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Conserved domains on  [gi|1034599857|ref|XP_016880169|]
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myosin-10 isoform X5 [Homo sapiens]

Protein Classification

MYSc_Myh10 and Myosin_tail_1 domain-containing protein (domain architecture ID 12036895)

protein containing domains Myosin_N, MYSc_Myh10, and Myosin_tail_1

Graphical summary

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List of domain hits

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 ...
857-1937 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: 396244 [Multi-domain]  Cd Length: 1081  Bit Score: 1488.51  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  857 TRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDL 936
Cdd:pfam01576    1 TRQEEEMQAKEEELQKVKEKQQKAESELKELEKKHQQLIEEKNILAEQLQAETELFAEAEEMRARLAARKQELEEILHDL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  937 ESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFIKEKKLMEDR 1016
Cdd:pfam01576   81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLEEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1017 IAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIDELKLQLAK 1096
Cdd:pfam01576  161 ISEFTSNLAEEEEKVKSLNKLKNKHEAMISDLEDRLKKEEKGRQELEKAKRKLDGESTDLQEQIAELQAQIEELRAQLAK 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1097 KEEELQGALARGDDETLHKNNALKVVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQE 1176
Cdd:pfam01576  241 KEEELQAALARLEEEGAQKNNALKKLRELQAQIAELQEDLESERAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQE 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1177 LRTKREQEVAELKKALEEETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVK 1256
Cdd:pfam01576  321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELSEQLEQAKRNKANLEKAKQALESENNELQAELKTLQQAK 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1257 AESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKASKLQNELDNVSTLLEEAEKKGIKFAKDAASLESQLQDTQELLQEE 1336
Cdd:pfam01576  401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSGLLSEAEGKSIKLSKDVSSLESQLQDTQELLQEE 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1337 TRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDAEALSQR 1416
Cdd:pfam01576  481 TRQKLNLSSRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSEMKKKLEEDAGAVEALEEAKKRLQRELEALTQR 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1417 LEEKALAYDKLEKTKNRLQQELDDLTVDLDHQRQVASNLEKKQKKFDQLLAEEKSISARYAEERDRAEAEAREKETKALS 1496
Cdd:pfam01576  561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1497 LARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEV 1576
Cdd:pfam01576  641 LSRALEEALEAKEELERQNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1577 NMQAMKAQFERDLQTRDEQNEEKKRLLIKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQL 1656
Cdd:pfam01576  721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGRDEAVKQL 800
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1657 RKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEITNSASGKSAL 1736
Cdd:pfam01576  801 KKLQAQMKELQRELEETRASRDEILAQSKESEKKLKSLEAELLQLQEDLAASERAKRQAQQERDELADEIANGASGKSAL 880
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1737 LDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGA 1816
Cdd:pfam01576  881 LDEKRRLEARIAQLEEELEEEQSNTELLNDRYRKLTLQVEQLTTELSAERSFSQKSESARQQLERQNKELKAKLQEMEGT 960
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1817 VKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLE 1896
Cdd:pfam01576  961 VKSKYKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRNADQYKDQAEKANSRMKQLKRQLE 1040
                         1050      1060      1070      1080
                   ....*....|....*....|....*....|....*....|.
gi 1034599857 1897 EAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1937
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESAESMNREVSTLRSKL 1081
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
99-780 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  Cd Length: 673  Bit Score: 1443.66  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857   99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14920      1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIpespkpvkhQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 258
Cdd:cd14920     81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNI---------PGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  259 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQET 338
Cdd:cd14920    152 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQET 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  339 MEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQ 418
Cdd:cd14920    232 MEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQ 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  419 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 498
Cdd:cd14920    312 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  499 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQL 578
Cdd:cd14920    392 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQL 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  579 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGM 658
Cdd:cd14920    472 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGM 551
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  659 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 738
Cdd:cd14920    552 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 631
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 1034599857  739 ILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 780
Cdd:cd14920    632 ILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
Myosin_N pfam02736
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ...
33-72 1.13e-08

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: 397036  Cd Length: 39  Bit Score: 52.38  E-value: 1.13e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1034599857   33 KKLVWIPSERHGFEAASIKEERGDEVMVELaENGKKAMVN 72
Cdd:pfam02736    1 KKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVK 39
 
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 ...
857-1937 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: 396244 [Multi-domain]  Cd Length: 1081  Bit Score: 1488.51  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  857 TRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDL 936
Cdd:pfam01576    1 TRQEEEMQAKEEELQKVKEKQQKAESELKELEKKHQQLIEEKNILAEQLQAETELFAEAEEMRARLAARKQELEEILHDL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  937 ESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFIKEKKLMEDR 1016
Cdd:pfam01576   81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLEEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1017 IAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIDELKLQLAK 1096
Cdd:pfam01576  161 ISEFTSNLAEEEEKVKSLNKLKNKHEAMISDLEDRLKKEEKGRQELEKAKRKLDGESTDLQEQIAELQAQIEELRAQLAK 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1097 KEEELQGALARGDDETLHKNNALKVVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQE 1176
Cdd:pfam01576  241 KEEELQAALARLEEEGAQKNNALKKLRELQAQIAELQEDLESERAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQE 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1177 LRTKREQEVAELKKALEEETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVK 1256
Cdd:pfam01576  321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELSEQLEQAKRNKANLEKAKQALESENNELQAELKTLQQAK 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1257 AESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKASKLQNELDNVSTLLEEAEKKGIKFAKDAASLESQLQDTQELLQEE 1336
Cdd:pfam01576  401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSGLLSEAEGKSIKLSKDVSSLESQLQDTQELLQEE 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1337 TRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDAEALSQR 1416
Cdd:pfam01576  481 TRQKLNLSSRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSEMKKKLEEDAGAVEALEEAKKRLQRELEALTQR 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1417 LEEKALAYDKLEKTKNRLQQELDDLTVDLDHQRQVASNLEKKQKKFDQLLAEEKSISARYAEERDRAEAEAREKETKALS 1496
Cdd:pfam01576  561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1497 LARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEV 1576
Cdd:pfam01576  641 LSRALEEALEAKEELERQNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1577 NMQAMKAQFERDLQTRDEQNEEKKRLLIKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQL 1656
Cdd:pfam01576  721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGRDEAVKQL 800
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1657 RKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEITNSASGKSAL 1736
Cdd:pfam01576  801 KKLQAQMKELQRELEETRASRDEILAQSKESEKKLKSLEAELLQLQEDLAASERAKRQAQQERDELADEIANGASGKSAL 880
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1737 LDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGA 1816
Cdd:pfam01576  881 LDEKRRLEARIAQLEEELEEEQSNTELLNDRYRKLTLQVEQLTTELSAERSFSQKSESARQQLERQNKELKAKLQEMEGT 960
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1817 VKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLE 1896
Cdd:pfam01576  961 VKSKYKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRNADQYKDQAEKANSRMKQLKRQLE 1040
                         1050      1060      1070      1080
                   ....*....|....*....|....*....|....*....|.
gi 1034599857 1897 EAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1937
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESAESMNREVSTLRSKL 1081
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
99-780 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  Cd Length: 673  Bit Score: 1443.66  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857   99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14920      1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIpespkpvkhQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 258
Cdd:cd14920     81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNI---------PGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  259 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQET 338
Cdd:cd14920    152 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQET 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  339 MEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQ 418
Cdd:cd14920    232 MEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQ 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  419 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 498
Cdd:cd14920    312 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  499 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQL 578
Cdd:cd14920    392 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQL 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  579 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGM 658
Cdd:cd14920    472 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGM 551
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  659 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 738
Cdd:cd14920    552 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 631
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 1034599857  739 ILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 780
Cdd:cd14920    632 ILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
Myosin_head pfam00063
Myosin head (motor domain);
87-780 0e+00

Myosin head (motor domain);


