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEkkkqlvrqvREMEAELEDERKQRSI 1607
Cdd:cd17683 2 EQLVDQLKTQISDLErfiNFLQHWGDLRARLEIAVNRVIELAETQQRLDEEDSSS---------YTDSSDDPVVRSEDEL 72
|
90
....*....|....*...
gi 806638593 1608 AMAARKKLEMDLKDLEAH 1625
Cdd:cd17683 73 TTAVRKELAPALRDLLQH 90
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1513-1648 |
5.11e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1513 KDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVR 1592
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEAD 587
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 806638593 1593 EMEAELEDERKQRSIAMAARkklemDLKDLEAHIDTANKNREEAIKQLRKLQAQMK 1648
Cdd:PRK00409 588 EIIKELRQLQKGGYASVKAH-----ELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1384-1670 |
5.24e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.87 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1384 EEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTktrlqqELDDLLVDLDHQRQSVSNLEKKQKKFDQLLAEEKTISAKYAEE 1463
Cdd:COG5185 281 NENANNLIKQFENTKEKIAEYTKSIDIKKAT------ESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1464 RDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSvheLEKSKRALEQQVEEMKTQLEE 1543
Cdd:COG5185 355 NLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILAT---LEDTLKAADRQIEELQRQIEQ 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1544 LEDELQATEDAKLRLEVNLQAMKAQFERDLQgrdEQSEEKKKQLVRQVREMEAELEDERKQrsiamaARKKLEMDLKDLE 1623
Cdd:COG5185 432 ATSSNEEVSKLLNELISELNKVMREADEESQ---SRLEEAYDEINRSVRSKKEDLNEELTQ------IESRVSTLKATLE 502
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 806638593 1624 AHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKE 1670
Cdd:COG5185 503 KLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASE 549
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
880-1716 |
5.37e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.74 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 880 AEKLQLQEQLQAEtELCAEAEELRARLTAK----KQELEEICHDLEARVEEEEERCQYLQAEKKKmqqnIQELEEQLEEE 955
Cdd:NF041483 220 AERLLNAASTQAQ-EATDHAEQLRSSTAAEsdqaRRQAAELSRAAEQRMQEAEEALREARAEAEK----VVAEAKEAAAK 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 956 ESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLEDRVAEFTTNLMEEEEKSKS---------LAKLKNKHE 1026
Cdd:NF041483 295 QLASAESANEQRTRTAKEEIARLVGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKARTvaaedtaaqLAKAARTAE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1027 AMITDLEERLRREEKQ-RQELEKTRRKLEGDSTDLSDQIAELQAQiaeLKMQLAKKEEELQAALARVEEEAaqknmalkk 1105
Cdd:NF041483 375 EVLTKASEDAKATTRAaAEEAERIRREAEAEADRLRGEAADQAEQ---LKGAAKDDTKEYRAKTVELQEEA--------- 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1106 iRELETQISELQEDLESErACRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVSILKKTLEDEAKTHEA 1185
Cdd:NF041483 443 -RRLRGEAEQLRAEAVAE-GERIRGEARREAVQQIEEAARTAEELLTKAKADADELRSTATAESERVRTEAIERATTLRR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1186 QIQEMRQKHSQAVEEL-AEQLEQTKRVKATLEKAKQTL--ENERGELANEVKA---LLQGKGDSEHKRKKVEAQLQELQv 1259
Cdd:NF041483 521 QAEETLERTRAEAERLrAEAEEQAEEVRAAAERAARELreETERAIAARQAEAaeeLTRLHTEAEERLTAAEEALADAR- 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1260 kfSEGERVRTELADKVSKLQVEL-DSVTGLLNQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEK 1338