Pssm-ID: 395017  Cd Length: 674  Bit Score: 1111.58  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857   87 VEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML 166
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  167 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKdhnipespkpvkhQGELERQLLQANPILESFGNAKTVKND 246
Cdd:pfam00063   81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN-------------VGRLEEQILQSNPILEAFGNAKTVRNN 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  247 NSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSN-GYIP 325
Cdd:pfam00063  148 NSSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQsGCYT 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  326 IPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAI 405
Cdd:pfam00063  228 IDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKAL 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  406 LTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCI 485
Cdd:pfam00063  308 CKRRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCI 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  486 NYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQE 565
Cdd:pfam00063  388 NYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYST 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  566 QGSHSKFQKPRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTE 645
Cdd:pfam00063  465 FSKHPHFQKPRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKS 543
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  646 TafgsAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFP 725
Cdd:pfam00063  544 T----PKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFP 619
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034599857  726 NRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 780
Cdd:pfam00063  620 NRITFQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
80-792 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  Cd Length: 677  Bit Score: 1018.24  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857    80 NPPKFSKVEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISE 159
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857   160 SAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnipespkpvkhQGELERQLLQANPILESFGN 239
Cdd:smart00242   81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTE---------------VGSVEDQILESNPILEAFGN 145
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857   240 AKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFL 319
Cdd:smart00242  146 AKTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYL 225
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857   320 SNG-YIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENT-VAQKLCHLLGMN 397
Cdd:smart00242  226 NQGgCLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVD 305
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857   398 VMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFEL 477
Cdd:smart00242  306 PEELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLS-FKDGSTYFIGVLDIYGFEIFEV 384
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857   478 NSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKT 557
Cdd:smart00242  385 NSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQT 461
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857   558 FVEKLVQEQGSHSKFQKPRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrivgl 637
Cdd:smart00242  462 FLEKLNQHHKKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS------- 533
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857   638 dqvtgmtetafGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGI 717
Cdd:smart00242  534 -----------GVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENI 602
                           650       660       670       680       690       700       710
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034599857   718 RICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFRAGVLAHLEEERD 792
Cdd:smart00242  603 RIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
COG5022 COG5022
Myosin heavy chain [General function prediction only];
36-1357 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 917.55  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857   36 VWIPSERHGFEAASIKEERGDEVMVELA---ENGKKAMVNKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLKDRYY 110
Cdd:COG5022     12 CWIPDEEKGWIWAEIIKEAFNKGKVTEEgkkEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  111 SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKK 190
Cdd:COG5022     92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  191 VIQYLAHVASSHKGRKdhnipespkpvkhqGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANI 270
Cdd:COG5022    172 IMQYLASVTSSSTVEI--------------SSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKI 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  271 ETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIP-IPGQQDKDNFQETMEAMHIMGFSH 349
Cdd:COG5022    238 ETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDE 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  350 EEILSMLKVVSSVLQFGNISFKKERNtDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFA 429
Cdd:COG5022    318 EEQDQIFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAI 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  430 VEALAKATYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQ 509
Cdd:COG5022    397 RDSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYV 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  510 REGIEWNFIDFgLDLQPCIDLIERpANPPGVLALLDEECWFPKATDKTFVEKLVQ--EQGSHSKFQKPRQLKDKadFCII 587
Cdd:COG5022    476 KEGIEWSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDNK--FVVK 551
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  588 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVgldqvtgmtetafgsayktKKGMFRTVGQLYK 667
Cdd:COG5022    552 HYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-------------------SKGRFPTLGSRFK 612
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  668 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA--- 744
Cdd:COG5022    613 ESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswt 692
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  745 -IPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFRAGVLAHLEEERDLKITDIIIFFQAVCRGYLARKAFAKKQQQLS 823
Cdd:COG5022    693 gEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIK 772
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  824 ALKVLQRNCAAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEEL--LKVKEKQTKVEGELEEMERKHQqlleeknil 901
Cdd:COG5022    773 KIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIikLQKTIKREKKLRETEEVEFSLK--------- 843
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  902 AEQLQAETELFAEAEEMRARLaaKKQELEEilhdlesrveeeeernQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLE 981
Cdd:COG5022    844 AEVLIQKFGRSLKAKKRFSLL--KKETIYL----------------QSAQRVELAERQLQELKIDVKSISSLKLVNLELE 905
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  982 KVTAEAKIKKMEEEILLLEDQNSKFIKEKKLMEDRIAECSS--QLAEEEEKAKNLAKIRNKQEVmISDLEERLKKEEKTR 1059
Cdd:COG5022    906 SEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPsiEYVKLPELNKLHEVESKLKET-SEEYEDLLKKSTILV 984
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1060 QELEKAKRKLDGettdLQDQIAELQAQIDELKLQLAKKEEElqgalargDDETLHKNNALKVVRELQAQIAELQEdfesE 1139
Cdd:COG5022    985 REGNKANSELKN----FKKELAELSKQYGALQESTKQLKEL--------PVEVAELQSASKIISSESTELSILKP----L 1048
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1140 KASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEEETKNHEA-----QIQDMRQRHATAL 1214
Cdd:COG5022   1049 QKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKpanvlQFIVAQMIKLNLL 1128
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1215 EELSEQLEQAkrfKANLEKNKQGLETDNKELACevkVLQQVKAESEHKRKKLDAQVQEL-----------HAKVSEGDRL 1283
Cdd:COG5022   1129 QEISKFLSQL---VNTLEPVFQKLSVLQLELDG---LFWEANLEALPSPPPFAALSEKRlyqsalydeksKLSSSEVNDL 1202
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1284 RVELAEKASKlQNELDNVSTLLEEAEKKGI------KFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSL 1357
Cdd:COG5022   1203 KNELIALFSK-IFSGWPRGDKLKKLISEGWvpteysTSLKGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEV 1281
PTZ00014 PTZ00014
myosin-A; Provisional
97-833 1.92e-131

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 433.30  E-value: 1.92e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857   97 NEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHE-MPPHIYAISESAYRCMLQDREDQSIL 175
Cdd:PTZ00014   108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  176 CTGESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIpespkpvkhqgelERQLLQANPILESFGNAKTVKNDNSSRFGKFI 255
Cdd:PTZ00014   188 VSGESGAGKTEATKQIMRYFA---SSKSGNMDLKI-------------QNAIMAANPVLEAFGNAKTIRNNNSSRFGRFM 251
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  256 RINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNF 335
Cdd:PTZ00014   252 QLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDF 331
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  336 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISF--KKERNTDQASM--PEN-TVAQKLCHLLGMNVMEFTRAILTPRI 410
Cdd:PTZ00014   332 EEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESlEVFNEACELLFLDYESLKKELTVKVT 411
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  411 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsFIGILDIAGFEIFELNSFEQLCINYTNE 490
Cdd:PTZ00014   412 YAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFINITNE 490
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  491 KLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVEKLVQEQGSHS 570
Cdd:PTZ00014   491 MLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNP 567
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  571 KFQKPRQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGldqvtgmtetafgs 650
Cdd:PTZ00014   568 KYKPAKVDSNK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKG-------------- 632
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  651 ayKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVF 730
Cdd:PTZ00014   633 --KLAKGQL--IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTF 708
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  731 QEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR---AGVLAHLEEERDLKITDIIIFFQAVCR 807
Cdd:PTZ00014   709 AEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALIL 788
                          730       740
                   ....*....|....*....|....*.
gi 1034599857  808 GYLARKAFAKKqqqlsaLKVLQRNCA 833
Cdd:PTZ00014   789 KIKKKRKVRKN------IKSLVRIQA 808
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
860-1693 1.35e-39

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 161.81  E-value: 1.35e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  860 EEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFA----EAEEMRARLAAKKQELEEILHD 935
Cdd:COG1196    178 ERKLERTEENLERLEDLLEELEKQLEKLERQAEKAERYQELKAELRELELALLLaklkELRKELEELEEELSRLEEELEE 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  936 LESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFIKEKKLMED 1015
Cdd:COG1196    258 LQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALKE 337
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1016 RIAECSSQLAEEEEKAKNLAKIRNKQEvmiSDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIDELKLQLA 1095
Cdd:COG1196    338 ELEERETLLEELEQLLAELEEAKEELE---EKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLE 414
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1096 KKEEELQGALARGDDETLHKNNALKVVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELED---TLDTTA 1172
Cdd:COG1196    415 RLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSSleaRLDRLE 494
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1173 AQQElRTKREQEVAELKKALEEETKNHEAQIQDMRQRHATALEE---------LSEQLEQAKRFKANLEKNKQGLETdnk 1243
Cdd:COG1196    495 AEQR-ASQGVRAVLEALESGLPGVYGPVAELIKVKEKYETALEAalgnrlqavVVENEEVAKKAIEFLKENKAGRAT--- 570
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1244 elaceVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVelaekasKLQNELDN--VSTLLEEAEK--KGIKFAKDA 1319
Cdd:COG1196    571 -----FLPLDRIKPLRSLKSDAAPGFLGLASDLIDFDPKYEP-------AVRFVLGDtlVVDDLEQARRlaRKLRIKYRI 638
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1320 ASLESQLQDTQELLQEETRQK---LNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKkvdddlgTI 1396
Cdd:COG1196    639 VTLDGDLVEPSGSITGGSRNKrssLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRR-------QL 711
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1397 ESLEEAKKKLLKDAEALSQRLEEKALAYDKLEKTKNRLQQELDDLTVDLDHQRQVASNLEKKQKKFDQLLAEEKSISARY 1476
Cdd:COG1196    712 EELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQAL 791
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1477 AEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQ 1556
Cdd:COG1196    792 QEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAE 871
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1557 LEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLIKQVR-ELEAELEDERKQRALAVASKKKMEIDL 1635
Cdd:COG1196    872 KEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERlEVELPELEEELEEEYEDTLETELEREI 951
                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034599857 1636 KDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKS 1693
Cdd:COG1196    952 ERLEEEIEALGPVNLRAIEEYEEVEERYEELKSQREDLEEAKEKLLEVIEELDKEKRE 1009
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1014-1870 1.24e-35