Cdd:NF041483 600 --AEAERIRREAAEETERLRTEAaERIRTLQAQAEQEAERLRTEAAADASAARAEGENVAVRLRSEAAAEAERLKSEAQE 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1339 NSFREQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETA--------EEAKRRLQKDLEGLSQRLEEKVAAYDK 1410
Cdd:NF041483 678 SADRVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSAraeadqerERAREQSEELLASARKRVEEAQAEAQR 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1411 LEKTKTRLQQELDDLLVDLDHQ-RQSVSNLEKKqkkfdqllAEEKTISAKYAEER--DRAEAEAREKETKALSLARALEE 1487
Cdd:NF041483 758 LVEEADRRATELVSAAEQTAQQvRDSVAGLQEQ--------AEEEIAGLRSAAEHaaERTRTEAQEEADRVRSDAYAERE 829
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1488 AMEQKAELERLNKQFRTEMEDLMSSKdDVGKSVHELEKSKRALEQQVEEMKTqleELEDELQATEDAKLRlevnlqaMKA 1567
Cdd:NF041483 830 RASEDANRLRREAQEETEAAKALAER-TVSEAIAEAERLRSDASEYAQRVRT---EASDTLASAEQDAAR-------TRA 898
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1568 QFERDLQGRDEQSEEKKKQLVrqvreMEAELEDERKQRSIAMAARKKLEMDLKDleahidtANKNREEAIKQLRKLQAqm 1647
Cdd:NF041483 899 DAREDANRIRSDAAAQADRLI-----GEATSEAERLTAEARAEAERLRDEARAE-------AERVRADAAAQAEQLIA-- 964
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 806638593 1648 kDCMRELDDTRASREEILAQAKENEKKLKSmEAEMIQLQEElAAAERAKRQAQQERDELADEIANSSGK 1716
Cdd:NF041483 965 -EATGEAERLRAEAAETVGSAQQHAERIRT-EAERVKAEAA-AEAERLRTEAREEADRTLDEARKDANK 1030
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1131-1223 |
5.40e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.86 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1131 EKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEvsilKKTLEDEAKTHEAQIQEMRQKHSQ-AVEELAEQLEQTK 1209
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQE----LVALEGLAAELEEKQQELEAQLEQlQEKAAETSQERKQ 216
|
90
....*....|....
gi 806638593 1210 RVKATLEKAKQTLE 1223
Cdd:PRK11448 217 KRKEITDQAAKRLE 230
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1437-1730 |
5.44e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.75 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1437 SNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFrtemEDLMSSKDDV 1516
Cdd:PRK04778 119 EDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEFSQF----VELTESGDYV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1517 GKSVH--ELEKSKRALEQQVEEMKTQLEELEDELQA------------TED----AKLRLEVNLQAMKAQFERDL----Q 1574
Cdd:PRK04778 195 EAREIldQLEEELAALEQIMEEIPELLKELQTELPDqlqelkagyrelVEEgyhlDHLDIEKEIQDLKEQIDENLalleE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1575 GRDEQSEEKKKQLVRQVREMEAELEDErkqrsiaMAARKKLEMDLKDLEAHIDTANKNR-----------------EEAI 1637
Cdd:PRK04778 275 LDLDEAEEKNEEIQERIDQLYDILERE-------VKARKYVEKNSDTLPDFLEHAKEQNkelkeeidrvkqsytlnESEL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1638 KQLRKLQAQMKDCMRELDDTRASRE-------EILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEI 1710
Cdd:PRK04778 348 ESVRQLEKQLESLEKQYDEITERIAeqeiaysELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKL 427
|
330 340
....*....|....*....|
gi 806638593 1711 ANSsgkgalaleeKRRLEAR 1730
Cdd:PRK04778 428 HEI----------KRYLEKS 437
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1001-1226 |