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: 148.67  E-value: 1.24e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1014 EDRIAECSSQL------AEEEEKAKNL-AKIRNKQ-EVMISDLEERLKKEEKTRQELEKAKRKLDgettDLQDQIAELQA 1085
Cdd:TIGR02168  192 EDILNELERQLkslerqAEKAERYKELkAELRELElALLVLRLEELREELEELQEELKEAEEELE----ELTAELQELEE 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1086 QIDELKLQLAKKEEELQGALARGDDETLHKNNALKVVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELE 1165
Cdd:TIGR02168  268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1166 DTLDTTAAQQELRTKREQEVAELKKALEEETKNHEAQIQDMRQRHATaLEELSEQLEQAKRFKANLEKNKQGLETDNkel 1245
Cdd:TIGR02168  348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ-IASLNNEIERLEARLERLEDRRERLQQEI--- 423
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1246 acevkvlqqvkaeSEHKRKKLDAQVQELHAKVSEGDRLRVELAEKASKLQNELDNVSTLLEEAEKKGIKFAKDAASLESQ 1325
Cdd:TIGR02168  424 -------------EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1326 LQDTQELLQEetrqKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVdddlgTIESLEEAKKk 1405
Cdd:TIGR02168  491 LDSLERLQEN----LEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAV-----VVENLNAAKK- 560
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1406 llkDAEALSQRLEEKALAYDKLEKTKNRLQQELDDLTVDLDHQRQVASNLEKKQKKFDQLLAeekSISARYAEERDRAEA 1485
Cdd:TIGR02168  561 ---AIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS---YLLGGVLVVDDLDNA 634
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1486 EAREKETKAL---------------SLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQV 1550
Cdd:TIGR02168  635 LELAKKLRPGyrivtldgdlvrpggVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEEL 714
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1551 EEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLiKQVRELEAELEDERKQRALAVASKKK 1630
Cdd:TIGR02168  715 EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE-ERLEEAEEELAEAEAEIEELEAQIEQ 793
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1631 MEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSER 1710
Cdd:TIGR02168  794 LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1711 ARRHAEQERDELADEITNSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSA-- 1788
Cdd:TIGR02168  874 ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtl 953
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1789 ------AQKSDNARQQLERQNKELKAKLQELeGAVKSKFKATISALEAKIGQLEEQLE--QEAKE--RAAANKLVRRTEK 1858
Cdd:TIGR02168  954 eeaealENKIEDDEEEARRRLKRLENKIKEL-GPVNLAAIEEYEELKERYDFLTAQKEdlTEAKEtlEEAIEEIDREARE 1032
                          890
                   ....*....|..
gi 1034599857 1859 KLKEIFMQVEDE 1870
Cdd:TIGR02168 1033 RFKDTFDQVNEN 1044
PTZ00121 PTZ00121
MAEBL; Provisional
859-1729 1.09e-22

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 106.76  E-value: 1.09e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  859 QEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEmrARLAAKKQELEEILHDLES 938
Cdd:PTZ00121  1068 QDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAED--ARKAEEARKAEDARKAEEA 1145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  939 RVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFIKEKKLMEDRIA 1018
Cdd:PTZ00121  1146 RKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKK 1225
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1019 ECSSQLAEE----EEKAKNLAKIRNKQEvmISDLEERLKKEEKTRQELEKAKRKLDGEttdlqdqiaELQAQIDELKLQL 1094
Cdd:PTZ00121  1226 AEAVKKAEEakkdAEEAKKAEEERNNEE--IRKFEEARMAHFARRQAAIKAEEARKAD---------ELKKAEEKKKADE 1294
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1095 AKKEEELQGAlargdDETLHKNNALKVVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQ 1174
Cdd:PTZ00121  1295 AKKAEEKKKA-----DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1175 QELRTKREQEVAELKKALEEETKNHEAQIQ-DMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKelACEVKVLQ 1253
Cdd:PTZ00121  1370 EKKKEEAKKKADAAKKKAEEKKKADEAKKKaEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKK--AEEAKKAD 1447
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1254 QVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKASKLQNEldnvstlLEEAEKKgikfAKDAASLESQLQDTQELL 1333
Cdd:PTZ00121  1448 EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK-------AEEAKKK----ADEAKKAAEAKKKADEAK 1516
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1334 QEETRQKlnlSSRIRQLEEEKNSLQEQQEEEEEARKNLEKqvlALQSQLADTKKKVDDDlgtiESLEEAKKKLLKDAEAL 1413
Cdd:PTZ00121  1517 KAEEAKK---ADEAKKAEEAKKADEAKKAEEKKKADELKK---AEELKKAEEKKKAEEA----KKAEEDKNMALRKAEEA 1586
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1414 SQ----RLEEKALAYDKLEKTKNRLQQELDDLTVDLDHQR----------QVASNLEKKQKKFDQLLAEEKSISARYAEE 1479
Cdd:PTZ00121  1587 KKaeeaRIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKkaeeekkkveQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1480 RDRAEAEAREKETkalslARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTqlEE 1559
Cdd:PTZ00121  1667 AKKAEEDKKKAEE-----AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK--EA 1739
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1560 LEDELQATEdakLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLIKQvreleaELEDERKQRALAVASKKKmeiDLKDLE 1639
Cdd:PTZ00121  1740 EEDKKKAEE---AKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE------ELDEEDEKRRMEVDKKIK---DIFDNF 1807
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1640 AQIEAANKARDEVIKQLRKLQ-AQMKDY----QRELEEARASRDEIFAQSKESEK---KLKSLEAEILQLQEELASSERA 1711
Cdd:PTZ00121  1808 ANIIEGGKEGNLVINDSKEMEdSAIKEVadskNMQLEEADAFEKHKFNKNNENGEdgnKEADFNKEKDLKEDDEEEIEEA 1887
                          890
                   ....*....|....*...
gi 1034599857 1712 RRHAEQERDELADEITNS 1729
Cdd:PTZ00121  1888 DEIEKIDKDDIEREIPNN 1905
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
1117-1446 1.43e-12

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 411490 [Multi-domain]  Cd Length: 660  Bit Score: 72.64  E-value: 1.43e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1117 NALKVVRELQAQIAELQEDF-ESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEEE 1195
Cdd:NF033930    55 AAKKAYEEAKKKAEDAQKKYdEDQKKTEEKAKKEKKASEEEQKANLAVQKAYVKYRKAQRRKKSDYKKKLAEADKKIDEA 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1196 TKNHE------AQIQDMRQRHATALEELSEQLEQAKRFKANLEKNkqgletdnkelacevkvLQQVKAESEHKRKKLDAQ 1269
Cdd:NF033930   135 KKKQKeakaefNKVRAKVVPEAEELAETKKKAEEAKAEEPVAKKK-----------------VDEAKKKVEEAKKKVEAE 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1270 VQELHAKVSEGDRLRVELAEkaskLQNELDNVSTLLEEAEKK-GIKFAKD--AASLESQLQDTQELLQEETRQKLNLSSR 1346
Cdd:NF033930   198 EAEIEKLQNEEVALEAKIAE----LENQVDNLEKELAEIDESdSEDYIKEglRAPLESELDAKQAKLAKKQTELEKLLDS 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1347 IRQLEEEKNSLqeqqeEEEEARKNLEKQVLALQSQLADTKKKVDDdlgtiesleeaKKKLLKDAEALSQRLEEKALAYDK 1426
Cdd:NF033930   274 LDPEGKTQDEL-----DKEAAEEELSKKIDELDNEVAKLEKEVSD-----------LENSDNNVADYYKEALEKDLATKK 337
                          330       340
                   ....*....|....*....|..
gi 1034599857 1427 --LEKTKNRLQQELDDLTVDLD 1446
Cdd:NF033930   338 aeLEKTQKDLDKALNELGPDGD 359
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
954-1273 3.21e-09

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 411490 [Multi-domain]  Cd Length: 660  Bit Score: 61.85  E-value: 3.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  954 KKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSK----FIKEKKLMEDRIAECSSQLAE--- 1026
Cdd:NF033930    50 VKKSEAAKKAYEEAKKKAEDAQKKYDEDQKKTEEKAKKEKKASEEEQKANLAvqkaYVKYRKAQRRKKSDYKKKLAEadk 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1027 --------EEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTdlqdQIAELQAQIDELKLQLAKKE 1098
Cdd:NF033930   130 kideakkkQKEAKAEFNKVRAKVVPEAEELAETKKKAEEAKAEEPVAKKKVDEAKK----KVEEAKKKVEAEEAEIEKLQ 205
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1099 EElqgalargddetlhknnalkvVRELQAQIAELQEdfESEKASRNKAEKQKRDLSEELEA-LKTELEDTLDttAAQQEL 1177
Cdd:NF033930   206 NE---------------------EVALEAKIAELEN--QVDNLEKELAEIDESDSEDYIKEgLRAPLESELD--AKQAKL 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1178 rTKREQEVAELKKALEEETKNHEAQIQDmrqrhaTALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKV-----L 1252
Cdd:NF033930   261 -AKKQTELEKLLDSLDPEGKTQDELDKE------AAEEELSKKIDELDNEVAKLEKEVSDLENSDNNVADYYKEalekdL 333
                          330       340
                   ....*....|....*....|.
gi 1034599857 1253 QQVKAESEHKRKKLDAQVQEL 1273
Cdd:NF033930   334 ATKKAELEKTQKDLDKALNEL 354
Myosin_N pfam02736
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ...
33-72 1.13e-08

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: 397036  Cd Length: 39  Bit Score: 52.38  E-value: 1.13e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1034599857   33 KKLVWIPSERHGFEAASIKEERGDEVMVELaENGKKAMVN 72
Cdd:pfam02736    1 KKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVK 39
Streccoc_I_II NF033804
antigen I/II family LPXTG-anchored adhesin; Members of the antigen I/II family are adhesins ...
1529-1876 1.82e-08

antigen I/II family LPXTG-anchored adhesin; Members of the antigen I/II family are adhesins with a glucan-binding domain, two types of repetitive regions, an isopeptide bond-forming domain associated with shear resistance, and a C-terminal LPXTG motif for anchoring to the cell wall. They occur in oral Streptococci, and tend to be major cell surface adhesins. Members of this family include SspA and SspB from Streptococcus gordonii, antigen I/II from S. mutans, etc.


Pssm-ID: 411384 [Multi-domain]  Cd Length: 1552  Bit Score: 59.95  E-value: 1.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1529 KDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATED------------------AKLRLEVNMQAMKAQFERDLQ 1590
Cdd:NF033804   133 KSDYAKQAEEIKKTTEAYKKEVAAHQAETDKINAENKAAKDkyqkdlkahqaevekintANATAKAEYEAKLAQYQKDLA 212
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1591 TRDEQNEEKKRLLIKQVRELEAELEdeRKQRALAVAsKKKMEIDLKDLEAQiEAANKARDEVIKQLRK-----LQAQMKD 1665
Cdd:NF033804   213 AVQKANEDSQADYQNKLSAYQTELA--RVQKANAEA-KEAYDKAVKENTAK-NAALQAENEAIKQRNEtakanYEAAMKQ 288
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1666 YQRELEEARASRDEIFAqskESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEITNSASG-KSALLDEKRRLE 1744
Cdd:NF033804   289 YEADLAAIKKAKEDNDA---DYQAKLAAYQTELARVQKANADAKAAYEKAVEENTAKNTAIQAENEAiKQRNAAAKATYE 365
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1745 ARIAQLEEELEEEQSNMELlNDRFRKTTLQvdTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKAT 1824
Cdd:NF033804   366 AALKQYEADLAAVKKANAA-NEADYQAKLA--AYQTELARVQKANADAKAAYEKAVEDNKAKNAALQAENEAIKQRNAAA 442
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034599857 1825 ISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQ 1876
Cdd:NF033804   443 KADYEAKLAKYQADLAKYKKDLAEYPAKLKAYEDEQAKIKAALAELEKKKNE 494
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
1540-1852 5.47e-08

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 411490 [Multi-domain]  Cd Length: 660  Bit Score: 58.00  E-value: 5.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1540 EKSKRALEQQVEEMRTQLEELEDELQATEDaklrlevnmqamKAQFERDL-QTRDEQNEEKKRLLIKQVRELEAELEDER 1618
Cdd:NF033930    54 EAAKKAYEEAKKKAEDAQKKYDEDQKKTEE------------KAKKEKKAsEEEQKANLAVQKAYVKYRKAQRRKKSDYK 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1619 KQRALAvasKKKMEIDLKDLEAQIEAANKARDEVI---KQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLE 1695
Cdd:NF033930   122 KKLAEA---DKKIDEAKKKQKEAKAEFNKVRAKVVpeaEELAETKKKAEEAKAEEPVAKKKVDEAKKKVEEAKKKVEAEE 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1696 AEILQLQEELASSERARRHAEQERDELADE---ITNSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTT 1772
Cdd:NF033930   199 AEIEKLQNEEVALEAKIAELENQVDNLEKElaeIDESDSEDYIKEGLRAPLESELDAKQAKLAKKQTELEKLLDSLDPEG 278
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1773 LQVDTLNAElAAERSAAQKSDNARQQLERQNKELKaKLQELEGAVKSKFKAtisALEAKIGQLEEQLEQEAKE-RAAANK 1851
Cdd:NF033930   279 KTQDELDKE-AAEEELSKKIDELDNEVAKLEKEVS-DLENSDNNVADYYKE---ALEKDLATKKAELEKTQKDlDKALNE 353

                   .
gi 1034599857 1852 L 1852
Cdd:NF033930   354 L 354
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
861-1140 1.37e-07

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 411490 [Multi-domain]  Cd Length: 660  Bit Score: 56.46  E-value: 1.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  861 EELQAKDEELLKVKEKQTKVEGELEEMERKHQQ-----------LLEEKNILAEQLQAETELFAEAEEMRARLAAKKQEL 929
Cdd:NF033930   108 KYRKAQRRKKSDYKKKLAEADKKIDEAKKKQKEakaefnkvrakVVPEAEELAETKKKAEEAKAEEPVAKKKVDEAKKKV 187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  930 EEIlhdlESRVEEEEERNQILQNEKKKMQAHIQdleeqldeeegarqklqlekvTAEAKIKKMEEEILLLEDQNSKFIKE 1009
Cdd:NF033930   188 EEA----KKKVEAEEAEIEKLQNEEVALEAKIA---------------------ELENQVDNLEKELAEIDESDSEDYIK 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1010 KKLMEDRIAECSSQLAEEEEKAKNLAKirnkqevmisdLEERLKKEEKTRQELEK--AKRKLDGETTDLQDQIAELQAQI 1087
Cdd:NF033930   243 EGLRAPLESELDAKQAKLAKKQTELEK-----------LLDSLDPEGKTQDELDKeaAEEELSKKIDELDNEVAKLEKEV 311
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034599857 1088 DELKLQLAKKEEELQGALARgdDETLHKNNALKVVRELQAQIAELQEDFESEK 1140
Cdd:NF033930   312 SDLENSDNNVADYYKEALEK--DLATKKAELEKTQKDLDKALNELGPDGDEEE 362
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
1367-1705 1.47e-07

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 411490 [Multi-domain]  Cd Length: 660  Bit Score: 56.46  E-value: 1.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1367 ARKNLEKQvlalQSQLADTKKKVDDDLGTIESLEEAKKKLLKDAEALSQRLEEKALAYDKLEKTKNRLQQEldDLTVDLD 1446
Cdd:NF033930    56 AKKAYEEA----KKKAEDAQKKYDEDQKKTEEKAKKEKKASEEEQKANLAVQKAYVKYRKAQRRKKSDYKK--KLAEADK 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1447 HQRQVASNLEKKQKKFDQLLA------EEKSISARYAEERDRAEAEAREKETKAlslaraleealeAKEEFERQNKQLRA 1520
Cdd:NF033930   130 KIDEAKKKQKEAKAEFNKVRAkvvpeaEELAETKKKAEEAKAEEPVAKKKVDEA------------KKKVEEAKKKVEAE 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1521 DMEdlmsskddvgknVHELEKSKRALEQQVEEMRTQLEELEDELqatedAKLRLEVNMQAMKAQFERDLQtrdeqneekK 1600
Cdd:NF033930   198 EAE------------IEKLQNEEVALEAKIAELENQVDNLEKEL-----AEIDESDSEDYIKEGLRAPLE---------S 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1601 RLLIKQVRELEAELEDERKQRALAVASKKKMEIdlkDLEAQIEAANKARDEvikqlrkLQAQMKDYQRELEEARASRDEI 1680
Cdd:NF033930   252 ELDAKQAKLAKKQTELEKLLDSLDPEGKTQDEL---DKEAAEEELSKKIDE-------LDNEVAKLEKEVSDLENSDNNV 321
                          330       340
                   ....*....|....*....|....*.
gi 1034599857 1681 FAQSKES-EKKLKSLEAEILQLQEEL 1705
Cdd:NF033930   322 ADYYKEAlEKDLATKKAELEKTQKDL 347
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
1625-1937 2.83e-07

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 411490 [Multi-domain]  Cd Length: 660  Bit Score: 55.69  E-value: 2.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1625 VASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEarasrdeifaQSKESEKKLKSLEAEILQLQEE 1704
Cdd:NF033930    36 VASQSKAEKDYDAAVKKSEAAKKAYEEAKKKAEDAQKKYDEDQKKTEE----------KAKKEKKASEEEQKANLAVQKA 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1705 LASSERARRHAEQERDELADEItnsasgKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKttlqvdtlnAELAA 1784
Cdd:NF033930   106 YVKYRKAQRRKKSDYKKKLAEA------DKKIDEAKKKQKEAKAEFNKVRAKVVPEAEELAETKKK---------AEEAK 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1785 --ERSAAQKSDNARQQLERQNKELKAKLQELEgavksKFKATISALEAKIGQLEEQleqeakeraaanklVRRTEKKLKE 1862
Cdd:NF033930   171 aeEPVAKKKVDEAKKKVEEAKKKVEAEEAEIE-----KLQNEEVALEAKIAELENQ--------------VDNLEKELAE 231
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034599857 1863 IfmqveDERRHADQYKEQMEK-ANARMKQLKRQLEEAEEEATRANAS---RRKLQRELDDATEANEgLSREVSTLKNRL 1937
Cdd:NF033930   232 I-----DESDSEDYIKEGLRApLESELDAKQAKLAKKQTELEKLLDSldpEGKTQDELDKEAAEEE-LSKKIDELDNEV 304
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
1284-1617 1.09e-06