5.59e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.48 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1001 VAEFTTNLMEEEEKSKSLAKlknkhEAMITDLEE--------RLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIA 1072
Cdd:pfam15709 302 TFVVTGNMESEEERSEEDPS-----KALLEKREQekasrdrlRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMRE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1073 ELKMQLAKKEEELQAALARVEEEAAQknmalkkiRELETQISELQEDLESERACRNKAEKQKRDLGEELEALKTELEDTL 1152
Cdd:pfam15709 377 ELELEQQRRFEEIRLRKQRLEEERQR--------QEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAE 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 806638593 1153 DSTAAQQELRSKREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVkATLEKAKQTLENER 1226
Cdd:pfam15709 449 AEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARL-ALEEAMKQAQEQAR 521
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1610-1852 |
5.59e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1610 AARKKLEMDLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTRASREEilaqakenEKKLKSMEAEMIQLQEEL 1689
Cdd:PRK11281 73 DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLSLRQL--------ESRLAQTLDQLQNAQNDL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1690 AAA-----------ERAKRQ---AQQERDELADEIANSS-GKGALALEEKRRLEARI----AQLEEELEEEQGNTELI-- 1748
Cdd:PRK11281 145 AEYnsqlvslqtqpERAQAAlyaNSQRLQQIRNLLKGGKvGGKALRPSQRVLLQAEQallnAQNDLQRKSLEGNTQLQdl 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1749 -NDRLKKANLQIDQINTDLNLERSHAqkNENARQQLERQNKElkakLQEMESAVKSKYKASIAALEAKIAQLEEQLDNET 1827
Cdd:PRK11281 225 lQKQRDYLTARIQRLEHQLQLLQEAI--NSKRLTLSEKTVQE----AQSQDEAARIQANPLVAQELEINLQLSQRLLKAT 298
|
250 260
....*....|....*....|....*
gi 806638593 1828 KERQAASKQVRRAEKKLkDVLLQVE 1852
Cdd:PRK11281 299 EKLNTLTQQNLRVKNWL-DRLTQSE 322
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1031-1170 |
5.92e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 41.58 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1031 DLEERLRREEKQRQeLEKTRRKLEGDSTDLSDQIAELQAQ-------IAELKMQLA-------KKEEELQAALARVEEEA 1096
Cdd:pfam05911 679 KTEENKRLKEEFEQ-LKSEKENLEVELASCTENLESTKSQlqeseqlIAELRSELAslkesnsLAETQLKCMAESYEDLE 757
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 806638593 1097 AQKNMALKKIRELETQISELQEDLESERACRNKAEKQKRDLGEELEalKTELEDTLDSTAAQQELRSKREQEVS 1170
Cdd:pfam05911 758 TRLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLE--RNEKKESSNCDADQEDKKLQQEKEIT 829
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1292-1559 |
6.60e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.95 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1292 SDSKSSKLTKDFSALESQLQDTQELLQEENRQklslSTKLKQMEDEKNSFREQLEEEEEAKRNLEKQIATLHAQVTDMKK 1371
Cdd:pfam15905 61 LKKKSQKNLKESKDQKELEKEIRALVQERGEQ----DKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1372 kmedgVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQELDDLLVDL----DHQRQSVSNLEKKQKKFD 1447
Cdd:pfam15905 137 -----VNELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTqknlEHSKGKVAQLEEKLVSTE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1448 QLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSK 1527
Cdd:pfam15905 212 KEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEK 291
|
250 260 270
....*....|....*....|....*....|..
gi 806638593 1528 ralEQQVEEMKTQLEELEDELQATEDaKLRLE 1559
Cdd:pfam15905 292 ---EELLREYEEKEQTLNAELEELKE-KLTLE 319
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1500-1710 |
7.05e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 40.40 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1500 KQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATED-AKLRLEVNLQAMKAQFERD-----L 1573
Cdd:pfam00261 4 QQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEErLAEALEKLEEAEKAADESErgrkvL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1574 QGRDEQSEEKKKQLVRQVRemEAELEDERKQRSIAMAARKklemdLKDLEAHIDTANKNREEAIKQLRKLQAQMKDCMRE 1653
Cdd:pfam00261 84 ENRALKDEEKMEILEAQLK--EAKEIAEEADRKYEEVARK-----LVVVEGDLERAEERAELAESKIVELEEELKVVGNN 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 806638593 1654 LDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEI 1710
Cdd:pfam00261 157 LKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDEL 213
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
865-1154 |
7.48e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 865 ENRLTEMETMQSQLMAEKLQLQEQLQaetELCAEAEELRARLTAKKQELEEichdLEARVEEEEERCQYLQAEKKKMQQN 944
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELNEELK---ELAEKRDELNAQVKELREEAQE----LREKRDELNEKVKELKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 945 IQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDQIIMEDQNCKLAKEKKLLedrvaefttnlmeeeEKSKSLAKLKNK 1024
Cdd:COG1340 87 LNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELV---------------EKIKELEKELEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1025 HEAMItDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALK 1104
Cdd:COG1340 152 AKKAL-EKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHE 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 806638593 1105 KIRELETQISELQEDLESERACRNKAEKQKRDlgEELEALKTELEDTLDS 1154
Cdd:COG1340 231 EIIELQKELRELRKELKKLRKKQRALKREKEK--EELEEKAEEIFEKLKK 278
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1002-1142 |
7.56e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 40.99 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1002 AEFTTNLME--EEEKSKSlAKLKNKHEAMITDLEERLRRE--------EKQRQELEKTRRKLEGDSTDLSDQIAELQAQI 1071
Cdd:pfam03148 203 EKFTQDNIEraEKERAAS-AQLRELIDSILEQTANDLRAQadavnfalRKRIEETEDAKNKLEWQLKKTLQEIAELEKNI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1072 AELKMQLAKKEEELQAALARVEEEAAQKNMAL----------KKIRELETQISELQEDLESERACRNKAEKQKRDLGEEL 1141
Cdd:pfam03148 282 EALEKAIRDKEAPLKLAQTRLENRTYRPNVELcrdeaqyglvDEVKELEETIEALKQKLAEAEASLQALERTRLRLEEDI 361
|
.
gi 806638593 1142 E 1142
Cdd:pfam03148 362 A 362
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1610-1711 |
7.64e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1610 AARKKLEMD-----LKDLEAHIDTANKNREEAIK--------QLRKLQAQMKDCMRELDDTRA---SREEILAQAKENEK 1673
Cdd:COG0542 399 AARVRMEIDskpeeLDELERRLEQLEIEKEALKKeqdeasfeRLAELRDELAELEEELEALKArweAEKELIEEIQELKE 478
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 806638593 1674 KLKSMEAEMIQLQEELAAAERAKRQAQQ-ERDEL-ADEIA 1711
Cdd:COG0542 479 ELEQRYGKIPELEKELAELEEELAELAPlLREEVtEEDIA 518
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1586-1733 |
7.94e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.48 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1586 QLVRQVREMEAELEDERKQRSIAMAARKKLEMdlkdLEAHIDTANKNREEAIKQLRKLQAQMKDCMRELDDTR--ASREE 1663
Cdd:pfam00529 55 DYQAALDSAEAQLAKAQAQVARLQAELDRLQA----LESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQidLARRR 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 806638593 1664 ILAQAKE-NEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIAnssgkgALALEEKRRLEARIAQ 1733
Cdd:pfam00529 131 VLAPIGGiSRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQ------AEVRSELSGAQLQIAE 195