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 411490 [Multi-domain]  Cd Length: 660  Bit Score: 53.76  E-value: 1.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1284 RVELAEKASKLQNELD---------NVSTLLEEAEKKGI----KFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQL 1350
Cdd:NF033930    30 RAEEAPVASQSKAEKDydaavkkseAAKKAYEEAKKKAEdaqkKYDEDQKKTEEKAKKEKKASEEEQKANLAVQKAYVKY 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1351 EEEKNSLQEQQEEEeeaRKNLEKQ---------------------VLALQSQLADTKKKVDDdlgTIESLEEAKKKL--- 1406
Cdd:NF033930   110 RKAQRRKKSDYKKK---LAEADKKideakkkqkeakaefnkvrakVVPEAEELAETKKKAEE---AKAEEPVAKKKVdea 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1407 LKDAEALSQRLEEKALAYDKLEKTKNRLQQELDDLtvdldhQRQVAsNLEKKQKKFDqllaeeKSISARYAEERDRAEAE 1486
Cdd:NF033930   184 KKKVEEAKKKVEAEEAEIEKLQNEEVALEAKIAEL------ENQVD-NLEKELAEID------ESDSEDYIKEGLRAPLE 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1487 ArEKETKALSLARAleealeakeeferqnkqlRADMEDLMSSKDDVGKNVHELEK--SKRALEQQVEEMRTQLEELEDEL 1564
Cdd:NF033930   251 S-ELDAKQAKLAKK------------------QTELEKLLDSLDPEGKTQDELDKeaAEEELSKKIDELDNEVAKLEKEV 311
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034599857 1565 qatEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLIKQVRELEAELEDE 1617
Cdd:NF033930   312 ---SDLENSDNNVADYYKEALEKDLATKKAELEKTQKDLDKALNELGPDGDEE 361
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
1607-1889 2.16e-06

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 411490 [Multi-domain]  Cd Length: 660  Bit Score: 52.61  E-value: 2.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1607 VRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEV-----------IKQLRKLQAQMKDYQRELEEARA 1675
Cdd:NF033930    50 VKKSEAAKKAYEEAKKKAEDAQKKYDEDQKKTEEKAKKEKKASEEEqkanlavqkayVKYRKAQRRKKSDYKKKLAEADK 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1676 SRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEitnSASGKSALLDEKRRLEARIAQLEEELE 1755
Cdd:NF033930   130 KIDEAKKKQKEAKAEFNKVRAKVVPEAEELAETKKKAEEAKAEEPVAKKK---VDEAKKKVEEAKKKVEAEEAEIEKLQN 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1756 EEQSnmelLNDRFRKTTLQVDTLNAELaAERSAAQKSDNARQQLERQ-NKELKAKLQELegAVKSKFKATISALEAKIGQ 1834
Cdd:NF033930   207 EEVA----LEAKIAELENQVDNLEKEL-AEIDESDSEDYIKEGLRAPlESELDAKQAKL--AKKQTELEKLLDSLDPEGK 279
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034599857 1835 LEEQLEQEAKErAAANKLVRRTEKKLKEIFMQVED----ERRHADQYKEQMEKANARMK 1889
Cdd:NF033930   280 TQDELDKEAAE-EELSKKIDELDNEVAKLEKEVSDlensDNNVADYYKEALEKDLATKK 337
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
1080-1336 8.21e-06

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: 380155 [Multi-domain]  Cd Length: 1848  Bit Score: 51.37  E-value: 8.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1080 IAELQAQIDELKLQlAKKEEELQGALArgdDETLHKNNALKVVRELQAQIAEL---QEDFES--EKASRNKAEKQKRDLS 1154
Cdd:NF012221  1537 TSESSQQADAVSKH-AKQDDAAQNALA---DKERAEADRQRLEQEKQQQLAAIsgsQSQLEStdQNALETNGQAQRDAIL 1612
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1155 EELEALKTELE------DTLDTTAAQQELRTK--REQEVAELKKALEEE---TKNH-EAQIQDMRQRHATALEELSEQLE 1222
Cdd:NF012221  1613 EESRAVTKELTtlaqglDALDSQATYAGESGDqwRNPFAGGLLDRVQEQlddAKKIsGKQLADAKQRHVDNQQKVKDAVA 1692
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1223 QAKRFKANLEKNKQGLETDNKelacevkvlqqvKAESEHKRKKLDAQVQELHAKVSEGDrlrvelaekasklqneldnVS 1302
Cdd:NF012221  1693 KSEAGVAQGEQNQANAEQDID------------DAKADAEKRKDDALAKQNEAQQAESD-------------------AN 1741
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1034599857 1303 TLLEEAEKKGIKFAKDAASLESQLQ-DTQELLQEE 1336
Cdd:NF012221  1742 AAANDAQSRGEQDASAAENKANQAQaDAKGAKQDE 1776
Streccoc_I_II NF033804
antigen I/II family LPXTG-anchored adhesin; Members of the antigen I/II family are adhesins ...
1370-1727 2.40e-05

antigen I/II family LPXTG-anchored adhesin; Members of the antigen I/II family are adhesins with a glucan-binding domain, two types of repetitive regions, an isopeptide bond-forming domain associated with shear resistance, and a C-terminal LPXTG motif for anchoring to the cell wall. They occur in oral Streptococci, and tend to be major cell surface adhesins. Members of this family include SspA and SspB from Streptococcus gordonii, antigen I/II from S. mutans, etc.


Pssm-ID: 411384 [Multi-domain]  Cd Length: 1552  Bit Score: 49.55  E-value: 2.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1370 NLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDAEALSQRLEEkalaydkLEKTKNrlqqelddltvdlDHQR 1449
Cdd:NF033804    93 DLDKAVKDAKSAGVNVVQDETVDKGTATTATENAQKQTEIKSDYAKQAEE-------IKKTTE-------------AYKK 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1450 QVASNlekkQKKFDQLLAEEKSISARYAEERDRAEAEArEKETKALSLARALEEALEAKEEF-----ERQNKQLRADMED 1524
Cdd:NF033804   153 EVAAH----QAETDKINAENKAAKDKYQKDLKAHQAEV-EKINTANATAKAEYEAKLAQYQKdlaavQKANEDSQADYQN 227
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1525 LMSSKDDVGKNVHELE-KSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLL 1603
Cdd:NF033804   228 KLSAYQTELARVQKANaEAKEAYDKAVKENTAKNAALQAENEAIKQRNETAKANYEAAMKQYEADLAAIKKAKEDNDADY 307
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1604 IKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKA---RDEVIKQlrKLQAQMKDYQRELEEARASRDei 1680
Cdd:NF033804   308 QAKLAAYQTELARVQKANADAKAAYEKAVEENTAKNTAIQAENEAikqRNAAAKA--TYEAALKQYEADLAAVKKANA-- 383
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1034599857 1681 fAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIT 1727
Cdd:NF033804   384 -ANEADYQAKLAAYQTELARVQKANADAKAAYEKAVEDNKAKNAALQ 429
dapto_LiaX NF038025
daptomycin-sensing surface protein LiaX; LiaX (lipid-II###interacting antibiotics X), as ...
1028-1172 1.83e-04

daptomycin-sensing surface protein LiaX; LiaX (lipid-II###interacting antibiotics X), as described in Enterococcus faecalis, is expressed under control of the the LiaR response regulator, and is involved in the process of resistance to daptomycin and to antimicrobial peptides of the innate immune response.


Pssm-ID: 411618  Cd Length: 513  Bit Score: 46.16  E-value: 1.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1028 EEKAKNLAKIRNKQEVMISDLEERlkKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIDELKLQLAKKEEELQ----- 1102
Cdd:NF038025    46 AEKDDLLDELENEQEEEPETFTEQ--KEEEDKEDLEAILDELATEANKASAELDEVNAEIQGVKEEIKEKQEQLMvldtk 123
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034599857 1103 ---GALargDDETLHKNNALKV-VRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTA 1172
Cdd:NF038025   124 eelDEL---SEEELAERQELEAeIKQLEAQLDELEEEKEELEEELKTIRKDQWSQTKEKISEKFDIPDDWKEQA 194
BREX_BrxC NF033441
BREX system P-loop protein BrxC; BrxC is a P-loop-containing protein, and probable ATPase, ...
1014-1253 2.21e-04

BREX system P-loop protein BrxC; BrxC is a P-loop-containing protein, and probable ATPase, from BREX (bacteriophage exclusion) systems of type 1.


Pssm-ID: 380283  Cd Length: 1173  Bit Score: 46.42  E-value: 2.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1014 EDRIAECSSQLAEEE-EKAKNLAKIRNK--------QEVMISDLEE--RLKKEEKTRQELEKAKRKLDGETTDLQDQIAE 1082
Cdd:NF033441   892 EDALAKEIREKFPELlEELKALAGRYQAggypgpdpLEPALALLEEilSIKDNEEFLKALNKKEDDLLDLIEDWEDVKSF 971
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1083 LQ-AQIDELKlQLAKKEEELQGALARGDDETLhkNNALKVVRELQA------QIAELQEDFES-EKASRNKAEKQKRDLS 1154
Cdd:NF033441   972 FEgDQLPIWD-RALRLLKEYEDNLDYELDEEA--EEAIEELRSILAdpdpysRIPDLPPLLEAlREALREALEELREAAL 1048
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1155 EELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEEETKnhEAQIQDMRQRHATA-LEELSEQLEQAKRFKANLEK 1233
Cdd:NF033441  1049 EAIEEAKAELEADLEWQELSDEQQNRLLAPFDELKERIEPEVS--IASLRALLDQLADAlLDRLLDRIEALIQRFQEEKA 1126
                          250       260
                   ....*....|....*....|
gi 1034599857 1234 NKQGLETDNKELACEVKVLQ 1253
Cdd:NF033441  1127 EPEVKEAAAEPPEPKVKTVS 1146
Streccoc_I_II NF033804
antigen I/II family LPXTG-anchored adhesin; Members of the antigen I/II family are adhesins ...
1049-1456 2.24e-04

antigen I/II family LPXTG-anchored adhesin; Members of the antigen I/II family are adhesins with a glucan-binding domain, two types of repetitive regions, an isopeptide bond-forming domain associated with shear resistance, and a C-terminal LPXTG motif for anchoring to the cell wall. They occur in oral Streptococci, and tend to be major cell surface adhesins. Members of this family include SspA and SspB from Streptococcus gordonii, antigen I/II from S. mutans, etc.