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1198-1465 |
8.43e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 41.19 E-value: 8.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1198 VEELAEQLEQTKR----VKAT------------LEKAKQTLENERGELANEVKALLQGKGDSEHKRKKVEAQLQELQVKF 1261
Cdd:PTZ00108 1104 VEKLNAELEKKEKelekLKNTtpkdmwledldkFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKK 1183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1262 SEGERVRTELaDKVSKLQVELDSVTGLLNQSDSKSSKlTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQMEDEKNSF 1341
Cdd:PTZ00108 1184 SSADKSKKAS-VVGNSKRVDSDEKRKLDDKPDNKKSN-SSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFS 1261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1342 REQLEEEEEAKRNLEKQIATLHAQVTDMKKKMEDGVGCLETAEEAKRRLQKDLEGLSQRLEEKVAAYDKLEKTKTRLQQE 1421
Cdd:PTZ00108 1262 SDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKKSKTRV 1341
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 806638593 1422 LDDLLVdldhqRQSVSNLEKKQKKFDQLLAEEKTISAKYAEERD 1465
Cdd:PTZ00108 1342 KQASAS-----QSSRLLRRPRKKKSDSSSEDDDDSEVDDSEDED 1380
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
851-1201 |
9.04e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 40.99 E-value: 9.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 851 EAELTKVREKHLAAENRLTEMETMQSQLMAEKlqLQEQLQAETELCAEAEELRARLTAKKQELeeichdleARVEEEEER 930
Cdd:PLN03229 435 EGEVEKLKEQILKAKESSSKPSELALNEMIEK--LKKEIDLEYTEAVIAMGLQERLENLREEF--------SKANSQDQL 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 931 CQYLQAEK-KKMQQNIQELEEQLEEEESARQKLQlekvtteaKLKKLEEDQIIMEdQNCKLAKEKKLLEDRVAEfTTNLM 1009
Cdd:PLN03229 505 MHPVLMEKiEKLKDEFNKRLSRAPNYLSLKYKLD--------MLNEFSRAKALSE-KKSKAEKLKAEINKKFKE-VMDRP 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1010 EEEEKSKSL-AKLKNKHEAMITDLEERLRRE-EKQRQELEKTRRKLEgDSTDLsdQIAELQAQIAELKMQLAkkEEELQA 1087
Cdd:PLN03229 575 EIKEKMEALkAEVASSGASSGDELDDDLKEKvEKMKKEIELELAGVL-KSMGL--EVIGVTKKNKDTAEQTP--PPNLQE 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1088 ALARVEEEAAQKNMALKKIRELETQISELQEDLESERACRNKAEKQKrdlgeeLEALKTELEDTL----DSTAAQQELRS 1163
Cdd:PLN03229 650 KIESLNEEINKKIERVIRSSDLKSKIELLKLEVAKASKTPDVTEKEK------IEALEQQIKQKIaealNSSELKEKFEE 723
|
330 340 350
....*....|....*....|....*....|....*...
gi 806638593 1164 KREQEVSILKKTLEDEAKTHEAQIQEMRQKHSQAVEEL 1201
Cdd:PLN03229 724 LEAELAAARETAAESNGSLKNDDDKEEDSKEDGSRVEV 761
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1516-1711 |
9.60e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.81 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1516 VGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFErDLQGRDEQS-----EEKKKQLVRQ 1590
Cdd:COG1842 14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAE-KWEEKARLAlekgrEDLAREALER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1591 VREMEAELEDERKQRSIAMAARKKLEMDLKDLEAHIDTANKNREEAIKQLR--KLQAQMKDCMRELDDTRASREeiLAQA 1668
Cdd:COG1842 93 KAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKaaKAQEKVNEALSGIDSDDATSA--LERM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 806638593 1669 KEnekKLKSMEAEMiQLQEELAAAERAKRQ--AQQERDELADEIA 1711
Cdd:COG1842 171 EE---KIEEMEARA-EAAAELAAGDSLDDElaELEADSEVEDELA 211
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1781-1877 |
9.68e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 9.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638593 1781 QQLERQNKELKAKLQEMESAVKSKYKASIAALEAKIAQLEEQLDnETKERQAASKQVRRAEKKLKDVLLQVEDERRNAEQ 1860
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELE-ALKARWEAEKELIEEIQELKEELEQRYGKIPELEK 492
|
90
....*....|....*..
gi 806638593 1861 FKDQADKASTRLKQLKR 1877
Cdd:COG0542 493 ELAELEEELAELAPLLR 509
|
|
| |