Pssm-ID: 411384 [Multi-domain]  Cd Length: 1552  Bit Score: 46.47  E-value: 2.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1049 EERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIDELKLQLAKKEEELQGALARGDDETLHKNNALKVVR-ELQA 1127
Cdd:NF033804   123 TENAQKQTEIKSDYAKQAEEIKKTTEAYKKEVAAHQAETDKINAENKAAKDKYQKDLKAHQAEVEKINTANATAKaEYEA 202
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1128 QIAELQEDFESEKASRNKAEKqkrDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEEETKNHEAQIQDMR 1207
Cdd:NF033804   203 KLAQYQKDLAAVQKANEDSQA---DYQNKLSAYQTELARVQKANAEAKEAYDKAVKENTAKNAALQAENEAIKQRNETAK 279
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1208 QRHATALEELSEQLEQAKRFKANLEKNKQG-LETDNKELACEVKVLQQVKA-------ESEHKRKKLDAQVQ-------- 1271
Cdd:NF033804   280 ANYEAAMKQYEADLAAIKKAKEDNDADYQAkLAAYQTELARVQKANADAKAayekaveENTAKNTAIQAENEaikqrnaa 359
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1272 -----ELHAKVSEGDRLRVELA---------EKASKLQNELDNVSTLLEEAEKKGIKFAKDAASLESQLQ-DTQELLQEE 1336
Cdd:NF033804   360 akatyEAALKQYEADLAAVKKAnaaneadyqAKLAAYQTELARVQKANADAKAAYEKAVEDNKAKNAALQaENEAIKQRN 439
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1337 TRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIE---------SLEEAKKKLL 1407
Cdd:NF033804   440 AAAKADYEAKLAKYQADLAKYKKDLAEYPAKLKAYEDEQAKIKAALAELEKKKNEDGYLSEpsaqslvydSEPNAQLSLT 519
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1408 KDAEALSQRLEEKALAYDKLEKTKNRLQqeLDDLTV-DLDHQRQVASNLE 1456
Cdd:NF033804   520 TDGKLLKASAVDEAFKKDTAQYGKKNLQ--LDNLNVtNLEQADATTSSVE 567
dapto_LiaX NF038025
daptomycin-sensing surface protein LiaX; LiaX (lipid-II###interacting antibiotics X), as ...
1567-1733 2.26e-04

daptomycin-sensing surface protein LiaX; LiaX (lipid-II###interacting antibiotics X), as described in Enterococcus faecalis, is expressed under control of the the LiaR response regulator, and is involved in the process of resistance to daptomycin and to antimicrobial peptides of the innate immune response.


Pssm-ID: 411618  Cd Length: 513  Bit Score: 46.16  E-value: 2.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1567 TEDAKLRLEvNMqAMKAQFERDLQTRDEQNEEKKRLLikQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAAN 1646
Cdd:NF038025    18 TEEALDLLE-NM-AKEKDEKQIKKAADEVTAEKDDLL--DELENEQEEEPETFTEQKEEEDKEDLEAILDELATEANKAS 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1647 KARDEVIKQLRKLQAQMKDYQREL-------------EEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARR 1713
Cdd:NF038025    94 AELDEVNAEIQGVKEEIKEKQEQLmvldtkeeldelsEEELAERQELEAEIKQLEAQLDELEEEKEELEEELKTIRKDQW 173
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1034599857 1714 HAEQER-----------DELADEITNSASGK 1733
Cdd:NF038025   174 SQTKEKisekfdipddwKEQATETLNQVGEK 204
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
1541-1886 2.47e-04

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 411407 [Multi-domain]  Cd Length: 684  Bit Score: 46.16  E-value: 2.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1541 KSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEvnMQAMKAQFERDLQTRDEQNEEKkrLLIKQVRELEAELEDERKQ 1620
Cdd:NF033838    58 EHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKK--LSDIKTEYLYELNVLKEKSEAE--LTSKTKKELDAAFEQFKKD 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1621 -----RALAVASKKKMEIDlKDLEAQIEAANKARDEVIKQLRKLQ-----AQMKDYQREL--EEARASRDEifAQSKESE 1688
Cdd:NF033838   134 tlepgKKVAEATKKVEEAE-KKAKDQKEEDRRNYPTNTYKTLELEiaesdVEVKKAELELvkEEAKEPRDE--EKIKQAK 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1689 KKLKSLEAEILQLQEELASSERARRHAEQERDELADEITNSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRF 1768
Cdd:NF033838   211 AKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKENDAKSSDSSV 290
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1769 RKTTLQVDTLN-----AELAAERSAAQKSDNARQQLERQN------KELKAKLQELEGAVKS------KFKATISALEAK 1831
Cdd:NF033838   291 GEETLPSPSLKpekkvAEAEKKVEEAKKKAKDQKEEDRRNyptntyKTLELEIAESDVKVKEaelelvKEEAKEPRNEEK 370
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034599857 1832 IGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANA 1886
Cdd:NF033838   371 IKQAKAKVESKKAEATRLEKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPA 425
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
1086-1497 3.59e-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: 380155 [Multi-domain]  Cd Length: 1848  Bit Score: 45.98  E-value: 3.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1086 QIDELKLQLAKKeeeLQGALARGDDETLHK-NNALKVVRELQAQIAE---LQEDFESEKASRNKAEKQKRDLS------- 1154
Cdd:NF012221  1355 EIDEVGSDLGDS---LTGSVTQVETPDLNAmQNALNIDESVLSTQAPnliVNGDFEQGAEGWNSTYGVEASHSasvyglr 1431
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1155 -EELEALKTELeDTLDTTAAQQELRTKREQEVAELKKALEEE---TKNHEAQIQDMRQRHATALEELSEQLEQAKRFKAN 1230
Cdd:NF012221  1432 aEGHGARVSEL-DTYTNTSLYQDLSNLTAGEVIALSFDFARRaglSTNNGIEVLWNGEVVFASSGDASAWQQKTLKLTAK 1510
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1231 LEKNK---------QGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVElAEKasklQNELDNV 1301
Cdd:NF012221  1511 AGSNRlefkgtghnDGLGYILDNVVATSESSQQADAVSKHAKQDDAAQNALADKERAEADRQRLE-QEK----QQQLAAI 1585
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1302 STLLEEAEkkgikfAKDAASLESQLQDTQELLQEE----TRQKLNLSSRIRQLEEEKNS----------------LQEQQ 1361
Cdd:NF012221  1586 SGSQSQLE------STDQNALETNGQAQRDAILEEsravTKELTTLAQGLDALDSQATYagesgdqwrnpfagglLDRVQ 1659
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1362 EEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDAEALSQRLEEKA-LAYDKLEKTKNRLQQELDD 1440
Cdd:NF012221  1660 EQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAeKRKDDALAKQNEAQQAESD 1739
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034599857 1441 LTVDL-------DHQRQVASNlekkqkKFDQLLAEEKSISARYAEERDRAEAEAREKETKALSL 1497
Cdd:NF012221  1740 ANAAAndaqsrgEQDASAAEN------KANQAQADAKGAKQDESDKPNRQGAAGSGLSGKAYSV 1797
BREX_BrxC NF033441
BREX system P-loop protein BrxC; BrxC is a P-loop-containing protein, and probable ATPase, ...
1286-1499 1.01e-03

BREX system P-loop protein BrxC; BrxC is a P-loop-containing protein, and probable ATPase, from BREX (bacteriophage exclusion) systems of type 1.


Pssm-ID: 380283  Cd Length: 1173  Bit Score: 44.11  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1286 ELAEKASKLQ----NELDNVSTLLEE--AEKKGIKFAKDAASLESQLQDTQELLQEeTRQKLNlSSRIRQLEEEKNSLQE 1359
Cdd:NF033441   912 ALAGRYQAGGypgpDPLEPALALLEEilSIKDNEEFLKALNKKEDDLLDLIEDWED-VKSFFE-GDQLPIWDRALRLLKE 989
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1360 -QQEEEEEARKNLEKQVLALQSQLADTK-----KKVDDDLGTIES-----LEEAKKKLLKDAEALSQRLEEKALAYDKLE 1428
Cdd:NF033441   990 yEDNLDYELDEEAEEAIEELRSILADPDpysriPDLPPLLEALREalreaLEELREAALEAIEEAKAELEADLEWQELSD 1069
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1429 KTKNRLQQELDDLTVDLDHQRQVASNLEKKQKKFDQLLAEEKSISARYAEERDR---------AEAEAREKETKALSLAR 1499
Cdd:NF033441  1070 EQQNRLLAPFDELKERIEPEVSIASLRALLDQLADALLDRLLDRIEALIQRFQEekaepevkeAAAEPPEPKVKTVSLPR 1149
dapto_LiaX NF038025
daptomycin-sensing surface protein LiaX; LiaX (lipid-II###interacting antibiotics X), as ...
1670-1846 1.32e-03

daptomycin-sensing surface protein LiaX; LiaX (lipid-II###interacting antibiotics X), as described in Enterococcus faecalis, is expressed under control of the the LiaR response regulator, and is involved in the process of resistance to daptomycin and to antimicrobial peptides of the innate immune response.


Pssm-ID: 411618  Cd Length: 513  Bit Score: 43.46  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1670 LEEARASRDEifAQSKESEKKLKSLEAEILQLQE---ELASSERARRHAEQERDELA---DEITNSASGKSALLDEkrrL 1743
Cdd:NF038025    25 LENMAKEKDE--KQIKKAADEVTAEKDDLLDELEneqEEEPETFTEQKEEEDKEDLEailDELATEANKASAELDE---V 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1744 EARIAQLEEELEEEQSNMELLNdrfrkTTLQVDTLNAELAAERsaaqksdnarQQLERQNKELKAKLQELEGAVkskfka 1823
Cdd:NF038025   100 NAEIQGVKEEIKEKQEQLMVLD-----TKEELDELSEEELAER----------QELEAEIKQLEAQLDELEEEK------ 158
                          170       180
                   ....*....|....*....|...
gi 1034599857 1824 tiSALEAKIGQLEEQLEQEAKER 1846
Cdd:NF038025   159 --EELEEELKTIRKDQWSQTKEK 179
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
860-1200 2.53e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 411407 [Multi-domain]  Cd Length: 684  Bit Score: 42.69  E-value: 2.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  860 EEELQAKDEELLKV--KEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETelfaeAEEMRARLAAKKQELEEILHDLE 937
Cdd:NF033838    64 ESHLEKILSEIQKSldKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAEL-----TSKTKKELDAAFEQFKKDTLEPG 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  938 SRVEEEEERnqiLQNEKKKMQAHiqDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEIL---LLEDQNSKFIKEKKL-M 1013
Cdd:NF033838   139 KKVAEATKK---VEEAEKKAKDQ--KEEDRRNYPTNTYKTLELEIAESDVEVKKAELELVkeeAKEPRDEEKIKQAKAkV 213
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1014 EDRIAECSS--------QLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQEL-EKA---KRKLDGETTDLQ--DQ 1079
Cdd:NF033838   214 ESKKAEATRlekiktdrEKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLgEPAtpdKKENDAKSSDSSvgEE 293
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1080 IAELQAQIDELKLQLAKKEEELQGALARGDDETLHKNNALKVVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEA 1159
Cdd:NF033838   294 TLPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRRNYPTNTYKTLELEIAESDVKVKEAELELVKEEAKEPRNEEKIKQ 373
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1034599857 1160 LKTELEDTLDTTAAQQELRTKREQEVAELKKALEEETKNHE 1200
Cdd:NF033838   374 AKAKVESKKAEATRLEKIKTDRKKAEEEAKRKAAEEDKVKE 414
dapto_LiaX NF038025
daptomycin-sensing surface protein LiaX; LiaX (lipid-II###interacting antibiotics X), as ...
1105-1235 7.52e-03

daptomycin-sensing surface protein LiaX; LiaX (lipid-II###interacting antibiotics X), as described in Enterococcus faecalis, is expressed under control of the the LiaR response regulator, and is involved in the process of resistance to daptomycin and to antimicrobial peptides of the innate immune response.


Pssm-ID: 411618  Cd Length: 513  Bit Score: 41.15  E-value: 7.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1105 LARGDDETLHKNNALKVVRELQAQIAELQEDFESEKAS--RNKAEKQKRDLSEELEALKTELEDT---LDTTAAQ----- 1174
Cdd:NF038025    28 MAKEKDEKQIKKAADEVTAEKDDLLDELENEQEEEPETftEQKEEEDKEDLEAILDELATEANKAsaeLDEVNAEiqgvk 107
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034599857 1175 QELRTKREQ---------------EVAELKKALEEETKNHEAQIQDMRQRHatalEELSEQLEQAKRFKANLEKNK 1235
Cdd:NF038025   108 EEIKEKQEQlmvldtkeeldelseEELAERQELEAEIKQLEAQLDELEEEK----EELEEELKTIRKDQWSQTKEK 179
Streccoc_I_II NF033804
antigen I/II family LPXTG-anchored adhesin; Members of the antigen I/II family are adhesins ...
1110-1464 8.01e-03

antigen I/II family LPXTG-anchored adhesin; Members of the antigen I/II family are adhesins with a glucan-binding domain, two types of repetitive regions, an isopeptide bond-forming domain associated with shear resistance, and a C-terminal LPXTG motif for anchoring to the cell wall. They occur in oral Streptococci, and tend to be major cell surface adhesins. Members of this family include SspA and SspB from Streptococcus gordonii, antigen I/II from S. mutans, etc.


Pssm-ID: 411384 [Multi-domain]  Cd Length: 1552  Bit Score: 41.46  E-value: 8.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1110 DETLHKNNALKVVRELQAQiAELQEDFEsekasrnkaeKQKRDLSEELEALKTELedtldttAAQQELRTKREQEVAELK 1189
Cdd:NF033804   111 DETVDKGTATTATENAQKQ-TEIKSDYA----------KQAEEIKKTTEAYKKEV-------AAHQAETDKINAENKAAK 172
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1190 KALEEETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEK--------------------------NKQGLETDNK 1243
Cdd:NF033804   173 DKYQKDLKAHQAEVEKINTANATAKAEYEAKLAQYQKDLAAVQKanedsqadyqnklsayqtelarvqkaNAEAKEAYDK 252
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1244 ELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVS--EGDRLRVELAE---------KASKLQNELDNVSTLLEEAEKKG 1312
Cdd:NF033804   253 AVKENTAKNAALQAENEAIKQRNETAKANYEAAMKqyEADLAAIKKAKedndadyqaKLAAYQTELARVQKANADAKAAY 332
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1313 IKFAKDAASLESQLQDTQELLQEETRQ-KLNLSSRIRQLEEEknsLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDD 1391
Cdd:NF033804   333 EKAVEENTAKNTAIQAENEAIKQRNAAaKATYEAALKQYEAD---LAAVKKANAANEADYQAKLAAYQTELARVQKANAD 409
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1392 DLGTIE-SLEEAKKK---LLKDAEALSQRLEEKALAYD-KLEKTKNRL---QQELDDLTVDL----DHQRQVASNLEKKQ 1459
Cdd:NF033804   410 AKAAYEkAVEDNKAKnaaLQAENEAIKQRNAAAKADYEaKLAKYQADLakyKKDLAEYPAKLkayeDEQAKIKAALAELE 489

                   ....*
gi 1034599857 1460 KKFDQ 1464
Cdd:NF033804   490 KKKNE 494
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
1032-1387 8.10e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 411407 [Multi-domain]  Cd Length: 684  Bit Score: 41.15  E-value: 8.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1032 KNLAKIRNKQEVMISDLEERLKKE--EKTRQELEKAKRKLDGETTDLQDQIAELQAQIDElklqlAKKEEELQgalargd 1109
Cdd:NF033838    91 KKLSDIKTEYLYELNVLKEKSEAEltSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEE-----AEKKAKDQ------- 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1110 DETLHKNNALKVVRELQAQIAElqEDFESEKASRN--KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAE 1187
Cdd:NF033838   159 KEEDRRNYPTNTYKTLELEIAE--SDVEVKKAELElvKEEAKEPRDEEKIKQAKAKVESKKAEATRLEKIKTDREKAEEE 236
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1188 LK-----KALEEETKNHEAQIQDMRQRHAT--ALEELSEqlEQAKRFKANLEKNKQGLET--------DNKELACEVKVL 1252
Cdd:NF033838   237 AKrradaKLKEAVEKNVATSEQDKPKRRAKrgVLGEPAT--PDKKENDAKSSDSSVGEETlpspslkpEKKVAEAEKKVE 314
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1253 QQVKA----ESEHKR-------KKLDAQVQELHAKVSEGDrlrVELA-EKASKLQNElDNVSTLLEEAEKKgikfaKDAA 1320
Cdd:NF033838   315 EAKKKakdqKEEDRRnyptntyKTLELEIAESDVKVKEAE---LELVkEEAKEPRNE-EKIKQAKAKVESK-----KAEA 385
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1321 SLESQLQDTQELLQEETRQKLNLSSRIRQLEEEK-------------------------NSLQEQQEEEEEARKNLEKQV 1375
Cdd:NF033838   386 TRLEKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQpqpapapqpekpapkpekpaeqpkaEKPADQQAEEDYARRSEEEYN 465
                          410
                   ....*....|..
gi 1034599857 1376 LALQSQLADTKK 1387
Cdd:NF033838   466 RLTQQQPPKTEK 477
 
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 ...
857-1937 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: 396244 [Multi-domain]  Cd Length: 1081  Bit Score: 1488.51  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  857 TRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDL 936
Cdd:pfam01576    1 TRQEEEMQAKEEELQKVKEKQQKAESELKELEKKHQQLIEEKNILAEQLQAETELFAEAEEMRARLAARKQELEEILHDL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  937 ESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFIKEKKLMEDR 1016
Cdd:pfam01576   81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLEEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1017 IAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIDELKLQLAK 1096
Cdd:pfam01576  161 ISEFTSNLAEEEEKVKSLNKLKNKHEAMISDLEDRLKKEEKGRQELEKAKRKLDGESTDLQEQIAELQAQIEELRAQLAK 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1097 KEEELQGALARGDDETLHKNNALKVVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQE 1176
Cdd:pfam01576  241 KEEELQAALARLEEEGAQKNNALKKLRELQAQIAELQEDLESERAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQE 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1177 LRTKREQEVAELKKALEEETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVK 1256
Cdd:pfam01576  321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELSEQLEQAKRNKANLEKAKQALESENNELQAELKTLQQAK 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1257 AESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKASKLQNELDNVSTLLEEAEKKGIKFAKDAASLESQLQDTQELLQEE 1336
Cdd:pfam01576  401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSGLLSEAEGKSIKLSKDVSSLESQLQDTQELLQEE 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1337 TRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDAEALSQR 1416
Cdd:pfam01576  481 TRQKLNLSSRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSEMKKKLEEDAGAVEALEEAKKRLQRELEALTQR 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1417 LEEKALAYDKLEKTKNRLQQELDDLTVDLDHQRQVASNLEKKQKKFDQLLAEEKSISARYAEERDRAEAEAREKETKALS 1496
Cdd:pfam01576  561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1497 LARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEV 1576
Cdd:pfam01576  641 LSRALEEALEAKEELERQNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1577 NMQAMKAQFERDLQTRDEQNEEKKRLLIKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQL 1656
Cdd:pfam01576  721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGRDEAVKQL 800
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1657 RKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEITNSASGKSAL 1736
Cdd:pfam01576  801 KKLQAQMKELQRELEETRASRDEILAQSKESEKKLKSLEAELLQLQEDLAASERAKRQAQQERDELADEIANGASGKSAL 880
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1737 LDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGA 1816
Cdd:pfam01576  881 LDEKRRLEARIAQLEEELEEEQSNTELLNDRYRKLTLQVEQLTTELSAERSFSQKSESARQQLERQNKELKAKLQEMEGT 960
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857 1817 VKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLE 1896
Cdd:pfam01576  961 VKSKYKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRNADQYKDQAEKANSRMKQLKRQLE 1040
                         1050      1060      1070      1080
                   ....*....|....*....|....*....|....*....|.
gi 1034599857 1897 EAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1937
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESAESMNREVSTLRSKL 1081
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
99-780 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  Cd Length: 673  Bit Score: 1443.66  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857   99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14920      1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIpespkpvkhQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 258
Cdd:cd14920     81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNI---------PGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  259 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQET 338
Cdd:cd14920    152 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQET 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  339 MEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQ 418
Cdd:cd14920    232 MEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQ 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  419 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 498
Cdd:cd14920    312 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  499 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQL 578
Cdd:cd14920    392 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQL 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  579 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGM 658
Cdd:cd14920    472 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGM 551
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  659 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 738
Cdd:cd14920    552 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 631
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 1034599857  739 ILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 780
Cdd:cd14920    632 ILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
99-780 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  Cd Length: 662  Bit Score: 1332.10  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857   99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01377      1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNipespkpvKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 258
Cdd:cd01377     81 ESGAGKTENTKKVIQYLASVAASSKKKKESG--------KKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIH 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  259 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYR-FLSNGYIPIPGQQDKDNFQE 337
Cdd:cd01377    153 FGSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVDDAEEFKL 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  338 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 417
Cdd:cd01377    233 TDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWV 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  418 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 497
Cdd:cd01377    313 TKGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFN 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  498 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSK-FQKPR 576
Cdd:cd01377    392 HHMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPK 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  577 QLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRivgldqvtgmtETAFGSAYKTKK 656
Cdd:cd01377    470 PKKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE-----------SGGGGGKKKKKG 538
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  657 GMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 736
Cdd:cd01377    539 GSFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQR 618
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....
gi 1034599857  737 YEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 780
Cdd:cd01377    619 YSILAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
MYSc_Myh18 cd14932
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...
99-780 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  Cd Length: 676  Bit Score: 1236.44  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857   99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14932      1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNipespKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 258
Cdd:cd14932     81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQS-----SIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  259 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQET 338
Cdd:cd14932    156 FDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAET 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  339 MEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQ 418
Cdd:cd14932    236 MEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQ 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  419 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 498
Cdd:cd14932    316 KAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  499 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQL 578
Cdd:cd14932    396 TMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKL 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  579 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGsAYKTKKGM 658
Cdd:cd14932    476 KDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHG-AFKTRKGM 554
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  659 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 738
Cdd:cd14932    555 FRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 634
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 1034599857  739 ILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 780
Cdd:cd14932    635 ILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
MYSc_Myh9 cd14919
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ...
99-780 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  Cd Length: 670  Bit Score: 1208.00  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857   99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14919      1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  179 ESGAGKTENTKKVIQYLAHVASSHKGRKDhnipespkpvkhQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 258
Cdd:cd14919     81 ESGAGKTENTKKVIQYLAHVASSHKSKKD------------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  259 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQET 338
Cdd:cd14919    149 FDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQET 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  339 MEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQ 418
Cdd:cd14919    229 MEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQ 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  419 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 498
Cdd:cd14919    309 KAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNH 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  499 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQL 578
Cdd:cd14919    389 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQL 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  579 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGM 658
Cdd:cd14919    469 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGM 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  659 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 738
Cdd:cd14919    549 FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 628
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 1034599857  739 ILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 780
Cdd:cd14919    629 ILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
MYSc_Myh11 cd14921
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...
99-780 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  Cd Length: 673  Bit Score: 1197.14  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857   99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14921      1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIpespkpvkhQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 258
Cdd:cd14921     81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSI---------TGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  259 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQET 338
Cdd:cd14921    152 FDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQET 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  339 MEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQ 418
Cdd:cd14921    232 LEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQ 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  419 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 498
Cdd:cd14921    312 KAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNH 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  499 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQL 578
Cdd:cd14921    392 TMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQL 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  579 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGM 658
Cdd:cd14921    472 KDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGM 551
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  659 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 738
Cdd:cd14921    552 FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 631
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 1034599857  739 ILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 780
Cdd:cd14921    632 ILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
MYSc_Myh19 cd15896
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ...
99-780 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  Cd Length: 675  Bit Score: 1187.94  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857   99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd15896      1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNipespKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 258
Cdd:cd15896     81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQN-----SLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  259 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQET 338
Cdd:cd15896    156 FDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTET 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  339 MEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQ 418
Cdd:cd15896    236 MEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQ 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  419 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 498
Cdd:cd15896    316 KAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  499 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQL 578
Cdd:cd15896    396 TMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKL 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  579 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTEtaFGSAYKTKKGM 658
Cdd:cd15896    476 KDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSE--MPGAFKTRKGM 553
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  659 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 738
Cdd:cd15896    554 FRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 633
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 1034599857  739 ILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 780
Cdd:cd15896    634 ILTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
MYSc_Myh2_insects_mollusks cd14911
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
99-780 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  Cd Length: 674  Bit Score: 1175.53  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857   99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14911      1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPESPKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 258
Cdd:cd14911     81 ESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  259 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQET 338
Cdd:cd14911    161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  339 MEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQ 418
Cdd:cd14911    241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  419 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 498
Cdd:cd14911    321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  499 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKpRQL 578
Cdd:cd14911    401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TDF 476
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  579 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrIVGLDQVTgMTETAFGSayKTKKGM 658
Cdd:cd14911    477 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQFGA--RTRKGM 552
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  659 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 738
Cdd:cd14911    553 FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE 632
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 1034599857  739 ILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 780
Cdd:cd14911    633 LLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
MYSc_Myh14_mammals cd14930
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ...
99-780 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  Cd Length: 670  Bit Score: 1143.67  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857   99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14930      1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPespkpvkhqGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 258
Cdd:cd14930     81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP---------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  259 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQdKDNFQET 338
Cdd:cd14930    152 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQET 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  339 MEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQ 418
Cdd:cd14930    231 LESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  419 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 498
Cdd:cd14930    311 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  499 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQL 578
Cdd:cd14930    391 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHL 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  579 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSayKTKKGM 658
Cdd:cd14930    471 RDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGG--RPRRGM 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  659 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 738
Cdd:cd14930    549 FRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYE 628
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 1034599857  739 ILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 780
Cdd:cd14930    629 ILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
Myosin_head pfam00063
Myosin head (motor domain);
87-780 0e+00

Myosin head (motor domain);


Pssm-ID: 395017  Cd Length: 674  Bit Score: 1111.58  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857   87 VEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML 166
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  167 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKdhnipespkpvkhQGELERQLLQANPILESFGNAKTVKND 246
Cdd:pfam00063   81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN-------------VGRLEEQILQSNPILEAFGNAKTVRNN 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  247 NSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSN-GYIP 325
Cdd:pfam00063  148 NSSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQsGCYT 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  326 IPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAI 405
Cdd:pfam00063  228 IDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKAL 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  406 LTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCI 485
Cdd:pfam00063  308 CKRRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCI 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  486 NYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQE 565
Cdd:pfam00063  388 NYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYST 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  566 QGSHSKFQKPRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTE 645
Cdd:pfam00063  465 FSKHPHFQKPRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKS 543
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857  646 TafgsAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFP 725
Cdd:pfam00063  544 T----PKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFP 619
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034599857  726 NRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 780
Cdd:pfam00063  620 NRITFQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
80-792 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  Cd Length: 677  Bit Score: 1018.24  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857    80 NPPKFSKVEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISE 159
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857   160 SAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnipespkpvkhQGELERQLLQANPILESFGN 239
Cdd:smart00242   81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTE---------------VGSVEDQILESNPILEAFGN 145
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599857   240 AKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFL 319
Cdd:smart00242  146 AKTLRNNNSSRFGKFIEIHFDAKGKIIGA</